emboss-test 6.4.0-2 / usr / share / EMBOSS / test / data / uniprotft.sw

ID   ANXA5_HUMAN             Reviewed;         320 AA.
AC   P08758; Q6FI16; Q8WV69;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   10-FEB-2009, entry version 116.
DE   RecName: Full=Annexin A5;
DE   AltName: Full=Annexin-5;
DE   AltName: Full=Annexin V;
DE   AltName: Full=Lipocortin V;
DE   AltName: Full=Endonexin II;
DE   AltName: Full=Calphobindin I;
DE            Short=CBP-I;
DE   AltName: Full=Placental anticoagulant protein I;
DE            Short=PAP-I;
DE   AltName: Full=Placental anticoagulant protein 4;
DE            Short=PP4;
DE   AltName: Full=Thromboplastin inhibitor;
DE   AltName: Full=Vascular anticoagulant-alpha;
DE            Short=VAC-alpha;
DE   AltName: Full=Anchorin CII;
GN   Name=ANXA5; Synonyms=ANX5, ENX2, PP4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88163463; PubMed=2964863; DOI=10.1021/bi00399a011;
RA   Funakoshi T., Hendrickson L.E., McMullen B.A., Fujikawa K.;
RT   "Primary structure of human placental anticoagulant protein.";
RL   Biochemistry 26:8087-8092(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-320.
RX   MEDLINE=88139278; PubMed=2963810;
RA   Iwasaki A., Suda M., Nakao H., Nagoya T., Saino Y., Arai K.,
RA   Mizoguchi T., Sato F., Yoshizaki H., Hirata M., Miyata T., Shidara Y.,
RA   Murata M., Maki M.;
RT   "Structure and expression of cDNA for an inhibitor of blood
RT   coagulation isolated from human placenta: a new lipocortin-like
RT   protein.";
RL   J. Biochem. 102:1261-1273(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=88271329; PubMed=2455636;
RX   DOI=10.1111/j.1432-1033.1988.tb14139.x;
RA   Maurer-Fogy I., Reutelingsperger C.P.M., Pieters J., Bodo G.,
RA   Stratowa C., Hauptmann R.;
RT   "Cloning and expression of cDNA for human vascular anticoagulant, a
RT   Ca2+-dependent phospholipid-binding protein.";
RL   Eur. J. Biochem. 174:585-592(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88228020; PubMed=2967291;
RA   Kaplan R., Jaye M., Burgess W.H., Schlaepfer D.D., Haigler H.T.;
RT   "Cloning and expression of cDNA for human endonexin II, a Ca2+ and
RT   phospholipid binding protein.";
RL   J. Biol. Chem. 263:8037-8043(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88273202; PubMed=2968983;
RA   Pepinsky R.B., Tizard R., Mattaliano R.J., Sinclair L.K., Miller G.T.,
RA   Browning J.L., Chow E.P., Burne C., Huang K.-S., Pratt D., Wachter L.,
RA   Hession C., Frey A.Z., Wallner B.P.;
RT   "Five distinct calcium and phospholipid binding proteins share
RT   homology with lipocortin I.";
RL   J. Biol. Chem. 263:10799-10811(1988).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88234495; PubMed=2967495;
RA   Grundmann U., Abel K.-J., Bohn H., Loebermann H., Lottspeich F.,
RA   Kuepper H.;
RT   "Characterization of cDNA encoding human placental anticoagulant
RT   protein (PP4): homology with the lipocortin family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:3708-3712(1988).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Lung;
RX   MEDLINE=95047484; PubMed=7958998; DOI=10.1016/0378-1119(94)90157-0;
RA   Fernandez M.-P., Morgan R.O., Fernandez M.R., Carcedo M.-T.;
RT   "The gene encoding human annexin V has a TATA-less promoter with a
RT   high G+C content.";
RL   Gene 149:253-260(1994).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94307733; PubMed=8034319; DOI=10.1006/geno.1994.1201;
RA   Cookson B.T., Engelhardt S., Smith C., Bamford H.A., Prochazka M.,
RA   Tait J.F.;
RT   "Organization of the human annexin V (ANX5) gene.";
RL   Genomics 20:463-467(1994).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Muscle, Ovary, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=90088443; PubMed=2532007;
RA   Rothhut R., Comera C., Cortial S., Haumont P.-Y., Diep Le K.H.,
RA   Cavadore J.-C., Conard J., Russo-Marie F., Lederer F.;
RT   "A 32 kDa lipocortin from human mononuclear cells appears to be
RT   identical with the placental inhibitor of blood coagulation.";
RL   Biochem. J. 263:929-935(1989).
RN   [12]
RP   PROTEIN SEQUENCE OF 7-18; 30-45; 187-201 AND 277-286, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RA   Quadroni M., Potts A., Barblan J., Bienvenut W.V.;
RL   Submitted (JAN-2005) to UniProtKB.
RN   [13]
RP   PROTEIN SEQUENCE OF 86-131; 259-297 AND 300-320.
RX   MEDLINE=87317598; PubMed=2957692;
RA   Schlaepfer D.D., Mehlman T., Burgess W.H., Haigler H.T.;
RT   "Structural and functional characterization of endonexin II, a
RT   calcium- and phospholipid-binding protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:6078-6082(1987).
RN   [14]
RP   PROTEIN SEQUENCE OF 85-93.
RX   MEDLINE=89066652; PubMed=2974032;
RA   Ahn N.G., Teller D.C., Bienkowski M.J., McMullen B.A., Lipkin E.W.,
RA   de Haen C.;
RT   "Sedimentation equilibrium analysis of five lipocortin-related
RT   phospholipase A2 inhibitors from human placenta. Evidence against a
RT   mechanistically relevant association between enzyme and inhibitor.";
RL   J. Biol. Chem. 263:18657-18663(1988).
RN   [15]
RP   PROTEIN SEQUENCE OF 152-161 AND 246-260.
RC   TISSUE=Adipocyte;
RX   PubMed=15242332; DOI=10.1042/BJ20040647;
RA   Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT   "Vectorial proteomics reveal targeting, phosphorylation and specific
RT   fragmentation of polymerase I and transcript release factor (PTRF) at
RT   the surface of caveolae in human adipocytes.";
RL   Biochem. J. 383:237-248(2004).
RN   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, AND MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-94, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18083107; DOI=10.1016/j.cell.2007.11.025;
RA   Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,
RA   Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,
RA   Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,
RA   Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,
RA   Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
RT   "Global survey of phosphotyrosine signaling identifies oncogenic
RT   kinases in lung cancer.";
RL   Cell 131:1190-1203(2007).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   MEDLINE=91065314; PubMed=2147412;
RA   Huber R., Roemisch J., Paques E.-P.;
RT   "The crystal and molecular structure of human annexin V, an
RT   anticoagulant protein that binds to calcium and membranes.";
RL   EMBO J. 9:3867-3874(1990).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE=91085549; PubMed=2148156; DOI=10.1016/0014-5793(90)81428-Q;
RA   Huber R., Schneider M., Mayr I., Roemisch J., Paques E.-P.;
RT   "The calcium binding sites in human annexin V by crystal structure
RT   analysis at 2.0-A resolution. Implications for membrane binding and
RT   calcium channel activity.";
RL   FEBS Lett. 275:15-21(1990).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE=92177413; PubMed=1311770; DOI=10.1016/0022-2836(92)90984-R;
RA   Huber R., Berendes R., Burger A., Schneider M., Karshikov A.,
RA   Luecke H., Roemisch J., Paques E.-P.;
RT   "Crystal and molecular structure of human annexin V after refinement.
RT   Implications for structure, membrane binding and ion channel formation
RT   of the annexin family of proteins.";
RL   J. Mol. Biol. 223:683-704(1992).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   MEDLINE=98062349; PubMed=9398511; DOI=10.1006/jmbi.1997.1375;
RA   Kaneko N., Ago H., Matsuda R., Inagaki E., Miyano M.;
RT   "Crystal structure of annexin V with its ligand K-201 as a calcium
RT   channel activity inhibitor.";
RL   J. Mol. Biol. 274:16-20(1997).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   MEDLINE=98118533; PubMed=9435213; DOI=10.1073/pnas.95.2.455;
RA   Budisa N., Minks C., Medrano F.J., Lutz J., Huber R., Moroder L.;
RT   "Residue-specific bioincorporation of non-natural, biologically active
RT   amino acids into proteins as possible drug carriers: structure and
RT   stability of the per-thiaproline mutant of annexin V.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:455-459(1998).
CC   -!- FUNCTION: This protein is an anticoagulant protein that acts as an
CC       indirect inhibitor of the thromboplastin-specific complex, which
CC       is involved in the blood coagulation cascade.
CC   -!- SUBUNIT: Monomer. Binds ATRX and EIF5B (By similarity).
CC   -!- INTERACTION:
CC       P70489:Abp10 (xeno); NbExp=1; IntAct=EBI-296601, EBI-78367;
CC       P70486:Atrx (xeno); NbExp=1; IntAct=EBI-296601, EBI-78333;
CC       Q9Z330:Dnmt1 (xeno); NbExp=1; IntAct=EBI-296601, EBI-78342;
CC       P70488:Eif5b (xeno); NbExp=1; IntAct=EBI-296601, EBI-78359;
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for
CC       calcium and phospholipid.
CC   -!- SIMILARITY: Belongs to the annexin family.
CC   -!- SIMILARITY: Contains 4 annexin repeats.
CC   -!- CAUTION: This protein has been independently sequenced by at least
CC       seven groups under different names.
CC   -!- CAUTION: Ref.9 sequence was thought to originate from mouse.
CC   -!- WEB RESOURCE: Name=R&D Systems' cytokine source book: Annexin V;
CC       URL="http://www.rndsystems.com/molecule_detail.aspx?m=1063";
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DR   EMBL; M18366; AAA35570.1; -; mRNA.
DR   EMBL; D00172; BAA00122.1; -; mRNA.
DR   EMBL; X12454; CAA30985.1; -; mRNA.
DR   EMBL; J03745; AAA52386.1; -; mRNA.
DR   EMBL; M21731; AAA36166.1; -; mRNA.
DR   EMBL; M19384; AAB59545.1; -; mRNA.
DR   EMBL; U01691; AAB40047.1; -; Genomic_DNA.
DR   EMBL; U01681; AAB40047.1; JOINED; Genomic_DNA.
DR   EMBL; U01682; AAB40047.1; JOINED; Genomic_DNA.
DR   EMBL; U01683; AAB40047.1; JOINED; Genomic_DNA.
DR   EMBL; U01685; AAB40047.1; JOINED; Genomic_DNA.
DR   EMBL; U01686; AAB40047.1; JOINED; Genomic_DNA.
DR   EMBL; U01687; AAB40047.1; JOINED; Genomic_DNA.
DR   EMBL; U01689; AAB40047.1; JOINED; Genomic_DNA.
DR   EMBL; U01690; AAB40047.1; JOINED; Genomic_DNA.
DR   EMBL; U05770; AAB60648.1; -; Genomic_DNA.
DR   EMBL; U05760; AAB60648.1; JOINED; Genomic_DNA.
DR   EMBL; U05761; AAB60648.1; JOINED; Genomic_DNA.
DR   EMBL; U05762; AAB60648.1; JOINED; Genomic_DNA.
DR   EMBL; U05764; AAB60648.1; JOINED; Genomic_DNA.
DR   EMBL; U05765; AAB60648.1; JOINED; Genomic_DNA.
DR   EMBL; U05766; AAB60648.1; JOINED; Genomic_DNA.
DR   EMBL; U05767; AAB60648.1; JOINED; Genomic_DNA.
DR   EMBL; U05768; AAB60648.1; JOINED; Genomic_DNA.
DR   EMBL; U05769; AAB60648.1; JOINED; Genomic_DNA.
DR   EMBL; CR536522; CAG38759.1; -; mRNA.
DR   EMBL; BC001429; AAH01429.1; -; mRNA.
DR   EMBL; BC004993; AAH04993.1; -; mRNA.
DR   EMBL; BC012804; AAH12804.1; -; mRNA.
DR   EMBL; BC012822; AAH12822.1; -; mRNA.
DR   EMBL; BC018671; AAH18671.1; -; mRNA.
DR   IPI; IPI00329801; -.
DR   PIR; D29250; AQHUP.
DR   RefSeq; NP_001145.1; -.
DR   UniGene; Hs.480653; -.
DR   UniGene; Hs.658778; -.
DR   PDB; 1ANW; X-ray; 2.40 A; A/B=1-320.
DR   PDB; 1ANX; X-ray; 1.90 A; A/B/C=1-320.
DR   PDB; 1AVH; X-ray; 2.30 A; A/B=1-320.
DR   PDB; 1AVR; X-ray; 2.30 A; A=1-320.
DR   PDB; 1HAK; X-ray; 3.00 A; A/B=1-320.
DR   PDB; 1HVD; X-ray; 2.00 A; A=1-320.
DR   PDB; 1HVE; X-ray; 2.30 A; A=1-320.
DR   PDB; 1HVF; X-ray; 2.00 A; A=1-320.
DR   PDB; 1HVG; X-ray; 3.00 A; A=1-320.
DR   PDB; 1SAV; X-ray; 2.50 A; A=1-320.
DR   PDBsum; 1ANW; -.
DR   PDBsum; 1ANX; -.
DR   PDBsum; 1AVH; -.
DR   PDBsum; 1AVR; -.
DR   PDBsum; 1HAK; -.
DR   PDBsum; 1HVD; -.
DR   PDBsum; 1HVE; -.
DR   PDBsum; 1HVF; -.
DR   PDBsum; 1HVG; -.
DR   PDBsum; 1SAV; -.
DR   IntAct; P08758; 8.
DR   PhosphoSite; P08758; -.
DR   Aarhus/Ghent-2DPAGE; 8213; IEF.
DR   Cornea-2DPAGE; P08758; -.
DR   OGP; P08758; -.
DR   REPRODUCTION-2DPAGE; IPI00329801; -.
DR   REPRODUCTION-2DPAGE; P08758; -.
DR   PeptideAtlas; P08758; -.
DR   PRIDE; P08758; -.
DR   Ensembl; ENSG00000164111; Homo sapiens.
DR   GeneID; 308; -.
DR   KEGG; hsa:308; -.
DR   GeneCards; GC04M122868; -.
DR   H-InvDB; HIX0004479; -.
DR   HGNC; HGNC:543; ANXA5.
DR   HPA; CAB003677; -.
DR   MIM; 131230; gene.
DR   PharmGKB; PA24833; -.
DR   HOGENOM; P08758; -.
DR   HOVERGEN; P08758; -.
DR   LinkHub; P08758; -.
DR   NextBio; 1243; -.
DR   ArrayExpress; P08758; -.
DR   Bgee; P08758; -.
DR   CleanEx; HS_ANXA5; -.
DR   GermOnline; ENSG00000164111; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:InterPro.
DR   GO; GO:0004859; F:phospholipase inhibitor activity; TAS:ProtInc.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006916; P:anti-apoptosis; TAS:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0050819; P:negative regulation of coagulation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR   InterPro; IPR001464; Annexin.
DR   InterPro; IPR015473; Annexins_V.
DR   InterPro; IPR002392; AnnexinV.
DR   Gene3D; G3DSA:1.10.220.10; Annexin; 4.
DR   PANTHER; PTHR10502; Annexin; 1.
DR   PANTHER; PTHR10502:SF26; Annexins_V; 1.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR00201; ANNEXINV.
DR   ProDom; PD000143; Annexin; 4.
DR   SMART; SM00335; ANX; 4.
DR   PROSITE; PS00223; ANNEXIN; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Annexin; Blood coagulation; Calcium;
KW   Calcium/phospholipid-binding; Direct protein sequencing;
KW   Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    320       Annexin A5.
FT                                /FTId=PRO_0000067487.
FT   REPEAT       24     84       Annexin 1.
FT   REPEAT       96    156       Annexin 2.
FT   REPEAT      180    240       Annexin 3.
FT   REPEAT      255    315       Annexin 4.
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES      94     94       Phosphotyrosine.
FT   MOD_RES     101    101       N6-acetyllysine.
FT   CONFLICT    135    135       S -> L (in Ref. 9; CAG38759).
FT   CONFLICT    279    279       I -> T (in Ref. 10; AAH18671).
FT   HELIX        17     28
FT   STRAND       29     32
FT   HELIX        35     42
FT   HELIX        47     61
FT   HELIX        65     72
FT   HELIX        75     85
FT   HELIX        88     99
FT   HELIX       102    104
FT   HELIX       107    116
FT   HELIX       119    133
FT   HELIX       137    144
FT   HELIX       147    157
FT   HELIX       169    184
FT   TURN        185    187
FT   HELIX       191    200
FT   HELIX       203    215
FT   HELIX       221    224
FT   TURN        227    229
FT   HELIX       232    245
FT   HELIX       247    257
FT   STRAND      260    263
FT   HELIX       266    275
FT   TURN        276    280
FT   HELIX       281    292
FT   HELIX       296    303
FT   HELIX       306    316
SQ   SEQUENCE   320 AA;  35937 MW;  45E14E3964BA4D1A CRC64;
     MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR QEISAAFKTL
     FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTNEKVL TEIIASRTPE
     ELRAIKQVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDAGIDEA QVEQDAQALF
     QAGELKWGTD EEKFITIFGT RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV
     VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVMVSRSEID LFNIRKEFRK NFATSLYSMI
     KGDTSGDYKK ALLLLCGEDD
//
ID   CSF3_HUMAN              Reviewed;         207 AA.
AC   P09919;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   10-FEB-2009, entry version 109.
DE   RecName: Full=Granulocyte colony-stimulating factor;
DE            Short=G-CSF;
DE   AltName: Full=Pluripoietin;
DE   AltName: INN=Filgrastim;
DE   AltName: INN=Lenograstim;
DE   Flags: Precursor;
GN   Name=CSF3; Synonyms=GCSF;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=86118679; PubMed=3484805; DOI=10.1038/319415a0;
RA   Nagata S., Tsuchiya M., Asano S., Kaziro Y., Yamazaki T., Yamamoto O.,
RA   Hirata Y., Kubota N., Oheda M., Nomura H., Ono M.;
RT   "Molecular cloning and expression of cDNA for human granulocyte
RT   colony-stimulating factor.";
RL   Nature 319:415-418(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=86220137; PubMed=2423327;
RA   Nagata S., Tsuchiya M., Asano S., Yamamoto O., Hirata Y., Kubota N.,
RA   Oheda M., Nomura H., Yamazaki T.;
RT   "The chromosomal gene structure and two mRNAs for human granulocyte
RT   colony-stimulating factor.";
RL   EMBO J. 5:575-581(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87196936; PubMed=3494801;
RA   Devlin J.J., Devlin P.E., Myambo K., Lilly M.B., Rado T.A.,
RA   Warren M.K.;
RT   "Expression of granulocyte colony-stimulating factor by human cell
RT   lines.";
RL   J. Leukoc. Biol. 41:302-306(1987).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-157 AND THR-174.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 19-207.
RX   MEDLINE=86151684; PubMed=2420009;
RA   Souza L.M., Boone T.C., Gabrilove J., Lai P.H., Zsebo K.M.,
RA   Murdock D.C., Chazin V.R., Bruszewski J., Lu H., Chen K.K.,
RA   Barendt J., Platzer E., Moore M.A.S., Mertelsmann R., Welte K.;
RT   "Recombinant human granulocyte colony-stimulating factor: effects on
RT   normal and leukemic myeloid cells.";
RL   Science 232:61-66(1986).
RN   [6]
RP   PROTEIN SEQUENCE OF 30-46.
RX   MEDLINE=96132662; PubMed=8554326; DOI=10.1006/abbi.1995.0047;
RA   Haniu M., Horan T., Arakawa T., Le J., Katta V., Rohde M.F.;
RT   "Extracellular domain of granulocyte-colony stimulating factor
RT   receptor. Interaction with its ligand and identification of a domain
RT   in close proximity of ligand-binding region.";
RL   Arch. Biochem. Biophys. 324:344-356(1995).
RN   [7]
RP   GLYCOSYLATION AT THR-166.
RX   MEDLINE=93293942; PubMed=7685769; DOI=10.1016/0021-9673(93)83098-D;
RA   Clogston C.L., Hu S., Boone T.C., Lu H.S.;
RT   "Glycosidase digestion, electrophoresis and chromatographic analysis
RT   of recombinant human granulocyte colony-stimulating factor glycoforms
RT   produced in Chinese hamster ovary cells.";
RL   J. Chromatogr. A 637:55-62(1993).
RN   [8]
RP   STRUCTURE BY NMR.
RX   MEDLINE=93106200; PubMed=1281794; DOI=10.1016/0014-5793(92)81521-M;
RA   Zink T., Ross A., Ambrosius D., Rudolph R., Holak T.A.;
RT   "Secondary structure of human granulocyte colony-stimulating factor
RT   derived from NMR spectroscopy.";
RL   FEBS Lett. 314:435-439(1992).
RN   [9]
RP   STRUCTURE BY NMR.
RX   MEDLINE=94304859; PubMed=7518249; DOI=10.1021/bi00194a009;
RA   Zink T., Ross A., Luers K., Cieslar C., Rudolph R., Holak T.A.;
RT   "Structure and dynamics of the human granulocyte colony-stimulating
RT   factor determined by NMR spectroscopy. Loop mobility in a four-helix-
RT   bundle protein.";
RL   Biochemistry 33:8453-8463(1994).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   MEDLINE=93281718; PubMed=7685117;
RA   Hill C.P., Osslund T.D., Eisenberg D.;
RT   "The structure of granulocyte-colony-stimulating factor and its
RT   relationship to other growth factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:5167-5171(1993).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 31-207 IN COMPLEX WITH CSF3R.
RX   PubMed=10537111; DOI=10.1038/44394;
RA   Aritomi M., Kunishima N., Okamoto T., Kuroki R., Ota Y., Morikawa K.;
RT   "Atomic structure of the GCSF-receptor complex showing a new cytokine-
RT   receptor recognition scheme.";
RL   Nature 401:713-717(1999).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 31-207 IN COMPLEX WITH CSF3R.
RX   PubMed=16492764; DOI=10.1073/pnas.0511264103;
RA   Tamada T., Honjo E., Maeda Y., Okamoto T., Ishibashi M., Tokunaga M.,
RA   Kuroki R.;
RT   "Homodimeric cross-over structure of the human granulocyte colony-
RT   stimulating factor (GCSF) receptor signaling complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3135-3140(2006).
CC   -!- FUNCTION: Granulocyte/macrophage colony-stimulating factors are
CC       cytokines that act in hematopoiesis by controlling the production,
CC       differentiation, and function of 2 related white cell populations
CC       of the blood, the granulocytes and the monocytes-macrophages. This
CC       CSF induces granulocytes.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P09919-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P09919-2; Sequence=VSP_002673;
CC   -!- PTM: O-glycan consists of Gal-GalNAc disaccharide which can be
CC       modified with up to two sialic acid residues (done in
CC       recombinantly expressed G-CSF from CHO cells).
CC   -!- PHARMACEUTICAL: Available under the names Neupogen or Granulokine
CC       (Amgen/Roche) and Granocyte (Rhone-Poulenc). Used to treat
CC       neutropenia (a disorder characterized by an extremely low number
CC       of neutrophils in blood).
CC   -!- SIMILARITY: Belongs to the IL-6 superfamily.
CC   -!- CAUTION: PubMed:2420009 misquotes the gene name as "CSF1".
CC   -!- WEB RESOURCE: Name=Neupogen/Granulokine; Note=Clinical information
CC       on Neupogen/Granulokine;
CC       URL="http://www.neupogen.com/";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/csf3/";
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; X03438; CAA27168.1; -; mRNA.
DR   EMBL; X03656; CAA27291.1; -; Genomic_DNA.
DR   EMBL; X03655; CAA27290.1; -; mRNA.
DR   EMBL; M17706; AAA35882.1; -; mRNA.
DR   EMBL; AF388025; AAK62469.1; -; Genomic_DNA.
DR   EMBL; M13008; AAA03056.1; -; Unassigned_DNA.
DR   IPI; IPI00018306; -.
DR   IPI; IPI00172503; -.
DR   PIR; A24573; A24573.
DR   PIR; A25093; FQHUGL.
DR   RefSeq; NP_000750.1; -.
DR   RefSeq; NP_757373.1; -.
DR   UniGene; Hs.2233; -.
DR   PDB; 1CD9; X-ray; 2.80 A; A/C=31-207.
DR   PDB; 1GNC; NMR; -; A=31-207.
DR   PDB; 1PGR; X-ray; 3.50 A; A/C/E/G=31-207.
DR   PDB; 1RHG; X-ray; 2.20 A; A/B/C=31-207.
DR   PDB; 2D9Q; X-ray; 2.80 A; A=31-207.
DR   PDBsum; 1CD9; -.
DR   PDBsum; 1GNC; -.
DR   PDBsum; 1PGR; -.
DR   PDBsum; 1RHG; -.
DR   PDBsum; 2D9Q; -.
DR   PRIDE; P09919; -.
DR   Ensembl; ENSG00000108342; Homo sapiens.
DR   GeneID; 1440; -.
DR   KEGG; hsa:1440; -.
DR   GeneCards; GC17P035425; -.
DR   H-InvDB; HIX0013789; -.
DR   HGNC; HGNC:2438; CSF3.
DR   HPA; CAB016131; -.
DR   HPA; HPA001412; -.
DR   MIM; 138970; gene.
DR   PharmGKB; PA26941; -.
DR   HOGENOM; P09919; -.
DR   HOVERGEN; P09919; -.
DR   DrugBank; DB00099; Filgrastim.
DR   DrugBank; DB00019; Pegfilgrastim.
DR   LinkHub; P09919; -.
DR   NextBio; 5893; -.
DR   Bgee; P09919; -.
DR   CleanEx; HS_CSF3; -.
DR   GermOnline; ENSG00000108342; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005856; C:cytoskeleton; IDA:HPA.
DR   GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR   GO; GO:0005125; F:cytokine activity; NAS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0005130; F:granulocyte colony-stimulating factor recep...; TAS:ProtInc.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; NAS:UniProtKB.
DR   GO; GO:0030851; P:granulocyte differentiation; NAS:UniProtKB.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR   InterPro; IPR012351; 4_helix_cytokine_core.
DR   InterPro; IPR003629; GCSF_MGF.
DR   InterPro; IPR003573; IL6_MGF_GCSF.
DR   Gene3D; G3DSA:1.20.1250.10; 4_helix_cytokine_core; 1.
DR   PANTHER; PTHR10511:SF2; GCSF_MGF; 1.
DR   Pfam; PF00489; IL6; 1.
DR   PIRSF; PIRSF001935; IL6_MGF_GCSF; 1.
DR   PRINTS; PR00433; IL6GCSFMGF.
DR   SMART; SM00126; IL6; 1.
DR   PROSITE; PS00254; INTERLEUKIN_6; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytokine;
KW   Direct protein sequencing; Glycoprotein; Growth factor;
KW   Pharmaceutical; Polymorphism; Secreted; Signal.
FT   SIGNAL        1     29       Probable.
FT   CHAIN        30    207       Granulocyte colony-stimulating factor.
FT                                /FTId=PRO_0000015570.
FT   CARBOHYD    166    166       O-linked (GalNAc...) (By similarity).
FT   DISULFID     69     75
FT   DISULFID     97    107
FT   VAR_SEQ      66     68       Missing (in isoform Short).
FT                                /FTId=VSP_002673.
FT   VARIANT     157    157       L -> M (in dbSNP:rs2227329).
FT                                /FTId=VAR_013073.
FT   VARIANT     174    174       A -> T (in dbSNP:rs2227330).
FT                                /FTId=VAR_013074.
FT   CONFLICT     30     30       A -> M (in Ref. 6; AA sequence).
FT   HELIX        41     71
FT   HELIX        77     80
FT   HELIX        81     86
FT   HELIX       105    124
FT   TURN        125    127
FT   TURN        130    132
FT   HELIX       133    156
FT   HELIX       176    204
SQ   SEQUENCE   207 AA;  22293 MW;  421F635ECC776996 CRC64;
     MAGPATQSPM KLMALQLLLW HSALWTVQEA TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA
     LQEKLVSECA TYKLCHPEEL VLLGHSLGIP WAPLSSCPSQ ALQLAGCLSQ LHSGLFLYQG
     LLQALEGISP ELGPTLDTLQ LDVADFATTI WQQMEELGMA PALQPTQGAM PAFASAFQRR
     AGGVLVASHL QSFLEVSYRV LRHLAQP
//
ID   COLI_HUMAN              Reviewed;         267 AA.
AC   P01189; P78442; Q9UD39; Q9UD40;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   10-FEB-2009, entry version 101.
DE   RecName: Full=Corticotropin-lipotropin;
DE   AltName: Full=Pro-opiomelanocortin;
DE            Short=POMC;
DE   Contains:
DE     RecName: Full=NPP;
DE   Contains:
DE     RecName: Full=Melanotropin gamma;
DE     AltName: Full=Gamma-MSH;
DE   Contains:
DE     RecName: Full=Potential peptide;
DE   Contains:
DE     RecName: Full=Corticotropin;
DE     AltName: Full=Adrenocorticotropic hormone;
DE              Short=ACTH;
DE   Contains:
DE     RecName: Full=Melanotropin alpha;
DE     AltName: Full=Alpha-MSH;
DE   Contains:
DE     RecName: Full=Corticotropin-like intermediary peptide;
DE              Short=CLIP;
DE   Contains:
DE     RecName: Full=Lipotropin beta;
DE     AltName: Full=Beta-LPH;
DE   Contains:
DE     RecName: Full=Lipotropin gamma;
DE     AltName: Full=Gamma-LPH;
DE   Contains:
DE     RecName: Full=Melanotropin beta;
DE     AltName: Full=Beta-MSH;
DE   Contains:
DE     RecName: Full=Beta-endorphin;
DE   Contains:
DE     RecName: Full=Met-enkephalin;
DE   Flags: Precursor;
GN   Name=POMC;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=82095599; PubMed=6274691; DOI=10.1016/0014-5793(81)80952-0;
RA   Takahashi H., Teranishi Y., Nakanishi S., Numa S.;
RT   "Isolation and structural organization of the human corticotropin-
RT   beta-lipotropin precursor gene.";
RL   FEBS Lett. 135:97-102(1981).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=83157116; PubMed=6299668;
RA   Whitfeld P.L., Seeburg P.H., Shine J.;
RT   "The human pro-opiomelanocortin gene: organization, sequence, and
RT   interspersion with repetitive DNA.";
RL   DNA 1:133-143(1982).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=84041488; PubMed=6314261; DOI=10.1093/nar/11.19.6847;
RA   Takahashi H., Hakamata Y., Watanabe Y., Kikuno R., Miyata T., Numa S.;
RT   "Complete nucleotide sequence of the human corticotropin-beta-
RT   lipotropin precursor gene.";
RL   Nucleic Acids Res. 11:6847-6858(1983).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 6-267.
RX   MEDLINE=87270895; PubMed=3606677;
RA   Golovin S.Y., Karginov V.A., Bondar A.A., Beklemishev A.B.,
RA   Chekhranova M.K., Mertvetsov N.P., Pankov Y.A.;
RT   "Synthesis, cloning and primary structure of DNA complementary to mRNA
RT   for human pituitary pro-opiomelanocortin.";
RL   Bioorg. Khim. 13:562-564(1987).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-267.
RX   MEDLINE=81054876; PubMed=6254047;
RA   Chang A.C.Y., Cochet M., Cohen S.N.;
RT   "Structural organization of human genomic DNA encoding the pro-
RT   opiomelanocortin peptide.";
RL   Proc. Natl. Acad. Sci. U.S.A. 77:4890-4894(1980).
RN   [7]
RP   PROTEIN SEQUENCE OF 27-102.
RX   MEDLINE=82037813; PubMed=6945581;
RA   Seidah N.G., Chretien M.;
RT   "Complete amino acid sequence of a human pituitary glycopeptide: an
RT   important maturation product of pro-opiomelanocortin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:4236-4240(1981).
RN   [8]
RP   PROTEIN SEQUENCE OF 27-102.
RX   MEDLINE=81264177; PubMed=6267033;
RA   Seidah N.G., Rochemont J., Hamelin J., Lis M., Chretien M.;
RT   "Primary structure of the major human pituitary pro-opiomelanocortin
RT   NH2-terminal glycopeptide. Evidence for an aldosterone-stimulating
RT   activity.";
RL   J. Biol. Chem. 256:7977-7984(1981).
RN   [9]
RP   PROTEIN SEQUENCE OF 105-134.
RX   MEDLINE=82068518; PubMed=6272808; DOI=10.1016/S0006-291X(81)80190-8;
RA   Seidah N.G., Rochemont J., Hamelin J., Benjannet S., Chretien M.;
RT   "The missing fragment of the pro-sequence of human pro-
RT   opiomelanocortin: sequence and evidence for C-terminal amidation.";
RL   Biochem. Biophys. Res. Commun. 102:710-716(1981).
RN   [10]
RP   PROTEIN SEQUENCE OF 138-176.
RX   MEDLINE=73227142; PubMed=4352834;
RA   Bennett H.P.J., Lowry P.J., McMartin C.;
RT   "Confirmation of the 1-20 amino acid sequence of human
RT   adrenocorticotrophin.";
RL   Biochem. J. 133:11-13(1973).
RN   [11]
RP   PROTEIN SEQUENCE OF 138-176.
RX   PubMed=14463577;
RA   Lee T.H., Lerner A.B., Buettner-Janusch V.;
RT   "On the structure of human corticotropin (adrenocorticotropic
RT   hormone).";
RL   J. Biol. Chem. 236:2970-2974(1961).
RN   [12]
RP   PROTEIN SEQUENCE OF 27-41.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally
RT   verified cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [13]
RP   SEQUENCE REVISION (CORTICOTROPIN).
RX   MEDLINE=72114902; PubMed=4334191;
RA   Riniker B., Sieber P., Rittel W., Zuber H.;
RT   "Revised amino-acid sequences for porcine and human
RT   adrenocorticotrophic hormone.";
RL   Nature New Biol. 235:114-115(1972).
RN   [14]
RP   SYNTHESIS OF CORTICOTROPIN.
RX   MEDLINE=72213328; PubMed=4338630; DOI=10.1002/hlca.19720550420;
RA   Sieber P., Rittel W., Riniker B.;
RT   "Synthesis of the human adrenal cortex hormone (alpha-h-ACTH) with a
RT   revised amino-acid sequence.";
RL   Helv. Chim. Acta 55:1243-1248(1972).
RN   [15]
RP   SYNTHESIS OF CORTICOTROPIN.
RX   MEDLINE=73122604; PubMed=4347148; DOI=10.1021/ja00785a049;
RA   Yamashiro D., Li C.H.;
RT   "Adrenocorticotropins. 44. Total synthesis of the human hormone by the
RT   solid-phase method.";
RL   J. Am. Chem. Soc. 95:1310-1315(1973).
RN   [16]
RP   PROTEIN SEQUENCE OF 179-267.
RX   MEDLINE=76174468; PubMed=1264228; DOI=10.1038/260622a0;
RA   Li C.H., Chung D.;
RT   "Primary structure of human beta-lipotropin.";
RL   Nature 260:622-624(1976).
RN   [17]
RP   PROTEIN SEQUENCE OF 217-234.
RA   Harris J.I.;
RT   "Structure of a melanocyte-stimulating hormone from the human
RT   pituitary gland.";
RL   Nature 184:167-169(1959).
RN   [18]
RP   PROTEIN SEQUENCE OF 237-267.
RX   MEDLINE=77223251; PubMed=195688;
RA   Dragon N., Seidah N.G., Lis M., Routhier R., Chretien M.;
RT   "Primary structure and morphine-like activity of human beta-
RT   endorphin.";
RL   Can. J. Biochem. 55:666-670(1977).
RN   [19]
RP   NUCLEOTIDE SEQUENCE OF 235-256.
RX   MEDLINE=86244321; PubMed=2424570; DOI=10.1016/0006-8993(86)90896-6;
RA   Bovenberg R.A.L., Burbach J.P.H., Wiegant V.M., Veeneman G.H.,
RA   van Boom J.H., Baas P.D., Jansz H.S., de Wied D.;
RT   "Gamma-endorphin and schizophrenia: amino acid composition of gamma-
RT   endorphin and nucleotide sequence of gamma-endorphin cDNA from
RT   pituitary glands of schizophrenic patients.";
RL   Brain Res. 376:29-37(1986).
RN   [20]
RP   PROTEOLYTIC PROCESSING.
RX   MEDLINE=88268753; PubMed=2839146;
RA   Fenger M., Johnsen A.H.;
RT   "Alpha-amidated peptides derived from pro-opiomelanocortin in normal
RT   human pituitary.";
RL   Biochem. J. 250:781-788(1988).
RN   [21]
RP   NUCLEOTIDE SEQUENCE OF 75-104, AND VARIANT 97-SER--GLY-99 DEL.
RC   TISSUE=Pituitary;
RX   MEDLINE=95129481; PubMed=7828531; DOI=10.1210/en.136.1.195;
RA   Morris J.C., Savva D., Lowry P.J.;
RT   "Reduced expression of a naturally deleted form of human
RT   proopiomelanocortin complementary deoxyribonucleic acid after
RT   transfection into Chinese hamster ovary cells.";
RL   Endocrinology 136:195-201(1995).
RN   [22]
RP   INVOLVEMENT IN PRO-OPIOMELANOCORTININ DEFICIENCY.
RX   PubMed=9620771; DOI=10.1038/509;
RA   Krude H., Biebermann H., Luck W., Horn R., Brabant G., Grueters A.;
RT   "Severe early-onset obesity, adrenal insufficiency and red hair
RT   pigmentation caused by POMC mutations in humans.";
RL   Nat. Genet. 19:155-157(1998).
RN   [23]
RP   INVOLVEMENT IN ABDOMINAL BODY FAT DISTRIBUTION.
RX   PubMed=16046320; DOI=10.2337/diabetes.54.8.2492;
RA   Baker M., Gaukrodger N., Mayosi B.M., Imrie H., Farrall M.,
RA   Watkins H., Connell J.M.C., Avery P.J., Keavney B.;
RT   "Association between common polymorphisms of the proopiomelanocortin
RT   gene and body fat distribution: a family study.";
RL   Diabetes 54:2492-2496(2005).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Pituitary;
RX   PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA   Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT   "Phosphoproteomic analysis of the human pituitary.";
RL   Pituitary 9:109-120(2006).
RN   [25]
RP   VARIANTS ASN-106; GLY-214 AND 97-SER--GLY-99 DEL.
RX   MEDLINE=98439629; PubMed=9768693; DOI=10.1210/jc.83.10.3737;
RA   Hinney A., Becker I., Heibult O., Nottebom K., Schmidt A., Ziegler A.,
RA   Mayer H., Siegfried W., Blum W.F., Remschmidt H., Hebebrand J.;
RT   "Systematic mutation screening of the pro-opiomelanocortin gene:
RT   identification of several genetic variants including three different
RT   insertions, one nonsense and two missense point mutations in probands
RT   of different weight extremes.";
RL   J. Clin. Endocrinol. Metab. 83:3737-3741(1998).
RN   [26]
RP   VARIANT GLN-236.
RX   MEDLINE=99208218; PubMed=10193875; DOI=10.1038/sj.ijo.0800814;
RA   Echwald S.M., Sorensen T.I., Andersen T., Tybjaerg-Hansen A.,
RA   Clausen J.O., Pedersen O.;
RT   "Mutational analysis of the proopiomelanocortin gene in Caucasians
RT   with early onset obesity.";
RL   Int. J. Obes. Relat. Metab. Disord. 23:293-298(1999).
RN   [27]
RP   VARIANTS THR-7; LEU-9; GLY-236 AND 97-SER--GLY-99 DEL.
RX   MEDLINE=21139901; PubMed=11244459; DOI=10.1038/sj.ijo.0801485;
RA   del Giudice E.M., Cirillo G., Santoro N., D'Urso L., Carbone M.T.,
RA   Toro R.D., Perrone L.;
RT   "Molecular screening of the proopiomelanocortin (POMC) gene in Italian
RT   obese children: report of three new mutations.";
RL   Int. J. Obes. Relat. Metab. Disord. 25:61-67(2001).
RN   [28]
RP   VARIANT GLY-236, CHARACTERIZATION OF VARIANT GLY-236, AND POSSIBLE
RP   INVOLVEMENT IN OBESITY.
RX   PubMed=12165561; DOI=10.1093/hmg/11.17.1997;
RA   Challis B.G., Pritchard L.E., Creemers J.W.M., Delplanque J.,
RA   Keogh J.M., Luan J., Wareham N.J., Yeo G.S.H., Bhattacharyya S.,
RA   Froguel P., White A., Farooqi I.S., O'Rahilly S.;
RT   "A missense mutation disrupting a dibasic prohormone processing site
RT   in pro-opiomelanocortin (POMC) increases susceptibility to early-onset
RT   obesity through a novel molecular mechanism.";
RL   Hum. Mol. Genet. 11:1997-2004(2002).
CC   -!- FUNCTION: ACTH stimulates the adrenal glands to release cortisol.
CC   -!- FUNCTION: MSH (melanocyte-stimulating hormone) increases the
CC       pigmentation of skin by increasing melanin production in
CC       melanocytes.
CC   -!- FUNCTION: Beta-endorphin and Met-enkephalin are endogenous
CC       opiates.
CC   -!- TISSUE SPECIFICITY: ACTH and MSH are produced by the pituitary
CC       gland.
CC   -!- PTM: Specific enzymatic cleavages at paired basic residues yield
CC       the different active peptides.
CC   -!- PTM: O-glycosylated; reducing sugar is probably N-
CC       acetylgalactosamine.
CC   -!- POLYMORPHISM: Genetic variation in POMC may influence abdominal
CC       body fat distribution [MIM:609830].
CC   -!- DISEASE: Defects in POMC may be associated with susceptibility to
CC       obesity [MIM:601665].
CC   -!- DISEASE: Defects in POMC are the cause of pro-opiomelanocortinin
CC       deficiency [MIM:609734]. Affected individuals present early-onset
CC       obesity, adrenal insufficiency and red hair.
CC   -!- SIMILARITY: Belongs to the POMC family.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Melanocyte-stimulating hormone
CC       entry;
CC       URL="http://en.wikipedia.org/wiki/Melanocyte-stimulating_hormone";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M38297; AAA60140.1; -; mRNA.
DR   EMBL; J00292; AAB59621.1; -; Genomic_DNA.
DR   EMBL; J00291; AAB59621.1; JOINED; Genomic_DNA.
DR   EMBL; V01510; CAA24754.1; -; Genomic_DNA.
DR   EMBL; BC065832; AAH65832.1; -; mRNA.
DR   EMBL; M25896; AAA35799.1; -; mRNA.
DR   IPI; IPI00000160; -.
DR   PIR; A17229; CTHUP.
DR   RefSeq; NP_000930.1; -.
DR   RefSeq; NP_001030333.1; -.
DR   UniGene; Hs.1897; -.
DR   PhosphoSite; P01189; -.
DR   PRIDE; P01189; -.
DR   Ensembl; ENSG00000115138; Homo sapiens.
DR   GeneID; 5443; -.
DR   KEGG; hsa:5443; -.
DR   GeneCards; GC02M025295; -.
DR   H-InvDB; HIX0029971; -.
DR   HGNC; HGNC:9201; POMC.
DR   HPA; CAB002765; -.
DR   MIM; 176830; gene.
DR   MIM; 601665; phenotype.
DR   MIM; 609734; phenotype.
DR   MIM; 609830; phenotype.
DR   Orphanet; 71526; Obesity due to pro-opiomelanocortin deficiency.
DR   PharmGKB; PA33526; -.
DR   HOGENOM; P01189; -.
DR   HOVERGEN; P01189; -.
DR   Reactome; REACT_14797; Signaling by GPCR.
DR   DrugBank; DB00741; Hydrocortisone.
DR   DrugBank; DB00836; Loperamide.
DR   DrugBank; DB01108; Trilostane.
DR   NextBio; 21063; -.
DR   ArrayExpress; P01189; -.
DR   Bgee; P01189; -.
DR   CleanEx; HS_POMC; -.
DR   GermOnline; ENSG00000115138; Homo sapiens.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005625; C:soluble fraction; TAS:ProtInc.
DR   GO; GO:0005179; F:hormone activity; TAS:ProtInc.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR001941; Mcortin_ACTH.
DR   InterPro; IPR013533; Mcortin_ACTH_C.
DR   InterPro; IPR013531; Mcrtin_ACTH_cent.
DR   InterPro; IPR013593; Melanocortin_N.
DR   InterPro; IPR013532; Opioid_neuropept.
DR   PANTHER; PTHR11416; Mcortin_ACTH; 1.
DR   Pfam; PF00976; ACTH_domain; 1.
DR   Pfam; PF08384; NPP; 1.
DR   Pfam; PF08035; Op_neuropeptide; 1.
DR   PRINTS; PR00383; MELANOCORTIN.
DR   ProDom; PD003250; Mcortin_ACTH; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Endorphin; Glycoprotein; Hormone; Obesity;
KW   Phosphoprotein; Polymorphism; Signal.
FT   SIGNAL        1     26
FT   PEPTIDE      27    102       NPP.
FT                                /FTId=PRO_0000024966.
FT   PEPTIDE      77     87       Melanotropin gamma.
FT                                /FTId=PRO_0000024967.
FT   PEPTIDE     105    134       Potential peptide.
FT                                /FTId=PRO_0000024968.
FT   PEPTIDE     138    176       Corticotropin.
FT                                /FTId=PRO_0000024969.
FT   PEPTIDE     138    150       Melanotropin alpha.
FT                                /FTId=PRO_0000024970.
FT   PEPTIDE     156    176       Corticotropin-like intermediary peptide.
FT                                /FTId=PRO_0000024971.
FT   PEPTIDE     179    267       Lipotropin beta.
FT                                /FTId=PRO_0000024972.
FT   PEPTIDE     179    234       Lipotropin gamma.
FT                                /FTId=PRO_0000024973.
FT   PEPTIDE     217    234       Melanotropin beta.
FT                                /FTId=PRO_0000024974.
FT   PEPTIDE     237    267       Beta-endorphin.
FT                                /FTId=PRO_0000024975.
FT   PEPTIDE     237    241       Met-enkephalin.
FT                                /FTId=PRO_0000024976.
FT   MOD_RES      87     87       Phenylalanine amide.
FT   MOD_RES     134    134       Glutamic acid 1-amide.
FT   MOD_RES     150    150       Valine amide.
FT   MOD_RES     168    168       Phosphoserine.
FT   CARBOHYD     71     71       O-linked (HexNAc...).
FT   CARBOHYD     91     91       N-linked (GlcNAc...).
FT   DISULFID     28     50       By similarity.
FT   VARIANT       7      7       S -> T.
FT                                /FTId=VAR_010699.
FT   VARIANT       9      9       S -> L.
FT                                /FTId=VAR_010700.
FT   VARIANT      62     62       P -> L (in dbSNP:rs28932471).
FT                                /FTId=VAR_029762.
FT   VARIANT      97     99       Missing.
FT                                /FTId=VAR_010714.
FT   VARIANT     106    106       D -> N.
FT                                /FTId=VAR_010715.
FT   VARIANT     132    132       P -> A (in dbSNP:rs8192606).
FT                                /FTId=VAR_029314.
FT   VARIANT     214    214       E -> G.
FT                                /FTId=VAR_010716.
FT   VARIANT     236    236       R -> G (may confer susceptibility to
FT                                obesity; reduces the ability to activate
FT                                melanocortin receptor 4;
FT                                dbSNP:rs28932472).
FT                                /FTId=VAR_010701.
FT   VARIANT     236    236       R -> Q.
FT                                /FTId=VAR_012201.
FT   CONFLICT     48     48       R -> G (in Ref. 6).
FT   CONFLICT    115    115       P -> T (in Ref. 2).
SQ   SEQUENCE   267 AA;  29424 MW;  B927323474A67536 CRC64;
     MPRSCCSRSG ALLLALLLQA SMEVRGWCLE SSQCQDLTTE SNLLECIRAC KPDLSAETPM
     FPGNGDEQPL TENPRKYVMG HFRWDRFGRR NSSSSGSSGA GQKREDVSAG EDCGPLPEGG
     PEPRSDGAKP GPREGKRSYS MEHFRWGKPV GKKRRPVKVY PNGAEDESAE AFPLEFKREL
     TGQRLREGDG PDGPADDGAG AQADLEHSLL VAAEKKDEGP YRMEHFRWGS PPKDKRYGGF
     MTSEKSQTPL VTLFKNAIIK NAYKKGE
//
ID   PYR1_HUMAN              Reviewed;        2225 AA.
AC   P27708; Q6P0Q0;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 3.
DT   10-FEB-2009, entry version 106.
DE   RecName: Full=CAD protein;
DE   Includes:
DE     RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase;
DE              EC=6.3.5.5;
DE   Includes:
DE     RecName: Full=Aspartate carbamoyltransferase;
DE              EC=2.1.3.2;
DE   Includes:
DE     RecName: Full=Dihydroorotase;
DE              EC=3.5.2.3;
GN   Name=CAD;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal lung fibroblast;
RX   MEDLINE=96190701; PubMed=8619816; DOI=10.1006/bbrc.1996.0213;
RA   Iwahana H., Fujimura M., Ii S., Kondo M., Moritani M., Takahashi Y.,
RA   Yamaoka T., Yoshimoto K., Itakura M.;
RT   "Molecular cloning of a human cDNA encoding a trifunctional enzyme of
RT   carbamoyl-phosphate synthetase-aspartate transcarbamoylase-
RT   dihydroorotase in de Novo pyrimidine synthesis.";
RL   Biochem. Biophys. Res. Commun. 219:249-255(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-13; 157-165; 169-177; 359-371; 501-516; 548-555;
RP   599-606; 697-719; 761-778; 843-854; 932-944; 1034-1048; 1067-1075;
RP   1110-1127; 1229-1240; 1263-1270; 1313-1323; 1326-1333; 1658-1667;
RP   1723-1731; 1840-1848; 1976-1986; 2025-2036; 2103-2110; 2179-2187 AND
RP   2215-2225, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Colon adenocarcinoma, and Hepatoma;
RA   Bienvenut W.V., Dhillon A.S., Matallanas D., Murray L., Brunton V.G.,
RA   Cooper W.N., Boldt K., von Kriegsheim A.F., Kolch W., Frame M.C.;
RL   Submitted (FEB-2008) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1752-2225.
RX   MEDLINE=91083839; PubMed=1979741;
RA   Davidson J.N., Rao G.N., Niswander L., Andreano C., Tamer C.,
RA   Chen K.C.;
RT   "Organization and nucleotide sequence of the 3' end of the human CAD
RT   gene.";
RL   DNA Cell Biol. 9:667-676(1990).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1823 AND SER-1859, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1423, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18187866; DOI=10.2116/analsci.24.161;
RA   Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
RT   "Automated phosphoproteome analysis for cultured cancer cells by two-
RT   dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
RL   Anal. Sci. 24:161-166(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1038; SER-1859 AND
RP   THR-1884, AND MASS SPECTROMETRY.
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859 AND THR-1884, AND
RP   MASS SPECTROMETRY.
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [11]
RP   VARIANTS [LARGE SCALE ANALYSIS] GLN-177 AND CYS-735.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: This protein is a "fusion" protein encoding four
CC       enzymatic activities of the pyrimidine pathway (GATase, CPSase,
CC       ATCase and DHOase).
CC   -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC       ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC   -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate
CC       + N-carbamoyl-L-aspartate.
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
CC       aspartate.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (for dihydroorotase
CC       activity) (Potential).
CC   -!- ENZYME REGULATION: Allosterically regulated and controlled by
CC       phosphorylation. 5-phosphoribose 1-diphosphate is an activator
CC       while UMP is an inhibitor of the CPSase reaction.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from HCO(3)(-): step 1/6.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from HCO(3)(-): step 2/6.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from HCO(3)(-): step 3/6.
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase
CC       (carbamoyl phosphate synthase) form together the glutamine-
CC       dependent CPSase (GD-CPSase) (EC 6.3.5.5).
CC   -!- SIMILARITY: In the central section; belongs to the DHOase family.
CC   -!- SIMILARITY: Contains 2 ATP-grasp domains.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Aspartate carbamoyltransferase
CC       entry;
CC       URL="http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase";
CC   -----------------------------------------------------------------------
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DR   EMBL; D78586; BAA11423.1; -; mRNA.
DR   EMBL; BC065510; AAH65510.1; -; mRNA.
DR   EMBL; M38561; AAA51907.1; -; Genomic_DNA.
DR   IPI; IPI00301263; -.
DR   PIR; A36240; A36240.
DR   RefSeq; NP_004332.2; -.
DR   UniGene; Hs.377010; -.
DR   HSSP; P00479; 3CSU.
DR   IntAct; P27708; 21.
DR   MEROPS; C26.952; -.
DR   MEROPS; M38.972; -.
DR   PhosphoSite; P27708; -.
DR   PeptideAtlas; P27708; -.
DR   PRIDE; P27708; -.
DR   Ensembl; ENSG00000084774; Homo sapiens.
DR   GeneID; 790; -.
DR   KEGG; hsa:790; -.
DR   H-InvDB; HIX0001913; -.
DR   HGNC; HGNC:1424; CAD.
DR   HPA; CAB007781; -.
DR   MIM; 114010; gene.
DR   PharmGKB; PA26023; -.
DR   HOGENOM; P27708; -.
DR   HOVERGEN; P27708; -.
DR   BioCyc; MetaCyc:MON-11353; -.
DR   BRENDA; 2.1.3.2; 247.
DR   BRENDA; 3.5.2.3; 247.
DR   BRENDA; 6.3.5.5; 247.
DR   Reactome; REACT_1698; Nucleotide metabolism.
DR   DrugBank; DB00128; L-Aspartic Acid.
DR   DrugBank; DB00130; L-Glutamine.
DR   NextBio; 3214; -.
DR   ArrayExpress; P27708; -.
DR   Bgee; P27708; -.
DR   CleanEx; HS_CAD; -.
DR   GermOnline; ENSG00000084774; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hyd...; TAS:ProtInc.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006207; P:'de novo' pyrimidine base biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR006220; Anth_synthII.
DR   InterPro; IPR006130; Asp/Orn_carbamoyltranf.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P_bd.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn_bd.
DR   InterPro; IPR002082; Aspartate_carbamoyltransf_euk.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR001317; CarbamoylP_synth_GATase.
DR   InterPro; IPR005483; CarbamoylP_synth_lsu.
DR   InterPro; IPR005479; CarbamoylP_synth_lsu_ATP-bd.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu_Gln-dep.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR004722; DHOmult.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR011702; GATASE.
DR   InterPro; IPR012998; GATase_1_AS.
DR   InterPro; IPR000991; GATase_class1_C.
DR   InterPro; IPR011607; MGS.
DR   InterPro; IPR013817; Pre-ATP_grasp.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 2.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00289; CPSase_L_chain; 2.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF02142; MGS; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00101; ATCASE.
DR   PRINTS; PR00098; CPSASE.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR   TIGRFAMs; TIGR00857; pyrC_multi; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; Cytoplasm; Direct protein sequencing;
KW   Hydrolase; Ligase; Metal-binding; Multifunctional enzyme;
KW   Phosphoprotein; Polymorphism; Pyrimidine biosynthesis; Repeat;
KW   Transferase; Zinc.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2   2225       CAD protein.
FT                                /FTId=PRO_0000199506.
FT   DOMAIN      177    363       Glutamine amidotransferase type-1.
FT   DOMAIN      519    711       ATP-grasp 1.
FT   DOMAIN     1052   1243       ATP-grasp 2.
FT   REGION        2    365       GATase (Glutamine amidotransferase).
FT   REGION      366    394       Linker.
FT   REGION      395   1455       CPSase (Carbamoyl-phosphate synthase).
FT   REGION      395    933       CPSase A.
FT   REGION      934   1455       CPSase B.
FT   REGION     1456   1788       DHOase (dihydroorotase).
FT   REGION     1789   1917       Linker.
FT   REGION     1918   2225       ATCase (Aspartate transcarbamylase).
FT   ACT_SITE    252    252       For GATase activity (By similarity).
FT   ACT_SITE    336    336       For GATase activity (By similarity).
FT   ACT_SITE    338    338       For GATase activity (By similarity).
FT   METAL      1471   1471       Zinc (Potential).
FT   METAL      1473   1473       Zinc (Potential).
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES    1038   1038       Phosphoserine.
FT   MOD_RES    1423   1423       Phosphoserine.
FT   MOD_RES    1823   1823       Phosphoserine.
FT   MOD_RES    1859   1859       Phosphoserine.
FT   MOD_RES    1884   1884       Phosphothreonine.
FT   VARIANT     177    177       R -> Q (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_035897.
FT   VARIANT     735    735       Y -> C (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_035898.
FT   CONFLICT    505    505       P -> T (in Ref. 1; BAA11423).
FT   CONFLICT    535    535       A -> G (in Ref. 1; BAA11423).
FT   CONFLICT    560    560       L -> V (in Ref. 1; BAA11423).
FT   CONFLICT   1103   1103       T -> A (in Ref. 1; BAA11423).
FT   CONFLICT   1513   1513       A -> G (in Ref. 1; BAA11423).
FT   CONFLICT   1676   1676       N -> D (in Ref. 1; BAA11423).
SQ   SEQUENCE   2225 AA;  242984 MW;  2AB8E8413E825A8F CRC64;
     MAALVLEDGS VLRGQPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL VLTYPLIGNY
     GIPPDEMDEF GLCKWFESSG IHVAALVVGE CCPTPSHWSA TRTLHEWLQQ HGIPGLQGVD
     TRELTKKLRE QGSLLGKLVQ NGTEPSSLPF LDPNARPLVP EVSIKTPRVF NTGGAPRILA
     LDCGLKYNQI RCLCQRGAEV TVVPWDHALD SQEYEGLFLS NGPGDPASYP SVVSTLSRVL
     SEPNPRPVFG ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGSGRCFL TSQNHGFAVE
     TDSLPADWAP LFTNANDGSN EGIVHNSLPF FSVQFHPEHQ AGPSDMELLF DIFLETVKEA
     TAGNPGGQTV RERLTERLCP PGIPTPGSGL PPPRKVLILG SGGLSIGQAG EFDYSGSQAI
     KALKEENIQT LLINPNIATV QTSQGLADKV YFLPITPHYV TQVIRNERPD GVLLTFGGQT
     ALNCGVELTK AGVLARYGVR VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ
     AQAAAERLGY PVLVRAAFAL GGLGSGFASN REELSALVAP AFAHTSQVLV DKSLKGWKEI
     EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRQ TAIKVTQHLG
     IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA LGIPLPELRN
     SVTGGTAAFE PSVDYCVVKI PRWDLSKFLR VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL
     RMVDENCVGF DHTVKPVSDM ELETPTDKRI FVVAAALWAG YSVDRLYELT RIDRWFLHRM
     KRIIAHAQLL EQHRGQPLPP DLLQQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV
     KQIDTVAAEW PAQTNYLYLT YWGTTHDLTF RTPHVLVLGS GVYRIGSSVE FDWCAVGCIQ
     QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM DIYELENPEG VILSMGGQLP
     NNMAMALHRQ QCRVLGTSPE AIDSAENRFK FSRLLDTIGI SQPQWRELSD LESARQFCQT
     VGYPCVVRPS YVLSGAAMNV AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV
     ASDGVVAAIA ISEHVENAGV HSGDATLVTP PQDITAKTLE RIKAIVHAVG QELQVTGPFN
     LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR VIMGEEVEPV GLMTGSGVVG
     VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL KAMLSTGFKI PKKNILLTIG
     SYKNKSELLP TVRLLESLGY SLYASLGTAD FYTEHGVKVT AVDWHFEEAV DGECPPQRSI
     LEQLAEKNFE LVINLSMRGA GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL
     GQIGPAPPLK VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGITMV
     CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGTVAG SAAGLKLYLN
     ETFSELRLDS VVQWMEHFET WPSHLPIVAH AEQQTVAAVL MVAQLTQRSV HICHVARKEE
     ILLIKAAKAR GLPVTCEVAP HHLFLSHDDL ERLGPGKGEV RPELGSRQDV EALWENMAVI
     DCFASDHAPH TLEEKCGSRP PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF
     HLPPQEDTYV EVDLEHEWTI PSHMPFSKAH WTPFEGQKVK GTVRRVVLRG EVAYIDGQVL
     VPPGYGQDVR KWPQGAVPQL PPSAPATSEM TTTPERPRRG IPGLPDGRFH LPPRIHRASD
     PGLPAEEPKE KSSRKVAEPE LMGTPDGTCY PPPPVPRQAS PQNLGTPGLL HPQTSPLLHS
     LVGQHILSVQ QFTKDQMSHL FNVAHTLRMM VQKERSLDIL KGKVMASMFY EVSTRTSSSF
     AAAMARLGGA VLSFSEATSS VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR
     PVINAGDGVG EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS
     LRYVAPPSLR MPPTVRAFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE RFGSTQEYEA
     CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR AAYFRQAENG MYIRMALLAT
     VLGRF
//
ID   ARGJ_BORPE              Reviewed;         408 AA.
AC   Q7VSW3;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   20-JAN-2009, entry version 36.
DE   RecName: Full=Arginine biosynthesis bifunctional protein argJ;
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase;
DE              EC=2.3.1.35;
DE     AltName: Full=Ornithine acetyltransferase;
DE              Short=OATase;
DE     AltName: Full=Ornithine transacetylase;
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase;
DE              EC=2.3.1.1;
DE     AltName: Full=N-acetylglutamate synthase;
DE              Short=AGS;
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein argJ alpha chain;
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein argJ beta chain;
GN   Name=argJ; OrderedLocusNames=BP3807;
OS   Bordetella pertussis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=520;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   MEDLINE=22827954; PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Catalyzes two activities which are involved in the
CC       cyclic version of arginine biosynthesis: the synthesis of
CC       acetylglutamate from glutamate and acetyl-CoA, and of ornithine by
CC       transacetylation between acetylornithine and glutamate (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + L-glutamate = L-
CC       ornithine + N-acetyl-L-glutamate.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-
CC       glutamate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-
CC       acetyl-L-ornithine (cyclic): step 1/1.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 1/4.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- MISCELLANEOUS: Some bacteria possess a monofunctional argJ, i.e.,
CC       capable of catalyzing only the fifth step of the arginine
CC       biosynthetic pathway.
CC   -!- SIMILARITY: Belongs to the argJ family.
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DR   EMBL; BX640422; CAE44062.1; -; Genomic_DNA.
DR   RefSeq; NP_882305.1; -.
DR   MEROPS; T05.001; -.
DR   GeneID; 2665079; -.
DR   GenomeReviews; BX470248_GR; BP3807.
DR   KEGG; bpe:BP3807; -.
DR   NMPDR; fig|257313.1.peg.3375; -.
DR   HOGENOM; Q7VSW3; -.
DR   BioCyc; BPER257313:BP3807-MON; -.
DR   BRENDA; 2.3.1.1; 21511.
DR   BRENDA; 2.3.1.35; 21511.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0004042; F:amino-acid N-acetyltransferase activity; IEA:HAMAP.
DR   GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:HAMAP.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01106; -; 1.
DR   InterPro; IPR002813; Arg_biosynth_ArgJ.
DR   PANTHER; PTHR23100; ArgJ; 1.
DR   Pfam; PF01960; ArgJ; 1.
DR   ProDom; PD004193; ArgJ; 2.
DR   TIGRFAMs; TIGR00120; ArgJ; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW   Complete proteome; Cytoplasm; Multifunctional enzyme; Transferase.
FT   CHAIN         1    192       Arginine biosynthesis bifunctional
FT                                protein argJ alpha chain (By similarity).
FT                                /FTId=PRO_0000002133.
FT   CHAIN       193    408       Arginine biosynthesis bifunctional
FT                                protein argJ beta chain (By similarity).
FT                                /FTId=PRO_0000002134.
FT   SITE        192    193       Cleavage; by autolysis (By similarity).
SQ   SEQUENCE   408 AA;  42685 MW;  FB609FC226449721 CRC64;
     MAVNLQIPSE SEILPVAGVE IGVAEAGIRK AGRRDLTVFR LAPGSAVAGV FTRNRFRAAP
     VQVCEAHLAQ GGPIRALVVN TGNANAGTGA PGLKNAQDTC AALGKLLDVP AEQILPFSTG
     VILEPLPMDR LTAGLPAAVA DLRADGWYGA AHGIMTTDTL PKIHSRRVNI GGKTVTITGI
     SKGAGMIRPN MATMLGFLAT DAGIAQPLLR QLAIELADVS FNRITVDGDT STNDSFILIA
     TGQAGVTVDS AGDAAYAALR DALAAAATDL AQKIVRDAEG ATKFMTIRVE EAGNTEEALK
     VAYAVAHSPL VKTAFFASDP NLGRILAAIG YAGIDDLDVS RLRLWLGDVL VAVDGGRNPD
     YQEADGQRVM KQAEILVRIA LGRGQVADTV YTCDFSHEYV TINADYRS
//
ID   CPG3_CAEEL              Reviewed;         292 AA.
AC   Q21771;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-DEC-2008, entry version 45.
DE   RecName: Full=Chondroitin proteoglycan 3;
DE   Flags: Precursor;
GN   Name=cpg-3; ORFNames=R06C7.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16785326; DOI=10.1083/jcb.200603003;
RA   Olson S.K., Bishop J.R., Yates J.R., Oegema K., Esko J.D.;
RT   "Identification of novel chondroitin proteoglycans in Caenorhabditis
RT   elegans: embryonic cell division depends on CPG-1 and CPG-2.";
RL   J. Cell Biol. 173:985-994(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-174, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17761667; DOI=10.1074/mcp.M600392-MCP200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
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DR   EMBL; DQ340625; ABC65813.1; -; mRNA.
DR   EMBL; Z71266; CAA95840.1; -; Genomic_DNA.
DR   PIR; T23966; T23966.
DR   RefSeq; NP_492047.1; -.
DR   UniGene; Cel.6027; -.
DR   IntAct; Q21771; 1.
DR   Ensembl; R06C7.4; Caenorhabditis elegans.
DR   GeneID; 172465; -.
DR   KEGG; cel:R06C7.4; -.
DR   NMPDR; fig|6239.3.peg.1845; -.
DR   WormBase; WBGene00011063; cpg-3.
DR   WormPep; R06C7.4; CE06247.
DR   NextBio; 875627; -.
DR   ArrayExpress; Q21771; -.
PE   1: Evidence at protein level;
KW   Complete proteome; Glycoprotein; Proteoglycan; Signal.
FT   SIGNAL        1     17       Potential.
FT   CHAIN        18    292       Chondroitin proteoglycan 3.
FT                                /FTId=PRO_0000320222.
FT   COMPBIAS    188    292       Cys-rich.
FT   CARBOHYD    174    174       N-linked (GlcNAc...).
FT   CARBOHYD    254    254       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   292 AA;  29731 MW;  FC5C58A2FD070098 CRC64;
     MRFVFIIALL LIGASLAHPA DPIRAKRDVS ASEDEFSGDS SGEISGESSG EASGEASGEA
     SGEASGEASG ESSGETSGES SGDEETSGEG SGEEGSGDTS PVVPVDELTL QQLETLNTYA
     QQVQAESQKL IHQANFVITE MTALSANAQN LGILSNIVLA NSQMVLDSAR LSLNETETET
     GTSAPATCVS SAVCYGDSGC GSGKCIGALA GTCNCNSCVF GWPCQEDSAC GGFNGACNSI
     TATCDCFAAY TKNNLTLAEA LTSFCNVETC NGAEDNVEKC HGLPCNYGFC VC
//
ID   DAPB_KLEPN              Reviewed;         185 AA.
AC   P45415;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   20-JAN-2009, entry version 51.
DE   RecName: Full=Dihydrodipicolinate reductase;
DE            Short=DHPR;
DE            EC=1.3.1.26;
DE   Flags: Fragment;
GN   Name=dapB;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13882 / IFO 13541 / NCTC 8172;
RX   MEDLINE=95131756; PubMed=7830578;
RA   Bott M., Dimroth P.;
RT   "Klebsiella pneumoniae genes for citrate lyase and citrate lyase
RT   ligase: localization, sequencing, and expression.";
RL   Mol. Microbiol. 14:347-356(1994).
CC   -!- CATALYTIC ACTIVITY: 2,3,4,5-tetrahydrodipicolinate + NAD(P)(+) =
CC       2,3-dihydrodipicolinate + NAD(P)H.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; tetrahydrodipicolinate from L-aspartate: step 4/4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the dihydrodipicolinate reductase family.
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DR   EMBL; X79817; CAA56219.1; -; Genomic_DNA.
DR   PIR; S60778; S60778.
DR   HSSP; P04036; 1DRW.
DR   SMR; P45415; 3-185.
DR   BRENDA; 1.3.1.26; 758.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0008839; F:dihydrodipicolinate reductase activity; IEA:HAMAP.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_00102; -; 1.
DR   InterPro; IPR000846; DapB.
DR   InterPro; IPR011770; DapB_bac/pln.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR20836; DapB_bac/pln; 1.
DR   Pfam; PF05173; DapB_C; 1.
DR   Pfam; PF01113; DapB_N; 1.
DR   ProDom; PD004105; DapB; 1.
DR   TIGRFAMs; TIGR00036; dapB; 1.
DR   PROSITE; PS01298; DAPB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Diaminopimelate biosynthesis;
KW   Lysine biosynthesis; NADP; Oxidoreductase.
FT   CHAIN         1   >185       Dihydrodipicolinate reductase.
FT                                /FTId=PRO_0000141447.
FT   NON_TER     185    185
SQ   SEQUENCE   185 AA;  19061 MW;  5BF3058561EC001E CRC64;
     MHDAQIRVAI AGAGGRMGRQ LIQAALQMEG VALGAALERE GSSLVGSDAG ELAGAGKAGV
     AVQSSLAAVK DDFDVLIDFT RPEGTLNHLA FCREHGKGMV IGTTGFDDAG KQAIRDAAQD
     IAIVFAANFS VGVNVLLKLL EKAAKVMGDY TDIEIIEAHH RHKVDAPSGT ALAMGEAIAG
     ALNKD
//
ID   ABP1_PIG                Reviewed;         141 AA.
AC   Q9TRC7; Q29317;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   20-JAN-2009, entry version 43.
DE   RecName: Full=Amiloride-sensitive amine oxidase [copper-containing];
DE            Short=Diamine oxidase;
DE            Short=DAO;
DE            EC=1.4.3.22;
DE   AltName: Full=Amiloride-binding protein;
DE            Short=ABP;
DE   AltName: Full=Histaminase;
DE   AltName: Full=PK-DAO;
DE   Flags: Fragments;
GN   Name=ABP1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-20.
RC   TISSUE=Kidney;
RX   MEDLINE=94193685; PubMed=8144586;
RA   Novotny W.F., Chassande O., Baker M., Lazdunski M., Barbry P.;
RT   "Diamine oxidase is the amiloride-binding protein and is inhibited by
RT   amiloride analogues.";
RL   J. Biol. Chem. 269:9921-9925(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-39, AND TOPAQUINONE AT TYR-28.
RC   TISSUE=Kidney;
RX   MEDLINE=93090748; PubMed=1457410; DOI=10.1021/bi00163a025;
RA   Janes S.M., Palcic M.M., Scaman C.H., Smith A.J., Brown D.E.,
RA   Dooley D.M., Mure M., Klinman J.P.;
RT   "Identification of topaquinone and its consensus sequence in copper
RT   amine oxidases.";
RL   Biochemistry 31:12147-12154(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 40-141.
RC   TISSUE=Small intestine;
RX   MEDLINE=96327607; PubMed=8672129; DOI=10.1007/s003359900153;
RA   Winteroe A.K., Fredholm M., Davies W.;
RT   "Evaluation and characterization of a porcine small intestine cDNA
RT   library: analysis of 839 clones.";
RL   Mamm. Genome 7:509-517(1996).
RN   [4]
RP   GLYCAN STRUCTURE, AND MASS SPECTROMETRY.
RC   TISSUE=Kidney;
RX   PubMed=10782293; DOI=10.1016/S0008-6215(99)00254-2;
RA   Huang Y., Mechref Y., Novotny M.V.;
RT   "N-linked oligosaccharide structures in the diamine oxidase from
RT   porcine kidney.";
RL   Carbohydr. Res. 323:111-125(2000).
CC   -!- FUNCTION: Catalyzes the degradation of compounds such as
CC       putrescine, histamine, spermine, and spermidine, substances
CC       involved in allergic and immune responses, cell proliferation,
CC       tissue differentiation, tumor formation, and possibly apoptosis
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Histamine + H(2)O + O(2) = (imidazol-4-
CC       yl)acetaldehyde + NH(3) + H(2)O(2).
CC   -!- COFACTOR: Binds 1 copper ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity).
CC   -!- COFACTOR: Contains 1 topaquinone per subunit.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space (By
CC       similarity).
CC   -!- PTM: Topaquinone (TPQ) is generated by copper-dependent
CC       autoxidation of a specific tyrosyl residue.
CC   -!- PTM: N-glycosylated; the glycans are primarily linear, di-, or
CC       tribranched fucosylated complex type.
CC   -!- MISCELLANEOUS: Inhibited by amiloride in a competitive manner (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
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DR   EMBL; F14708; CAA23203.1; -; mRNA.
DR   PIR; B54410; B54410.
DR   GlycoSuiteDB; Q9TRC7; -.
DR   HOVERGEN; Q9TRC7; -.
DR   BRENDA; 1.4.3.6; 249.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0008131; F:amine oxidase activity; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0009308; P:cellular amine metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000269; Cu_amine_oxidase.
DR   PROSITE; PS01164; COPPER_AMINE_OXID_1; PARTIAL.
DR   PROSITE; PS01165; COPPER_AMINE_OXID_2; PARTIAL.
PE   1: Evidence at protein level;
KW   Calcium; Copper; Direct protein sequencing; Glycoprotein;
KW   Heparin-binding; Metal-binding; Oxidoreductase; Secreted; TPQ.
FT   CHAIN         1   >141       Amiloride-sensitive amine oxidase
FT                                [copper-containing].
FT                                /FTId=PRO_0000064100.
FT   REGION      103    110       Heparin-binding (By similarity).
FT   ACT_SITE     28     28       Schiff-base intermediate with substrate;
FT                                via topaquinone (By similarity).
FT   METAL        45     45       Copper (By similarity).
FT   METAL        47     47       Copper (By similarity).
FT   METAL        54     54       Calcium 1 (By similarity).
FT   METAL        55     55       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        56     56       Calcium 1 (By similarity).
FT   METAL        97     97       Calcium 2 (By similarity).
FT   MOD_RES      28     28       2',4',5'-topaquinone.
FT   CARBOHYD     73     73       N-linked (GlcNAc...) (Potential).
FT   NON_CONS     20     21
FT   NON_CONS     39     40
FT   NON_TER     141    141
SQ   SEQUENCE   141 AA;  16221 MW;  93590774ACDD99DC CRC64;
     TPGPKAGVFA AGVAEDLKAV TTSTVYNYDY IWDFIFYYNL IGNMHTHLVN YRVDLDVAGT
     TNSFQTLQME LENITNPWSP RHRLVQPTLK QTRYSRERQA AFRFGQPLPK YLLITSPKEN
     PWGHRAVPLQ LHFMADQVLP P
//
ID   110KD_PLAKN             Reviewed;         296 AA.
AC   P13813;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   22-JUL-2008, entry version 35.
DE   RecName: Full=110 kDa antigen;
DE   AltName: Full=PK110;
DE   Flags: Fragment;
OS   Plasmodium knowlesi.
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=5850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88039002; PubMed=2444886; DOI=10.1016/0166-6851(87)90007-7;
RA   Perler F.B., Moon A.M., Qiang B.Q., Meda M., Dalton M., Card C.,
RA   Schmidt-Ullrich R., Wallach D., Lynch J., Donelson J.E.;
RT   "Cloning and characterization of an abundant Plasmodium knowlesi
RT   antigen which cross reacts with Gambian sera.";
RL   Mol. Biochem. Parasitol. 25:185-193(1987).
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DR   EMBL; M19152; AAA29471.1; -; mRNA.
DR   PIR; A54527; A54527.
DR   ProDom; PD153432; Csurface_antigen; 2.
PE   2: Evidence at transcript level;
KW   Malaria; Repeat.
FT   CHAIN        <1    296       110 kDa antigen.
FT                                /FTId=PRO_0000217176.
FT   REPEAT      132    143       1; approximate.
FT   REPEAT      144    155       2; approximate.
FT   REPEAT      156    167       3.
FT   REPEAT      168    179       4; approximate.
FT   REPEAT      180    191       5.
FT   REPEAT      192    203       6; approximate.
FT   REPEAT      204    215       7.
FT   REPEAT      216    227       8.
FT   REPEAT      228    239       9.
FT   REPEAT      240    251       10.
FT   REPEAT      252    263       11.
FT   REPEAT      264    275       12.
FT   REPEAT      276    287       13; approximate.
FT   REPEAT      288    293       14; truncated.
FT   REGION      132    296       13.5 X 12 AA approximate tandem repeats
FT                                of E-E-T-Q-K-T-V-E-P-E-Q-T.
FT   NON_TER       1      1
SQ   SEQUENCE   296 AA;  34077 MW;  B0D7CD175C7A3625 CRC64;
     FNSNMLRGSV CEEDVSLMTS IDNMIEEIDF YEKEIYKGSH SGGVIKGMDY DLEDDENDED
     EMTEQMVEEV ADHITQDMID EVAHHVLDNI THDMAHMEEI VHGLSGDVTQ IKEIVQKVNV
     AVEKVKHIVE TEETQKTVEP EQIEETQNTV EPEQTEETQK TVEPEQTEET QNTVEPEQIE
     ETQKTVEPEQ TEEAQKTVEP EQTEETQKTV EPEQTEETQK TVEPEQTEET QKTVEPEQTE
     ETQKTVEPEQ TEETQKTVEP EQTEETQKTV EPEQTEETQN TVEPEPTQET QNTVEP
//
ID   12S_PROFR               Reviewed;         611 AA.
AC   Q8GBW6; Q05617;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   20-JAN-2009, entry version 43.
DE   RecName: Full=Methylmalonyl-CoA carboxyltransferase 12S subunit;
DE            EC=2.1.3.1;
DE   AltName: Full=Transcarboxylase 12S subunit;
OS   Propionibacterium freudenreichii subsp. shermanii.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Propionibacterineae; Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=1752;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-6; 13-39;
RP   56-63; 71-112; 199-213; 252-280; 351-372; 395-405; 500-516; 532-567
RP   AND 598-607.
RC   STRAIN=St33;
RX   MEDLINE=93374821; PubMed=8366018;
RA   Thornton C.G., Kumar G.K., Haase F.C., Phillips N.F.B., Woo S.B.,
RA   Park V.M., Magner W.J., Shenoy B.C., Wood H.G., Samols D.;
RT   "Primary structure of the monomer of the 12S subunit of
RT   transcarboxylase as deduced from DNA and characterization of the
RT   product expressed in Escherichia coli.";
RL   J. Bacteriol. 175:5301-5308(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-525, AND X-RAY CRYSTALLOGRAPHY (1.9
RP   ANGSTROMS) OF 1-524.
RX   PubMed=12743028; DOI=10.1093/emboj/cdg244;
RA   Hall P.R., Wang Y.-F., Rivera-Hainaj R.E., Zheng X., Pusztai-Carey M.,
RA   Carey P.R., Yee V.C.;
RT   "Transcarboxylase 12S crystal structure: hexamer assembly and
RT   substrate binding to a multienzyme core.";
RL   EMBO J. 22:2334-2347(2003).
CC   -!- FUNCTION: The 12S subunit specifically catalyzes the transfer of
CC       the carboxyl group of methylmalonyl CoA to the biotin of the 1.3S
CC       subunit forming propanoyl-CoA and carboxylated 1.3S-biotin.
CC   -!- CATALYTIC ACTIVITY: (S)-methylmalonyl-CoA + pyruvate = propanoyl-
CC       CoA + oxaloacetate.
CC   -!- SUBUNIT: Homohexamer. Transcarboxylase is composed of three
CC       subunits: 1.3S, 5S, and 12S. The core of the enzyme is composed of
CC       six 12S subunits. On each side of the core there are three pairs
CC       of 5S subunits. Each 5S dimer is attached to the core by two 1.3S
CC       subunits. Thus the total number of chains is 30 (6 + 12 + 12).
CC   -!- SIMILARITY: Contains 1 carboxyltransferase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA25676.1; Type=Frameshift; Positions=Several;
CC       Sequence=CAD59919.1; Type=Frameshift; Positions=519;
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DR   EMBL; L04196; AAA25676.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AJ535715; CAD59919.1; ALT_FRAME; mRNA.
DR   PIR; A48665; A48665.
DR   PDB; 1ON3; X-ray; 1.90 A; A/B/C/D/E/F=1-518.
DR   PDB; 1ON9; X-ray; 2.00 A; A/B/C/D/E/F=1-518.
DR   PDBsum; 1ON3; -.
DR   PDBsum; 1ON9; -.
DR   BioCyc; MetaCyc:MON-12429; -.
DR   BRENDA; 2.1.3.1; 4086.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0047154; F:methylmalonyl-CoA carboxytransferase activity; IEA:EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR000022; Carboxyl_trans.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Transferase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    611       Methylmalonyl-CoA carboxyltransferase 12S
FT                                subunit.
FT                                /FTId=PRO_0000146817.
FT   CONFLICT     35     35       R -> L (in Ref. 1; AAA25676).
FT   CONFLICT    143    143       Missing (in Ref. 1; AAA25676).
FT   CONFLICT    181    182       GG -> C (in Ref. 1; AAA25676).
FT   CONFLICT    377    377       Missing (in Ref. 1; AAA25676).
FT   CONFLICT    390    390       A -> R (in Ref. 1; AAA25676).
FT   HELIX        13     28
FT   TURN         29     31
FT   HELIX        33     41
FT   HELIX        47     54
FT   STRAND       61     63
FT   TURN         73     78
FT   HELIX        82     85
FT   STRAND       86     93
FT   STRAND       96    103
FT   TURN        105    107
FT   HELIX       108    110
FT   HELIX       114    130
FT   STRAND      134    140
FT   HELIX       145    148
FT   HELIX       149    165
FT   TURN        166    168
FT   STRAND      171    181
FT   HELIX       182    184
FT   HELIX       185    189
FT   STRAND      190    196
FT   STRAND      200    204
FT   HELIX       206    213
FT   HELIX       219    223
FT   HELIX       225    230
FT   STRAND      236    241
FT   HELIX       242    254
FT   HELIX       277    281
FT   HELIX       294    300
FT   HELIX       302    304
FT   STRAND      306    310
FT   STRAND      317    324
FT   STRAND      327    334
FT   HELIX       339    341
FT   HELIX       345    360
FT   STRAND      365    371
FT   HELIX       378    382
FT   HELIX       385    398
FT   STRAND      403    412
FT   HELIX       413    417
FT   TURN        418    420
FT   HELIX       422    424
FT   STRAND      427    431
FT   STRAND      436    440
FT   HELIX       442    449
FT   HELIX       451    456
FT   HELIX       460    475
FT   HELIX       478    483
FT   STRAND      486    490
FT   HELIX       493    495
FT   HELIX       496    506
FT   HELIX       507    509
SQ   SEQUENCE   611 AA;  65927 MW;  625F1B284107B1FC CRC64;
     MAENNNLKLA STMEGRVEQL AEQRQVIEAG GGERRVEKQH SQGKQTARER LNNLLDPHSF
     DEVGAFRKHR TTLFGMDKAV VPADGVVTGR GTILGRPVHA ASQDFTVMGG SAGETQSTKV
     VETMEQALLT GTPFLFFYDS GGARIQEGID SLSGYGKMFF ANVKLSGVVP QIAIIAGPCA
     GGASYSPALT DFIIMTKKAH MFITGPQVIK SVTGEDVTAD ELGGAEAHMA ISGNIHFVAE
     DDDAAELIAK KLLSFLPQNN TEEASFVNPN NDVSPNTELR DIVPIDGKKG YDVRDVIAKI
     VDWGDYLEVK AGYATNLVTA FARVNGRSVG IVANQPSVMS GCLDINASDK AAEFVNFCDS
     FNIPLVQLVD VPGFLPGVQQ EYGGIIRHGA KMLYAYSEAT VPKITVVLRK AYGGSYLAMC
     NRDLGADAVY AWPSAEIAVM GAEGAANVIF RKEIKAADDP DAMRAEKIEE YQNAFNTPYV
     AAARGQVDDV IDPADTRRKI ASALEMYATK RQTRPAKKPW KLPLLSEEEI MADEEEKDLM
     IATLNKRVAS LESELGSLQS DTQGVTEDVL TAISAVAAYL GNDGSAEVVH FAPSPNWVRE
     GRRALQNHSI R
//
ID   14331_PSEMZ             Reviewed;          80 AA.
AC   P85938;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-NOV-2008, entry version 3.
DE   RecName: Full=14-3-3-like protein 1;
DE   Flags: Fragments;
OS   Pseudotsuga menziesii (Douglas-fir).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Coniferopsida; Coniferales; Pinaceae; Pseudotsuga.
OX   NCBI_TaxID=3357;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Root;
RX   PubMed=18602030; DOI=10.1016/j.jprot.2008.06.004;
RA   Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.;
RT   "A proteomics approach to identify proteins differentially expressed
RT   in Douglas-fir seedlings infected by Phellinus sulphurascens.";
RL   J. Proteomics 71:425-438(2008).
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR   GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
DR   InterPro; IPR000308; 14-3-3.
DR   Gene3D; G3DSA:1.20.190.20; 14-3-3; 1.
DR   PANTHER; PTHR18860; 14-3-3; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   ProDom; PD000600; 14-3-3; 1.
DR   SMART; SM00101; 14_3_3; 1.
DR   PROSITE; PS00796; 1433_1; PARTIAL.
DR   PROSITE; PS00797; 1433_2; PARTIAL.
PE   1: Evidence at protein level;
KW   Direct protein sequencing.
FT   CHAIN        <1    >80       14-3-3-like protein 1.
FT                                /FTId=PRO_0000347314.
FT   NON_CONS     10     11
FT   NON_CONS     18     19
FT   NON_CONS     30     31
FT   NON_CONS     53     54
FT   NON_CONS     70     71
FT   NON_TER       1      1
FT   NON_TER      80     80
SQ   SEQUENCE   80 AA;  8974 MW;  8EA57FD9417CADE7 CRC64;
     YEEMVEFMEK NLLSVAYKII SSIEQKEESR ICEGILRLLD SHLIPSSTAA ESKSAQDIAA
     AELAPTHPIR DSTLIMQLLR
//
ID   2SS1_ARATH              Reviewed;         164 AA.
AC   P15457;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   10-FEB-2009, entry version 74.
DE   RecName: Full=2S seed storage protein 1;
DE   AltName: Full=2S albumin storage protein;
DE   AltName: Full=NWMU2-2S albumin 1;
DE   Contains:
DE     RecName: Full=2S seed storage protein 1 small subunit;
DE   Contains:
DE     RecName: Full=2S seed storage protein 1 large subunit;
DE   Flags: Precursor;
GN   Name=AT2S1; OrderedLocusNames=At4g27140; ORFNames=T24A18.90;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 38-73 AND
RP   84-162.
RC   STRAIN=cv. C24;
RX   PubMed=16666238;
RA   Krebbers E., Herdies L., de Clercq A., Seurinck J., Leemans J.,
RA   van Damme J., Segura M., Gheysen G., van Montagu M.,
RA   Vandekerckhove J.;
RT   "Determination of the processing sites of an Arabidopsis 2S albumin
RT   and characterization of the complete gene family.";
RL   Plant Physiol. 87:859-866(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. C24;
RX   PubMed=8012403;
RA   da Silva Conceicao A., Krebbers E.;
RT   "A cotyledon regulatory region is responsible for the different
RT   spatial expression patterns of Arabidopsis 2S albumin genes.";
RL   Plant J. 5:493-505(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: This is a 2S seed storage protein.
CC   -!- SUBUNIT: The mature protein consists of a small and a large chain
CC       linked by disulfide bonds.
CC   -!- MISCELLANEOUS: This is the most abundant isoform of 2S albumin in
CC       Arabidopsis.
CC   -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
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DR   EMBL; M22032; AAA32743.1; -; Genomic_DNA.
DR   EMBL; Z24745; CAA80870.1; -; Genomic_DNA.
DR   EMBL; AL035680; CAB38844.1; -; Genomic_DNA.
DR   EMBL; AL161566; CAB79569.1; -; Genomic_DNA.
DR   EMBL; AF370541; AAK48968.1; -; mRNA.
DR   EMBL; AY072508; AAL66923.1; -; mRNA.
DR   IPI; IPI00524704; -.
DR   PIR; JA0161; NWMU1.
DR   RefSeq; NP_194444.1; -.
DR   UniGene; At.158; -.
DR   HSSP; P24565; 1PNB.
DR   PRIDE; P15457; -.
DR   ProMEX; P15457; -.
DR   GeneID; 828822; -.
DR   GenomeReviews; CT486007_GR; AT4G27140.
DR   KEGG; ath:AT4G27140; -.
DR   NMPDR; fig|3702.1.peg.20649; -.
DR   TAIR; At4g27140; -.
DR   ArrayExpress; P15457; -.
DR   GermOnline; AT4G27140; Arabidopsis thaliana.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:InterPro.
DR   InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib.
DR   InterPro; IPR000617; Napin.
DR   InterPro; IPR013771; Trypsin/amylase_inhib.
DR   Gene3D; G3DSA:1.10.120.10; Trypsin/amylase_inhib; 1.
DR   Pfam; PF00234; Tryp_alpha_amyl; 1.
DR   PRINTS; PR00496; NAPIN.
DR   ProDom; PD002498; Napin; 1.
DR   SMART; SM00499; AAI; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Seed storage protein;
KW   Signal; Storage protein.
FT   SIGNAL        1     21
FT   PROPEP       22     37
FT                                /FTId=PRO_0000032088.
FT   CHAIN        38     73       2S seed storage protein 1 small subunit.
FT                                /FTId=PRO_0000032089.
FT   PROPEP       74     83
FT                                /FTId=PRO_0000032090.
FT   CHAIN        84    162       2S seed storage protein 1 large subunit.
FT                                /FTId=PRO_0000032091.
FT   PROPEP      163    164
FT                                /FTId=PRO_0000032092.
SQ   SEQUENCE   164 AA;  19014 MW;  2BF28CB474D9832B CRC64;
     MANKLFLVCA ALALCFLLTN ASIYRTVVEF EEDDATNPIG PKMRKCRKEF QKEQHLRACQ
     QLMLQQARQG RSDEFDFEDD MENPQGQQQE QQLFQQCCNE LRQEEPDCVC PTLKQAAKAV
     RLQGQHQPMQ VRKIYQTAKH LPNVCDIPQV DVCPFNIPSF PSFY
//
ID   A33_PLEWA               Reviewed;         625 AA.
AC   Q02084;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   25-NOV-2008, entry version 56.
DE   RecName: Full=Zinc-binding protein A33;
OS   Pleurodeles waltlii (Iberian ribbed newt).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Caudata; Salamandroidea; Salamandridae;
OC   Pleurodeles.
OX   NCBI_TaxID=8319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Ovary;
RX   MEDLINE=93154311; PubMed=7679068;
RA   Bellini M., Lacroix J.-C., Gall J.G.;
RT   "A putative zinc-binding protein on lampbrush chromosome loops.";
RL   EMBO J. 12:107-114(1993).
RN   [2]
RP   SEQUENCE REVISION TO 15-60 AND 427-429.
RA   Bellini M., Lacroix J.-C., Gall J.G.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, ZINC-BINDING, AND MUTAGENESIS OF
RP   CYS-178; CYS-202 AND HIS-267.
RX   PubMed=7593179; DOI=10.1083/jcb.131.3.563;
RA   Bellini M., Lacroix J.-C., Gall J.G.;
RT   "A zinc-binding domain is required for targeting the maternal nuclear
RT   protein PwA33 to lampbrush chromosome loops.";
RL   J. Cell Biol. 131:563-570(1995).
CC   -!- FUNCTION: May be a nuclear regulatory protein that is stored in
CC       the germinal vesicle for use during early embryogenesis and may
CC       play a role in the synthesis or processing of pre-mRNA during
CC       oogenesis. Binds 3 Zn(2+) ions.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Lampbrush chromosome loops and
CC       in some nucleoplasmic particles of the germinal vesicle.
CC   -!- DEVELOPMENTAL STAGE: It first appears on the chromosome loops and
CC       in the nucleoplasm of the germinal vesicle (GV). It is transmitted
CC       to the egg at GV breakdown and appears in embryonic nuclei at the
CC       mid-blastula stage and is found in many but not all nuclei at
CC       still later stages of embryogenesis.
CC   -!- DOMAIN: B box-type zinc binding domain is required for targeting
CC       this protein to lampbrush chromosome loops and for normal
CC       functioning of this protein in the oocyte.
CC   -!- SIMILARITY: Contains 1 B box-type zinc finger.
CC   -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
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DR   EMBL; L04190; AAA49614.2; -; mRNA.
DR   PIR; S28418; S28418.
DR   HSSP; Q92021; 1FRE.
DR   HOVERGEN; Q02084; -.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:InterPro.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   InterPro; IPR001870; B302.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR003879; Butyrophylin.
DR   InterPro; IPR000953; Chromodomain.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_rcpt.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   PRINTS; PR01406; BBOXZNFINGER.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Developmental protein; Metal-binding; Nucleus;
KW   RNA-binding; Zinc; Zinc-finger.
FT   CHAIN         1    625       Zinc-binding protein A33.
FT                                /FTId=PRO_0000055746.
FT   DOMAIN      429    625       B30.2/SPRY.
FT   ZN_FING     163    203       RING-type.
FT   ZN_FING     234    275       B box-type.
FT   COILED      337    386
FT   MUTAGEN     178    178       C->F: No effect on intranuclear
FT                                localization.
FT   MUTAGEN     202    202       C->F: No effect on intranuclear
FT                                localization.
FT   MUTAGEN     267    267       H->N: No Zn(2+) binding. Inhibits the
FT                                targeting to lampbrush chromosome loops
FT                                and to nucleoplasmic particles.
SQ   SEQUENCE   625 AA;  71053 MW;  BCE8003BB6BF5B13 CRC64;
     MANSTVAEPE KMEQSGTCEE DEEEENMEGD EDECDDDEEE NMEPAETVTI GSTYKCRRSD
     NTLHAAEIIK TRKTKENAEE FYVHYVGLNR RQNEWVDKSR VLQAKQIKTE ELNNTEDETN
     GVSDQSEGKA ARSNKRKIED GDGDQKKRKV DDEEDDFTED LTCPLCRSLF KEPVILECGH
     NFCKHCIDKS WESASAFSCP ECKEVLTERK YTTNRVLANL VKKAAVGVKD KDVKPKEKCD
     EHDERLKLFC KDDGTLACVI CRDSLKHSNH NFLPIQDAVG VYRDQLIALV SPLETTMKEN
     QKLKCDQSQK ISLHRENIVD CKKHIECEFE KLHQFLREKE AKMVEDLNAE REGLLKDMEA
     NLVKMTDNCE FIEEAISTTQ SRLNESDPIA FLTDIKSFIE KCCEEHRKGV PAESVLVNKE
     LSQGRFKGPL QYIIWKELKS VVQPGLAPLT LDPNTAHPNL VLSEGLTSVK YTDTKQQLPD
     NPKRFSQCIL VLGAEGFDSG KHYWEVEVGN KTAWDVGMAS ESSNRKGKIK LNPKNGYWAI
     WLRNGNAFKA LESPSKTLNL TSKPSKIGVY LDYEGGQVSF YNADDMSPIY TFNGSFTEKL
     YPYLSPFLQD SGKNAEPLKL VHTKL
//
ID   AACT_HUMAN              Reviewed;         423 AA.
AC   P01011; B3KVQ7; Q13703; Q2TU87; Q2TU88; Q59GP9; Q6LBY8; Q6LDT7;
AC   Q6NSC9; Q8N177; Q96DW8; Q9UC47; Q9UNU9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 2.
DT   10-FEB-2009, entry version 126.
DE   RecName: Full=Alpha-1-antichymotrypsin;
DE            Short=ACT;
DE   AltName: Full=Cell growth-inhibiting gene 24/25 protein;
DE   Contains:
DE     RecName: Full=Alpha-1-antichymotrypsin His-Pro-less;
DE   Flags: Precursor;
GN   Name=SERPINA3; Synonyms=AACT; ORFNames=GIG24, GIG25;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   MEDLINE=84080367; PubMed=6606438; DOI=10.1021/bi00291a001;
RA   Chandra T., Stackhouse R., Kidd V.J., Robson K.J.H., Woo S.L.C.;
RT   "Sequence homology between human alpha 1-antichymotrypsin, alpha 1-
RT   antitrypsin, and antithrombin III.";
RL   Biochemistry 22:5055-5061(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN COPD, AND VARIANTS
RP   BOCHUM-1 PRO-78 AND BONN-1 ALA-252.
RX   MEDLINE=94063919; PubMed=8244391; DOI=10.1006/geno.1993.1396;
RA   Poller W., Faber J.-P., Weidinger S., Tief K., Scholz S., Fischer M.,
RA   Olek K., Kirchgesser M., Heidtmann H.-H.;
RT   "A leucine-to-proline substitution causes a defective alpha 1-
RT   antichymotrypsin allele associated with familial obstructive lung
RT   disease.";
RL   Genomics 17:740-743(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-9.
RA   Kim J.W.;
RT   "Identification of a human cell growth inhibiting gene.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-9.
RC   TISSUE=Urinary bladder;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-9.
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno F.R.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND
RP   VARIANTS THR-9 AND ARG-267.
RC   TISSUE=Brain, Liver, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-46, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   MEDLINE=88135764; PubMed=3257719; DOI=10.1016/0092-8674(88)90462-X;
RA   Abraham C.R., Selkoe D.J., Potter H.;
RT   "Immunochemical identification of the serine protease inhibitor alpha
RT   1-antichymotrypsin in the brain amyloid deposits of Alzheimer's
RT   disease.";
RL   Cell 52:487-501(1988).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 17-423 (ISOFORM 1), AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Hippocampus;
RX   MEDLINE=99098931; PubMed=9880565; DOI=10.1074/jbc.274.3.1821;
RA   Hwang S.-R., Steineckert B., Kohn A., Palkovits M., Hook V.Y.H.;
RT   "Molecular studies define the primary structure of alpha1-
RT   antichymotrypsin (ACT) protease inhibitor in Alzheimer's disease
RT   brains. Comparison of act in hippocampus and liver.";
RL   J. Biol. Chem. 274:1821-1827(1999).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-86 AND 130-423 (ISOFORM 1).
RA   Rubin H.;
RL   Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   PROTEIN SEQUENCE OF 24-34.
RX   MEDLINE=89323223; PubMed=2787670; DOI=10.1016/0167-4838(89)90139-8;
RA   Lindmark B., Hilja H., Alan R., Eriksson S.;
RT   "The microheterogeneity of desialylated alpha 1-antichymotrypsin: the
RT   occurrence of two amino-terminal isoforms, one lacking a His-Pro
RT   dipeptide.";
RL   Biochim. Biophys. Acta 997:90-95(1989).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 36-45.
RX   MEDLINE=94354957; PubMed=7521171;
RA   Korzus E., Luisetti M., Travis J.;
RT   "Interactions of alpha-1-antichymotrypsin, alpha-1-proteinase
RT   inhibitor, and alpha-2-macroglobulin with the fungal enzyme,
RT   seaprose.";
RL   Biol. Chem. Hoppe-Seyler 375:335-341(1994).
RN   [12]
RP   PROTEIN SEQUENCE OF 41-60.
RX   MEDLINE=83178256; PubMed=6687683; DOI=10.1016/0006-291X(83)90325-X;
RA   Morii M., Travis J.;
RT   "Structural alterations in alpha 1-antichymotrypsin from normal and
RT   acute phase human plasma.";
RL   Biochem. Biophys. Res. Commun. 111:438-443(1983).
RN   [13]
RP   PROTEIN SEQUENCE OF 48-68 (ISOFORMS 1/2).
RX   MEDLINE=96216555; PubMed=8647626;
RX   DOI=10.1002/(SICI)1097-0215(19960529)66:5<636::AID-IJC10>3.0.CO;2-2;
RA   Pinczower G.D., Williams R.P.W., Gianello R.D., Robinson H.C.,
RA   Preston B.N., Linnane A.W.;
RT   "Characterisation of the tumour-associated carbohydrate epitope
RT   recognised by monoclonal antibody 4D3.";
RL   Int. J. Cancer 66:636-644(1996).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 87-129 (ISOFORMS 1/2), AND FUNCTION.
RC   TISSUE=Liver;
RX   MEDLINE=90110106; PubMed=2404007;
RA   Rubin H., Wang Z., Nickbarg E.B., McLarney S., Naidoo N.,
RA   Schoenberger O.L., Johnson J.L., Cooperman B.S.;
RT   "Cloning, expression, purification, and biological activity of
RT   recombinant native and variant human alpha 1-antichymotrypsins.";
RL   J. Biol. Chem. 265:1199-1207(1990).
RN   [15]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 205-423.
RX   MEDLINE=84295637; PubMed=6547997; DOI=10.1038/311175a0;
RA   Hill R.E., Shaw P.H., Boyd P.A., Baumann H., Hastie N.D.;
RT   "Plasma protease inhibitors in mouse and man: divergence within the
RT   reactive centre regions.";
RL   Nature 311:175-177(1984).
RN   [16]
RP   ACTIVE SITE.
RX   MEDLINE=84032476; PubMed=6556193;
RA   Morii M., Travis J.;
RT   "Amino acid sequence at the reactive site of human alpha 1-
RT   antichymotrypsin.";
RL   J. Biol. Chem. 258:12749-12752(1983).
RN   [17]
RP   GLYCOSYLATION AT ASN-93 AND ASN-106.
RX   MEDLINE=22660472; PubMed=12754519; DOI=10.1038/nbt827;
RA   Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT   "Identification and quantification of N-linked glycoproteins using
RT   hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL   Nat. Biotechnol. 21:660-666(2003).
RN   [18]
RP   INTERACTION WITH DNAJC1.
RX   PubMed=14668352; DOI=10.1074/jbc.M310903200;
RA   Kroczynska B., Evangelista C.M., Samant S.S., Elguindi E.C.,
RA   Blond S.Y.;
RT   "The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human
RT   homologue interacts with alpha1-antichymotrypsin and kinetically
RT   interferes with its serpin inhibitory activity.";
RL   J. Biol. Chem. 279:11432-11443(2004).
RN   [19]
RP   REGION RCL.
RX   PubMed=15638460; DOI=10.1007/s00239-004-2640-9;
RA   Horvath A.J., Forsyth S.L., Coughlin P.B.;
RT   "Expression patterns of murine antichymotrypsin-like genes reflect
RT   evolutionary divergence at the Serpina3 locus.";
RL   J. Mol. Evol. 59:488-497(2004).
RN   [20]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93, AND MASS SPECTROMETRY.
RC   TISSUE=Plasma;
RX   PubMed=14760718; DOI=10.1002/pmic.200300556;
RA   Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT   "Screening for N-glycosylated proteins by liquid chromatography mass
RT   spectrometry.";
RL   Proteomics 4:454-465(2004).
RN   [21]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-93; ASN-106;
RP   ASN-127; ASN-186 AND ASN-271, AND MASS SPECTROMETRY.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-423.
RX   MEDLINE=91202538; PubMed=2016749; DOI=10.1016/0022-2836(91)90704-A;
RA   Baumann U., Huber R., Bode W., Grosse D., Lesjak M., Laurell C.-B.;
RT   "Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7-A
RT   resolution and its comparison with other serpins.";
RL   J. Mol. Biol. 218:595-606(1991).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370
RP   AND ARG-372.
RX   MEDLINE=96433079; PubMed=8836107; DOI=10.1038/nsb1096-888;
RA   Lukacs C.M., Zhong J.Q., Plotnick M.I., Rubin H., Cooperman B.S.,
RA   Christianson D.W.;
RT   "Arginine substitutions in the hinge region of antichymotrypsin affect
RT   serpin beta-sheet rearrangement.";
RL   Nat. Struct. Biol. 3:888-893(1996).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370;
RP   ARG-372 AND ARG-374.
RX   MEDLINE=98198038; PubMed=9521649; DOI=10.1021/bi972359e;
RA   Lukacs C.M., Rubin H., Christianson D.W.;
RT   "Engineering an anion-binding cavity in antichymotrypsin modulates the
RT   'spring-loaded' serpin-protease interaction.";
RL   Biochemistry 37:3297-3304(1998).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 26-423.
RX   MEDLINE=20087203; PubMed=10618372; DOI=10.1073/pnas.97.1.67;
RA   Gooptu B., Hazes B., Chang W.-S.W., Dafforn T.R., Carrell R.W.,
RA   Read R.J., Lomas D.A.;
RT   "Inactive conformation of the serpin alpha(1)-antichymotrypsin
RT   indicates two-stage insertion of the reactive loop: implications for
RT   inhibitory function and conformational disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:67-72(2000).
RN   [26]
RP   VARIANT ISEHARA-1 VAL-401.
RX   MEDLINE=92316200; PubMed=1618300; DOI=10.1016/0014-5793(92)80590-D;
RA   Tsuda M., Sei Y., Yamamura M., Yamamoto M., Shinohara Y.;
RT   "Detection of a new mutant alpha-1-antichymotrypsin in patients with
RT   occlusive-cerebrovascular disease.";
RL   FEBS Lett. 304:66-68(1992).
RN   [27]
RP   VARIANT BONN-1 ALA-252.
RX   MEDLINE=92292844; PubMed=1351206; DOI=10.1016/0140-6736(92)91301-N;
RA   Poller W., Faber J.-P., Scholz S., Weindinger S., Bartholome K.,
RA   Olek K., Eriksson S.;
RT   "Mis-sense mutation of alpha 1-antichymotrypsin gene associated with
RT   chronic lung disease.";
RL   Lancet 339:1538-1538(1992).
RN   [28]
RP   VARIANT VAL-401.
RX   PubMed=11289720; DOI=10.1007/s100380170125;
RA   Tachikawa H., Tsuda M., Onoe K., Ueno M., Takagi S., Shinohara Y.;
RT   "Alpha-1-antichymotrypsin gene A1252G variant (ACT Isehara-1) is
RT   associated with a lacunar type of ischemic cerebrovascular disease.";
RL   J. Hum. Genet. 46:45-47(2001).
CC   -!- FUNCTION: Although its physiological function is unclear, it can
CC       inhibit neutrophil cathepsin G and mast cell chymase, both of
CC       which can convert angiotensin-1 to the active angiotensin-2.
CC   -!- SUBUNIT: Interacts with DNAJC1.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P01011-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P01011-2; Sequence=VSP_014227, VSP_014228;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=P01011-3; Sequence=VSP_014225, VSP_014226;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Plasma. Synthesized in the liver. Like the
CC       related alpha-1-antitrypsin, its concentration increases in the
CC       acute phase of inflammation or infection. Found in the myloid
CC       plaques from the hippocampus of Alzheimer's disease brains.
CC   -!- DOMAIN: The reactive center loop (RCL) extends out from the body
CC       of the protein and directs binding to the target protease. The
CC       protease cleaves the serpin at the reactive site within the RCL,
CC       establishing a covalent linkage between the carboxyl group of the
CC       serpin reactive site and the serine hydroxyl of the protease. The
CC       resulting inactive serpin-protease complex is highly stable.
CC   -!- DISEASE: Defects in SERPINA3 may be a cause of chronic obstructive
CC       pulmonary disease (COPD) [MIM:107280].
CC   -!- MISCELLANEOUS: Alpha-1-antichymotrypsin can bind DNA.
CC   -!- SIMILARITY: Belongs to the serpin family.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA51543.1; Type=Frameshift; Positions=101, 106, 111, 117, 123, 129, 421;
CC       Sequence=AAT08029.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=AAT08029.1; Type=Frameshift; Positions=4;
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Alpha-1 antichymotrypsin entry;
CC       URL="http://en.wikipedia.org/wiki/Alpha_1-antichymotrypsin";
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DR   EMBL; K01500; AAA51543.1; ALT_FRAME; mRNA.
DR   EMBL; X68733; CAA48671.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X68734; CAA48671.1; JOINED; Genomic_DNA.
DR   EMBL; X68735; CAA48671.1; JOINED; Genomic_DNA.
DR   EMBL; X68736; CAA48671.1; JOINED; Genomic_DNA.
DR   EMBL; X68737; CAA48671.1; JOINED; Genomic_DNA.
DR   EMBL; AY513275; AAT08028.1; -; mRNA.
DR   EMBL; AY513276; AAT08029.1; ALT_SEQ; mRNA.
DR   EMBL; AK123091; BAG53869.1; -; mRNA.
DR   EMBL; AB209060; BAD92297.1; ALT_INIT; mRNA.
DR   EMBL; BC003559; AAH03559.3; -; mRNA.
DR   EMBL; BC010530; AAH10530.1; -; mRNA.
DR   EMBL; BC013189; AAH13189.1; -; mRNA.
DR   EMBL; BC034554; AAH34554.1; -; mRNA.
DR   EMBL; BC070265; AAH70265.1; -; mRNA.
DR   EMBL; M18906; AAA51559.1; -; mRNA.
DR   EMBL; AF089747; AAD08810.1; -; mRNA.
DR   EMBL; J05176; AAA51560.1; -; mRNA.
DR   EMBL; X00947; CAA25459.1; -; Genomic_DNA.
DR   IPI; IPI00550991; -.
DR   IPI; IPI00607870; -.
DR   IPI; IPI00847635; -.
DR   PIR; A90475; ITHUC.
DR   PIR; S62374; S62374.
DR   RefSeq; NP_001076.2; -.
DR   UniGene; Hs.534293; -.
DR   UniGene; Hs.653605; -.
DR   PDB; 1AS4; X-ray; 2.10 A; A=43-383, B=387-423.
DR   PDB; 1QMN; X-ray; 2.27 A; A=26-423.
DR   PDB; 2ACH; X-ray; 2.70 A; A=24-383, B=384-423.
DR   PDB; 3CAA; X-ray; 2.40 A; A=43-383, B=387-423.
DR   PDB; 4CAA; X-ray; 2.90 A; A=43-383, B=387-423.
DR   PDBsum; 1AS4; -.
DR   PDBsum; 1QMN; -.
DR   PDBsum; 2ACH; -.
DR   PDBsum; 3CAA; -.
DR   PDBsum; 4CAA; -.
DR   IntAct; P01011; 1.
DR   MEROPS; I04.002; -.
DR   GlycoSuiteDB; P01011; -.
DR   PhosphoSite; P01011; -.
DR   SWISS-2DPAGE; P01011; -.
DR   DOSAC-COBS-2DPAGE; P01011; -.
DR   Siena-2DPAGE; P01011; -.
DR   PRIDE; P01011; -.
DR   Ensembl; ENSG00000196136; Homo sapiens.
DR   GeneID; 12; -.
DR   KEGG; hsa:12; -.
DR   GeneCards; GC14P094148; -.
DR   H-InvDB; HIX0011931; -.
DR   H-InvDB; HIX0079611; -.
DR   HGNC; HGNC:16; SERPINA3.
DR   HPA; CAB016647; -.
DR   HPA; HPA002560; -.
DR   MIM; 107280; gene.
DR   PharmGKB; PA35020; -.
DR   HOVERGEN; P01011; -.
DR   LinkHub; P01011; -.
DR   NextBio; 23; -.
DR   ArrayExpress; P01011; -.
DR   Bgee; P01011; -.
DR   GermOnline; ENSG00000196136; Homo sapiens.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR   GO; GO:0030569; F:chymotrypsin inhibitor activity; NAS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; NAS:UniProtKB.
DR   InterPro; IPR000215; Protease_inhib_I4_serpin.
DR   PANTHER; PTHR11461; Prot_inh_serpin; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acute phase; Alternative splicing;
KW   Direct protein sequencing; Disease mutation; Glycoprotein;
KW   Polymorphism; Protease inhibitor; Secreted; Serine protease inhibitor;
KW   Signal.
FT   SIGNAL        1     23
FT   CHAIN        24    423       Alpha-1-antichymotrypsin.
FT                                /FTId=PRO_0000032411.
FT   CHAIN        26    423       Alpha-1-antichymotrypsin His-Pro-less.
FT                                /FTId=PRO_0000032412.
FT   DNA_BIND    235    237
FT   REGION      369    394       RCL.
FT   SITE        383    384       Reactive bond.
FT   CARBOHYD     33     33       N-linked (GlcNAc...).
FT   CARBOHYD     93     93       N-linked (GlcNAc...).
FT   CARBOHYD    106    106       N-linked (GlcNAc...).
FT   CARBOHYD    127    127       N-linked (GlcNAc...).
FT   CARBOHYD    186    186       N-linked (GlcNAc...).
FT   CARBOHYD    271    271       N-linked (GlcNAc...).
FT   VAR_SEQ      64     95       LVLKAPDKNVIFSPLSISTALAFLSLGAHNTT -> SPRWS
FT                                IRLCLMYLRRAQKHLLPQQSKSPSFLH (in isoform
FT                                3).
FT                                /FTId=VSP_014225.
FT   VAR_SEQ      96    423       Missing (in isoform 3).
FT                                /FTId=VSP_014226.
FT   VAR_SEQ     215    216       AK -> ER (in isoform 2).
FT                                /FTId=VSP_014227.
FT   VAR_SEQ     217    423       Missing (in isoform 2).
FT                                /FTId=VSP_014228.
FT   VARIANT       9      9       A -> T (in dbSNP:rs4934).
FT                                /FTId=VAR_006973.
FT   VARIANT      78     78       L -> P (in COPD; Bochum-1;
FT                                dbSNP:rs1800463).
FT                                /FTId=VAR_006974.
FT   VARIANT     167    167       A -> G.
FT                                /FTId=VAR_006975.
FT   VARIANT     252    252       P -> A (in COPD; Bonn-1; dbSNP:rs17473).
FT                                /FTId=VAR_006976.
FT   VARIANT     267    267       K -> R (in dbSNP:rs17853314).
FT                                /FTId=VAR_037902.
FT   VARIANT     401    401       M -> V (associated with occlusive-
FT                                cerebrovascular disease; Isehara-1).
FT                                /FTId=VAR_006977.
FT   VARIANT     407    407       D -> G (in dbSNP:rs10956).
FT                                /FTId=VAR_011742.
FT   CONFLICT     55     55       D -> S (in Ref. 12; AA sequence).
FT   CONFLICT     69     69       P -> L (in Ref. 1; AAA51543).
FT   CONFLICT    101    101       K -> R (in Ref. 5; BAD92297).
FT   CONFLICT    106    106       N -> Y (in Ref. 3; AAT08028).
FT   CONFLICT    198    198       D -> N (in Ref. 3; AAT08029).
FT   CONFLICT    199    199       L -> P (in Ref. 1; AAA51543).
FT   CONFLICT    234    234       S -> N (in Ref. 3; AAT08029).
FT   CONFLICT    339    339       S -> G (in Ref. 3; AAT08028).
FT   CONFLICT    346    346       I -> S (in Ref. 3; AAT08028).
FT   CONFLICT    361    363       AVL -> VVS (in Ref. 1; AAA51543).
FT   HELIX        49     67
FT   STRAND       73     75
FT   HELIX        77     88
FT   HELIX        93    102
FT   TURN        107    109
FT   HELIX       112    126
FT   STRAND      134    144
FT   HELIX       151    161
FT   STRAND      164    168
FT   HELIX       173    187
FT   TURN        188    190
FT   STRAND      203    219
FT   HELIX       223    225
FT   STRAND      227    234
FT   STRAND      237    256
FT   TURN        257    260
FT   STRAND      261    279
FT   HELIX       284    289
FT   HELIX       293    302
FT   STRAND      304    314
FT   STRAND      316    323
FT   HELIX       325    330
FT   HELIX       335    337
FT   HELIX       344    347
FT   STRAND      348    350
FT   STRAND      352    365
FT   STRAND      367    382
FT   STRAND      391    394
FT   STRAND      399    405
FT   STRAND      412    418
SQ   SEQUENCE   423 AA;  47651 MW;  B002F946C86A8951 CRC64;
     MERMLPLLAL GLLAAGFCPA VLCHPNSPLD EENLTQENQD RGTHVDLGLA SANVDFAFSL
     YKQLVLKAPD KNVIFSPLSI STALAFLSLG AHNTTLTEIL KGLKFNLTET SEAEIHQSFQ
     HLLRTLNQSS DELQLSMGNA MFVKEQLSLL DRFTEDAKRL YGSEAFATDF QDSAAAKKLI
     NDYVKNGTRG KITDLIKDLD SQTMMVLVNY IFFKAKWEMP FDPQDTHQSR FYLSKKKWVM
     VPMMSLHHLT IPYFRDEELS CTVVELKYTG NASALFILPD QDKMEEVEAM LLPETLKRWR
     DSLEFREIGE LYLPKFSISR DYNLNDILLQ LGIEEAFTSK ADLSGITGAR NLAVSQVVHK
     AVLDVFEEGT EASAATAVKI TLLSALVETR TIVRFNRPFL MIIVPTDTQN IFFMSKVTNP
     KQA
//
ID   ACTA_STRPU              Reviewed;         376 AA.
AC   P53472;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-NOV-2008, entry version 46.
DE   RecName: Full=Actin, cytoskeletal 1A;
DE   AltName: Full=Actin, cytoskeletal IA;
GN   Name=CYIA;
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa;
OC   Echinoidea; Euechinoidea; Echinacea; Echinoida; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=83192079; PubMed=6302475;
RA   Schuler M.A., McOsker P., Keller E.B.;
RT   "DNA sequence of two linked actin genes of sea urchin.";
RL   Mol. Cell. Biol. 3:448-456(1983).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC   -!- SIMILARITY: Belongs to the actin family.
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DR   EMBL; J01168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   HSSP; P02570; 1HLU.
DR   SMR; P53472; 5-372.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR004000; Actin_like.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   3: Inferred from homology;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding.
FT   PROPEP        1      2       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000722.
FT   CHAIN         3    376       Actin, cytoskeletal 1A.
FT                                /FTId=PRO_0000000723.
FT   MOD_RES       3      3       N-acetylaspartate (By similarity).
FT   UNSURE       54     54
FT   UNSURE      235    235
FT   UNSURE      236    236
FT   UNSURE      240    240
FT   UNSURE      304    304
SQ   SEQUENCE   376 AA;  41849 MW;  E379184F832D1820 CRC64;
     MCDDDVAALV IDNGSGMVKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PMEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
     TQIMFETFNS PAMYVAIQAV LSLYASGRTT GIVFDSGDGV SHTVPIYEGY ALPHAILRLD
     LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMQT AASSSSLEKS
     YELPDGQVIT IGNERFRCPE ALFQPAFLGM ESAGIHETCY NSIMKCDVDI RKDLYANTVL
     SGGSTMFPGI ADRMQKEITA LAPPTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDESGPSI VHRKCF
//
ID   AGRIN_CHICK             Reviewed;        2073 AA.
AC   P31696; Q90609; Q90685;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   10-FEB-2009, entry version 92.
DE   RecName: Full=Agrin;
DE   Flags: Precursor;
GN   Name=AGRN; Synonyms=AGRIN;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-221 (ISOFORMS 1 AND 6), GLYCOSYLATION,
RP   INTERACTION WITH LAMININ, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Spinal cord;
RX   MEDLINE=96101933; PubMed=8522611; DOI=10.1083/jcb.131.6.1547;
RA   Denzer A.J., Gesemann M., Schumacher B., Rueegg M.A.;
RT   "An amino-terminal extension is required for the secretion of chick
RT   agrin and its binding to extracellular matrix.";
RL   J. Cell Biol. 131:1547-1560(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 94-2073 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=92232297; PubMed=1314620; DOI=10.1016/0896-6273(92)90089-V;
RA   Tsim K.W.K., Rueegg M.A., Escher G., Kroeger S., McMahan U.J.;
RT   "cDNA that encodes active agrin.";
RL   Neuron 8:677-689(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1901-1913 (ISOFORMS 4 AND 5).
RC   STRAIN=White leghorn;
RX   MEDLINE=93345745; PubMed=8393816; DOI=10.1006/dbio.1993.1210;
RA   Thomas W.S., O'Dowd D.K., Smith M.A.;
RT   "Developmental expression and alternative splicing of chick agrin
RT   RNA.";
RL   Dev. Biol. 158:523-535(1993).
RN   [4]
RP   ALTERNATIVE SPLICING.
RX   MEDLINE=92232298; PubMed=1314621; DOI=10.1016/0896-6273(92)90090-Z;
RA   Rueegg M.A., Tsim K.W.K., Horton S.E., Kroeger S., Escher G.,
RA   Gensch E.M., McMahan U.J.;
RT   "The agrin gene codes for a family of basal lamina proteins that
RT   differ in function and distribution.";
RL   Neuron 8:691-699(1992).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 26-156 IN COMPLEX WITH
RP   LAMININ, AND DISULFIDE BOND.
RX   PubMed=11473262; DOI=10.1038/90422;
RA   Stetefeld J., Jenny M., Schulthess T., Landwehr R., Schumacher B.,
RA   Frank S., Rueegg M.A., Engel J., Kammerer R.A.;
RT   "The laminin-binding domain of agrin is structurally related to N-
RT   TIMP-1.";
RL   Nat. Struct. Biol. 8:705-709(2001).
RN   [6]
RP   STRUCTURE BY NMR OF 1870-2073 IN COMPLEX WITH CALCIUM IONS, X-RAY
RP   CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 1870-2073 IN COMPLEX WITH CALCIUM
RP   IONS, AND DISULFIDE BOND.
RX   PubMed=15016366; DOI=10.1016/j.str.2004.02.001;
RA   Stetefeld J., Alexandrescu A.T., Maciejewski M.W., Jenny M.,
RA   Rathgeb-Szabo K., Schulthess T., Landwehr R., Frank S., Rueegg M.A.,
RA   Kammerer R.A.;
RT   "Modulation of agrin function by alternative splicing and Ca2+
RT   binding.";
RL   Structure 12:503-515(2004).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-156, INTERACTION WITH
RP   LAMININ, AND DISULFIDE BOND.
RX   PubMed=15694127; DOI=10.1016/j.matbio.2004.11.003;
RA   Mascarenhas J.B., Rueegg M.A., Sasaki T., Eble J.A., Engel J.,
RA   Stetefeld J.;
RT   "Structure and laminin-binding specificity of the NtA domain expressed
RT   in eukaryotic cells.";
RL   Matrix Biol. 23:507-513(2005).
CC   -!- FUNCTION: Component of the basal lamina that causes the
CC       aggregation of acetylcholine receptors and acetylcholine-esterase
CC       on the surface of muscle fibers of the neuromuscular junction.
CC   -!- SUBUNIT: Binds to laminin.
CC   -!- INTERACTION:
CC       Q70E31:DAG1; NbExp=1; IntAct=EBI-457650, EBI-457683;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix. Note=Synaptic basal lamina at the neuromuscular junction.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC         Comment=Additional isoforms seem to exist. Isoforms differ in
CC         their acetylcholine receptor clustering activity;
CC       Name=1;
CC         IsoId=P31696-1; Sequence=Displayed;
CC       Name=2; Synonyms=Agrin-related protein 1;
CC         IsoId=P31696-2; Sequence=VSP_001370;
CC       Name=3; Synonyms=Agrin-related protein 2;
CC         IsoId=P31696-3; Sequence=VSP_001369, VSP_001370;
CC       Name=4;
CC         IsoId=P31696-4; Sequence=VSP_012543;
CC       Name=5;
CC         IsoId=P31696-5; Sequence=VSP_012543, VSP_001370;
CC       Name=6;
CC         IsoId=P31696-6; Sequence=VSP_020095;
CC   -!- TISSUE SPECIFICITY: Detected in embryonic brain, spinal cord,
CC       skeletal muscle, vitreous humor and liver (at protein level).
CC   -!- PTM: Contains heparan sulfate chains as well as N-linked and O-
CC       linked oligosaccharides.
CC   -!- SIMILARITY: Contains 4 EGF-like domains.
CC   -!- SIMILARITY: Contains 9 Kazal-like domains.
CC   -!- SIMILARITY: Contains 2 laminin EGF-like domains.
CC   -!- SIMILARITY: Contains 3 laminin G-like domains.
CC   -!- SIMILARITY: Contains 1 NtA (N-terminal agrin) domain.
CC   -!- SIMILARITY: Contains 1 SEA domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA48585.1; Type=Frameshift; Positions=110;
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DR   EMBL; U35613; AAC59740.1; -; mRNA.
DR   EMBL; M94271; AAA48585.1; ALT_FRAME; mRNA.
DR   EMBL; M97371; AAA48586.1; -; mRNA.
DR   EMBL; M97372; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; U07271; AAA16788.1; -; mRNA.
DR   IPI; IPI00579891; -.
DR   IPI; IPI00590466; -.
DR   IPI; IPI00592771; -.
DR   IPI; IPI00597536; -.
DR   IPI; IPI00603573; -.
DR   IPI; IPI00786263; -.
DR   PIR; JH0591; AGCH.
DR   RefSeq; NP_990858.1; -.
DR   UniGene; Gga.4448; -.
DR   PDB; 1JB3; X-ray; 1.60 A; A=26-156.
DR   PDB; 1JC7; X-ray; 2.73 A; A=26-156.
DR   PDB; 1PXU; X-ray; 2.20 A; A=25-155.
DR   PDB; 1PZ7; X-ray; 1.42 A; A/B=1870-2073.
DR   PDB; 1PZ8; X-ray; 2.35 A; A/B/C/D=1870-2073.
DR   PDB; 1PZ9; X-ray; 2.80 A; A/B=1870-2073.
DR   PDB; 1Q56; NMR; -; A=1870-2073.
DR   PDBsum; 1JB3; -.
DR   PDBsum; 1JC7; -.
DR   PDBsum; 1PXU; -.
DR   PDBsum; 1PZ7; -.
DR   PDBsum; 1PZ8; -.
DR   PDBsum; 1PZ9; -.
DR   PDBsum; 1Q56; -.
DR   IntAct; P31696; 1.
DR   PRIDE; P31696; -.
DR   Ensembl; ENSGALG00000002041; Gallus gallus.
DR   GeneID; 396538; -.
DR   KEGG; gga:396538; -.
DR   HOVERGEN; P31696; -.
DR   GO; GO:0005605; C:basal lamina; IEA:InterPro.
DR   GO; GO:0043236; F:laminin binding; IEA:InterPro.
DR   GO; GO:0007213; P:acetylcholine receptor signaling, muscarini...; IEA:InterPro.
DR   GO; GO:0043113; P:receptor clustering; IEA:InterPro.
DR   InterPro; IPR004850; Agrin_NtA.
DR   InterPro; IPR013320; ConA_like_subgrp.
DR   InterPro; IPR006210; EGF.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR002049; EGF_laminin.
DR   InterPro; IPR006209; EGF_like.
DR   InterPro; IPR013032; EGF_like_reg_CS.
DR   InterPro; IPR003645; Fol_N.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR012679; Laminin_G_1.
DR   InterPro; IPR002350; Prot_inh_Kazal.
DR   InterPro; IPR000082; SEA.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 3.
DR   Pfam; PF00008; EGF; 4.
DR   Pfam; PF00050; Kazal_1; 9.
DR   Pfam; PF00053; Laminin_EGF; 2.
DR   Pfam; PF00054; Laminin_G_1; 3.
DR   Pfam; PF03146; NtA; 1.
DR   Pfam; PF01390; SEA; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00180; EGF_Lam; 2.
DR   SMART; SM00274; FOLN; 6.
DR   SMART; SM00280; KAZAL; 9.
DR   SMART; SM00282; LamG; 3.
DR   SMART; SM00200; SEA; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 2.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR   PROSITE; PS51121; NTA; 1.
DR   PROSITE; PS50024; SEA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Heparan sulfate;
KW   Laminin EGF-like domain; Proteoglycan; Repeat; Secreted; Signal.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25   2073       Agrin.
FT                                /FTId=PRO_0000055624.
FT   DOMAIN       25    159       NtA.
FT   DOMAIN      172    244       Kazal-like 1.
FT   DOMAIN      248    319       Kazal-like 2.
FT   DOMAIN      320    391       Kazal-like 3.
FT   DOMAIN      394    462       Kazal-like 4.
FT   DOMAIN      468    536       Kazal-like 5.
FT   DOMAIN      537    601       Kazal-like 6.
FT   DOMAIN      602    666       Kazal-like 7.
FT   DOMAIN      669    751       Kazal-like 8.
FT   DOMAIN      793    846       Laminin EGF-like 1.
FT   DOMAIN      847    893       Laminin EGF-like 2.
FT   DOMAIN      899    969       Kazal-like 9.
FT   DOMAIN     1144   1266       SEA.
FT   DOMAIN     1347   1383       EGF-like 1.
FT   DOMAIN     1388   1563       Laminin G-like 1.
FT   DOMAIN     1564   1601       EGF-like 2.
FT   DOMAIN     1603   1640       EGF-like 3.
FT   DOMAIN     1650   1831       Laminin G-like 2.
FT   DOMAIN     1832   1870       EGF-like 4.
FT   DOMAIN     1894   2070       Laminin G-like 3.
FT   CA_BIND    1945   2014
FT   COMPBIAS    974   1113       Ser/Thr-rich.
FT   COMPBIAS   1268   1337       Ser/Thr-rich.
FT   CARBOHYD    130    130       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    508    508       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    777    777       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    882    882       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    932    932       N-linked (GlcNAc...) (Potential).
FT   DISULFID     26     98
FT   DISULFID    204    223       Potential.
FT   DISULFID    212    244       Potential.
FT   DISULFID    278    298       Potential.
FT   DISULFID    287    319       Potential.
FT   DISULFID    351    370       Potential.
FT   DISULFID    359    391       Potential.
FT   DISULFID    422    441       Potential.
FT   DISULFID    430    462       Potential.
FT   DISULFID    496    515       Potential.
FT   DISULFID    504    536       Potential.
FT   DISULFID    561    580       Potential.
FT   DISULFID    569    601       Potential.
FT   DISULFID    625    645       Potential.
FT   DISULFID    634    666       Potential.
FT   DISULFID    710    730       Potential.
FT   DISULFID    719    751       Potential.
FT   DISULFID    793    805       By similarity.
FT   DISULFID    795    812       By similarity.
FT   DISULFID    814    823       By similarity.
FT   DISULFID    826    844       By similarity.
FT   DISULFID    847    859       By similarity.
FT   DISULFID    849    866       By similarity.
FT   DISULFID    868    877       By similarity.
FT   DISULFID    880    891       By similarity.
FT   DISULFID    928    948       Potential.
FT   DISULFID    937    969       Potential.
FT   DISULFID   1351   1362       By similarity.
FT   DISULFID   1356   1371       By similarity.
FT   DISULFID   1373   1382       By similarity.
FT   DISULFID   1568   1579       By similarity.
FT   DISULFID   1573   1589       By similarity.
FT   DISULFID   1591   1600       By similarity.
FT   DISULFID   1607   1618       By similarity.
FT   DISULFID   1612   1628       By similarity.
FT   DISULFID   1630   1639       By similarity.
FT   DISULFID   1836   1849       By similarity.
FT   DISULFID   1843   1858       By similarity.
FT   DISULFID   1860   1869       By similarity.
FT   DISULFID   2044   2070
FT   VAR_SEQ     150    156       Missing (in isoform 6).
FT                                /FTId=VSP_020095.
FT   VAR_SEQ    1766   1769       Missing (in isoform 3).
FT                                /FTId=VSP_001369.
FT   VAR_SEQ    1901   1901       S -> SHLSNEIPA (in isoform 4 and isoform
FT                                5).
FT                                /FTId=VSP_012543.
FT   VAR_SEQ    1902   1912       Missing (in isoform 2, isoform 3 and
FT                                isoform 5).
FT                                /FTId=VSP_001370.
FT   CONFLICT   1247   1249       RTI -> SIL (in Ref. 2; AAA48586).
FT   HELIX        31     36
FT   STRAND       39     53
FT   TURN         54     57
FT   STRAND       58     70
FT   HELIX        72     78
FT   TURN         83     85
FT   STRAND       86     92
FT   STRAND      107    114
FT   HELIX       117    119
FT   TURN        120    125
FT   STRAND      126    129
FT   HELIX       138    152
FT   STRAND     1879   1881
FT   STRAND     1884   1889
FT   STRAND     1892   1895
FT   STRAND     1914   1927
FT   STRAND     1930   1938
FT   STRAND     1946   1952
FT   STRAND     1955   1964
FT   STRAND     1967   1974
FT   STRAND     1977   1979
FT   STRAND     1981   1988
FT   STRAND     1991   1996
FT   STRAND     2002   2005
FT   STRAND     2013   2015
FT   STRAND     2018   2023
FT   TURN       2029   2032
FT   HELIX      2035   2038
FT   STRAND     2042   2050
FT   TURN       2057   2059
SQ   SEQUENCE   2073 AA;  224118 MW;  6E67129075A4E130 CRC64;
     MGGSGAAATL ALGLALGLAL GGWANCPERE LQRREEEANV VLTGTVEEIM NVDPVHHTYS
     CKVRVWRYLK GKDIVTHEIL LDGGNKVVIG GFGDPLICDN QVSTGDTRIF FVNPAPQYMW
     PAHRNELMLN SSLMRITLRN LEEVEHCVEE HRKLLADKPN SYFTQTPPTP RDACRGMLCG
     FGAVCERSPT DPSQASCVCK KTACPVVVAP VCGSDYSTYS NECELEKAQC NQQRRIKVIS
     KGPCGSKDPC AEVTCSFGST CVRSADGQTA GCVCPASCSG VAESIVCGSD GKDYRSECDL
     NKHACDKQEN VFKKFDGACD PCKGILNDMN RVCRVNPRTR RVELLSRPEN CPSKREPVCG
     DDGVTYASEC VMGRTGAIRG LEIQKVRSGQ CQHQDKCKDE CKFNAVCLKR WHARCSCDRI
     TCDGTYRPVC ARDSRTYSND CERQKAECHQ KAAIPVKHSG PCDLGTPSPC LSVECTFGAT
     CVVKNREPVC ECQQVCQGRY DPVCGSDNRT YGNPCELNAM ACVLKREIRV KHKGPCDRCG
     KCQFGAICEA ETGRCVCPTE CVPSSQPVCG TDGNTYGSEC ELHVRACTQQ KNILVAAQGD
     CKSCGTTVCS FGSTCVGGQC VCPRCEQQPL AQVCGTDGLT YDNRCELRAA SCQQQKSIEV
     AKMGPCEDEC GSGGSGSGDG SECEQDRCRH YGGWWDEDAE DDRCVCDFTC LAVPRSPVCG
     SDDVTYANEC ELKKTRCEKR QNLYVTSQGA CRALTTTPPP LPVVHCSQTI YGCCPDNMTL
     ALGVGAAGCP STCQCNPYGS YGGTCDPATG QCSCKPGVGG LKCDRCEPGF WNFRGIVTDS
     KSGCTPCNCD PVGSVRDDCE QMTGLCSCKT GITGMKCNQC PNGSKMGMAG CEKDPSAPKS
     CEEMSCEFGA TCVEVNGFAH CECPSPLCSE ANMTKVCGSD GVTYGDQCQL KTIACRQGQL
     ITVKHVGQCH ESITHTSHTM PPTPLPTLPL DKLIVPPPLQ LTTQAPEPTE LATTSLLMEA
     SPTTRSHPTT RRVTTTRPVT TPWMTHGVLK TTVRPLSTSP VVLATTQPPY AESGSAEGSG
     DQEMSISGDQ ESSGAGSAGE EEVEESQVTP TPAIERATCY NTPLGCCSDG KTAAADAEGS
     NCPATKVFQG VLILEEVEGQ ELFYTPEMAD PKSELFGETA RSIESALDEL FRNSDVKNDF
     KSIRVRDLGQ SSAVRVIVES HFDPATSYTA ADVQAASLKQ IRASKKRTIL VKKPQQEHVK
     FMDFDWIPRI FTTTITTTTA TTMAPATTRR HTTASAATTA HILRQDTVGH PSAKLAAPAS
     TRRPTSTLPT TARRKPTRQP PSTTKKPSRP CDSHPCLHGG TCEDDGREFT CRCPAGKGGA
     VCEKPIRYFI PSFGGKSYLA FKMMKAYHTV RIAMEFRATE LSGLLLYNGQ NRGKDFISLA
     LVGGFVELRF NTGSGTGVIT SKVRVEPGKW HQLVVNRNRR SGMLAVDGEH VSGESPTGTD
     GLNLDTDLFV GGAPEDQMAV VAERTAATVG LKGSIRLLDV NNQMYDLREK GSDVLYGSGV
     GECGNDPCHP NPCHHGASCH VKEAEMFHCE CLHSYTGPTC ADERNPCDPT PCHISATCLV
     LPEGGAMCAC PMGREGEFCE RVTEQDHTMP FLPEFNGFSY LELNGLQTLF LTCRQMSMEV
     VFLAKSPSGM IFYNGQKTDG KGDFVSLALH DGYLEYRYDL GKGAAVLRSK EPVPLNTWIS
     VLLERSGRKG VMRINNGERV MGESPKSRKV PHAFLNLKEP FYVGGAPDFS KLARAAAIST
     SFYGAVQRIS IKGVPLLKEQ HIRSAVEIST FRAHPCTQKP NPCQNGGTCS PRLESYECAC
     QRGFSGAHCE KVIIEKAAGD AEAIAFDGRT YMEYHNAVTK SPDALDYPAE PSEKALQSNH
     FELSIKTEAT QGLILWSGKG LERSDYIALA IVDGFVQMMY DLGSKPVVLR STVPINTNHW
     THIKAYRVQR EGSLQVGNEA PITGSSPLGA TQLDTDGALW LGGMERLSVA HKLPKAYSTG
     FIGCIRDVIV DRQELHLVED ALNNPTILHC SAK
//
ID   CC14A_HUMAN             Reviewed;         594 AA.
AC   Q9UNH5; O43171; O60727; O60728; Q8IXX0;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   10-FEB-2009, entry version 67.
DE   RecName: Full=Dual specificity protein phosphatase CDC14A;
DE            EC=3.1.3.48;
DE            EC=3.1.3.16;
DE   AltName: Full=CDC14 cell division cycle 14 homolog A;
GN   Name=CDC14A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RX   MEDLINE=98037751; PubMed=9367992; DOI=10.1074/jbc.272.47.29403;
RA   Li L., Ernsting B.R., Wishart M.J., Lohse D.L., Dixon J.E.;
RT   "A family of putative tumor suppressors is structurally and
RT   functionally conserved in humans and yeast.";
RL   J. Biol. Chem. 272:29403-29406(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=99339990; PubMed=10409437; DOI=10.1006/geno.1999.5863;
RA   Wong A.K.C., Chen Y., Lian L., Ha P.C., Petersen K., Laity K.,
RA   Carillo A., Emerson M., Heichman K., Gupte J., Tavtigian S.V.,
RA   Teng D.H.-F.;
RT   "Genomic structure, chromosomal location, and mutation analysis of the
RT   human CDC14A gene.";
RL   Genomics 59:248-251(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 2 AND 3).
RC   TISSUE=Placenta;
RA   Hao L., Baskerville C., Charbonneau H.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-345 AND PHE-589.
RG   NIEHS SNPs program;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   DEPHOSPHORYLATION OF FZR1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   CYS-278.
RX   PubMed=11598127; DOI=10.1074/jbc.M108126200;
RA   Bembenek J., Yu H.;
RT   "Regulation of the anaphase-promoting complex by the dual specificity
RT   phosphatase human Cdc14a.";
RL   J. Biol. Chem. 276:48237-48242(2001).
RN   [7]
RP   SUBSTRATE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP   OF ASP-251; CYS-278 AND ARG-284.
RX   MEDLINE=22129382; PubMed=12134069; DOI=10.1091/mbc.01-11-0535;
RA   Kaiser B.K., Zimmerman Z.A., Charbonneau H., Jackson P.K.;
RT   "Disruption of centrosome structure, chromosome segregation, and
RT   cytokinesis by misexpression of human Cdc14A phosphatase.";
RL   Mol. Biol. Cell 13:2289-2300(2002).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF MET-362 AND
RP   ILE-364.
RX   MEDLINE=21941132; PubMed=11901424; DOI=10.1038/ncb777;
RA   Mailand N., Lukas C., Kaiser B.K., Jackson P.K., Bartek J., Lukas J.;
RT   "Deregulated human Cdc14A phosphatase disrupts centrosome separation
RT   and chromosome segregation.";
RL   Nat. Cell Biol. 4:317-322(2002).
RN   [9]
RP   INTERACTION WITH KIF20A, AND SUBCELLULAR LOCATION.
RX   PubMed=15263015; DOI=10.1083/jcb.200403084;
RA   Gruneberg U., Neef R., Honda R., Nigg E.A., Barr F.A.;
RT   "Relocation of Aurora B from centromeres to the central spindle at the
RT   metaphase to anaphase transition requires MKlp2.";
RL   J. Cell Biol. 166:167-172(2004).
RN   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] TYR-493.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Dual-specificity phosphatase. Required for centrosome
CC       separation and productive cytokinesis during cell division. May
CC       dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-
CC       FZR1 dependent degradation of mitotic cyclins and subsequent exit
CC       from mitosis.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- SUBUNIT: Interacts with KIF20A, which is required to localize
CC       CDC14 to the midzone of the mitotic spindle.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Centrosome. Note=Centrosomal during
CC       interphase, released into the cytoplasm at the onset of mitosis.
CC       Subsequently localizes to the midzone of the mitotic spindle.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=CDC14A1;
CC         IsoId=Q9UNH5-1; Sequence=Displayed;
CC       Name=2; Synonyms=CDC14A2;
CC         IsoId=Q9UNH5-2; Sequence=VSP_012037;
CC       Name=3; Synonyms=CDC14A3;
CC         IsoId=Q9UNH5-3; Sequence=VSP_012035, VSP_012036;
CC       Name=4; Synonyms=CDC14A4;
CC         IsoId=Q9UNH5-4; Sequence=VSP_012322, VSP_012323;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: Composed of two structurally equivalent A and B domains
CC       that adopt a dual specificity protein phosphatase (DSP) fold (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class CDC14 subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB88277.1; Type=Frameshift; Positions=6;
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/cdc14a/";
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DR   EMBL; AF000367; AAB88277.1; ALT_FRAME; mRNA.
DR   EMBL; AF122013; AAD49217.1; -; mRNA.
DR   EMBL; AF064102; AAC16659.1; -; mRNA.
DR   EMBL; AF064103; AAC16660.1; -; mRNA.
DR   EMBL; AY623111; AAT38107.1; -; Genomic_DNA.
DR   EMBL; BC038979; AAH38979.1; -; mRNA.
DR   IPI; IPI00021145; -.
DR   IPI; IPI00031770; -.
DR   IPI; IPI00217676; -.
DR   IPI; IPI00219831; -.
DR   RefSeq; NP_003663.2; -.
DR   RefSeq; NP_201569.1; -.
DR   RefSeq; NP_201570.1; -.
DR   UniGene; Hs.127411; -.
DR   HSSP; O60729; 1OHE.
DR   PRIDE; Q9UNH5; -.
DR   Ensembl; ENSG00000079335; Homo sapiens.
DR   GeneID; 8556; -.
DR   KEGG; hsa:8556; -.
DR   GeneCards; GC01P100530; -.
DR   H-InvDB; HIX0028511; -.
DR   HGNC; HGNC:1718; CDC14A.
DR   MIM; 603504; gene.
DR   PharmGKB; PA26254; -.
DR   HOVERGEN; Q9UNH5; -.
DR   BRENDA; 3.1.3.16; 247.
DR   BRENDA; 3.1.3.48; 247.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   LinkHub; Q9UNH5; -.
DR   NextBio; 32065; -.
DR   ArrayExpress; Q9UNH5; -.
DR   Bgee; Q9UNH5; -.
DR   CleanEx; HS_CDC14A; -.
DR   GermOnline; ENSG00000079335; Homo sapiens.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR   GO; GO:0005515; F:protein binding; IPI:HGNC.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphata...; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR   GO; GO:0006470; P:protein amino acid dephosphorylation; IEA:InterPro.
DR   InterPro; IPR000387; Tyr_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000340; Tyr_Pase_dual_specific.
DR   Pfam; PF00782; DSPc; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Hydrolase; Nucleus;
KW   Polymorphism; Protein phosphatase.
FT   CHAIN         1    594       Dual specificity protein phosphatase
FT                                CDC14A.
FT                                /FTId=PRO_0000094876.
FT   REGION        7    162       A.
FT   REGION      163    176       Linker.
FT   REGION      177    343       B.
FT   ACT_SITE    278    278       Phosphocysteine intermediate (By
FT                                similarity).
FT   VAR_SEQ     174    191       RVENGDFNWIVPGKFLAF -> VILFTPLKPTFLISKSIM
FT                                (in isoform 4).
FT                                /FTId=VSP_012322.
FT   VAR_SEQ     192    594       Missing (in isoform 4).
FT                                /FTId=VSP_012323.
FT   VAR_SEQ     380    383       DNLE -> VSFP (in isoform 3).
FT                                /FTId=VSP_012035.
FT   VAR_SEQ     384    594       Missing (in isoform 3).
FT                                /FTId=VSP_012036.
FT   VAR_SEQ     586    594       SLQSEYVHY -> VSAQTPPPGPQNPECNFCALPSQPRLPP
FT                                KKFNSAKEAF (in isoform 2).
FT                                /FTId=VSP_012037.
FT   VARIANT     345    345       R -> Q.
FT                                /FTId=VAR_019957.
FT   VARIANT     493    493       D -> Y (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_035655.
FT   VARIANT     589    589       S -> F (in dbSNP:rs28364923).
FT                                /FTId=VAR_019958.
FT   MUTAGEN     251    251       D->A: Loss of phosphatase activity.
FT   MUTAGEN     278    278       C->S: Loss of phosphatase activity.
FT   MUTAGEN     284    284       R->A: Loss of phosphatase activity.
FT   MUTAGEN     362    362       M->A: Inappropriate nucleolar
FT                                localization; when associated with A-364.
FT   MUTAGEN     364    364       I->A: Inappropriate nucleolar
FT                                localization; when associated with A-362.
FT   CONFLICT    164    164       F -> I (in Ref. 1; AAB88277).
FT   CONFLICT    182    182       W -> C (in Ref. 1; AAB88277).
SQ   SEQUENCE   594 AA;  66574 MW;  D5552E2BAEEA84DF CRC64;
     MAAESGELIG ACEFMKDRLY FATLRNRPKS TVNTHYFSID EELVYENFYA DFGPLNLAMV
     YRYCCKLNKK LKSYSLSRKK IVHYTCFDQR KRANAAFLIG AYAVIYLKKT PEEAYRALLS
     GSNPPYLPFR DASFGNCTYN LTILDCLQGI RKGLQHGFFD FETFDVDEYE HYERVENGDF
     NWIVPGKFLA FSGPHPKSKI ENGYPLHAPE AYFPYFKKHN VTAVVRLNKK IYEAKRFTDA
     GFEHYDLFFI DGSTPSDNIV RRFLNICENT EGAIAVHCKA GLGRTGTLIA CYVMKHYRFT
     HAEIIAWIRI CRPGSIIGPQ QHFLEEKQAS LWVQGDIFRS KLKNRPSSEG SINKILSGLD
     DMSIGGNLSK TQNMERFGED NLEDDDVEMK NGITQGDKLR ALKSQRQPRT SPSCAFRSDD
     TKGHPRAVSQ PFRLSSSLQG SAVTLKTSKM ALSPSATAKR INRTSLSSGA TVRSFSINSR
     LASSLGNLNA ATDDPENKKT SSSSKAGFTA SPFTNLLNGS SQPTTRNYPE LNNNQYNRSS
     NSNGGNLNSP PGPHSAKTEE HTTILRPSYT GLSSSSARFL SRSIPSLQSE YVHY
//
ID   EGFR_HUMAN              Reviewed;        1210 AA.
AC   P00533; O00688; O00732; P06268; Q14225; Q68GS5; Q92795; Q9BZS2;
AC   Q9GZX1; Q9H2C9; Q9H3C9; Q9UMD7; Q9UMD8; Q9UMG5;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   10-FEB-2009, entry version 142.
DE   RecName: Full=Epidermal growth factor receptor;
DE            EC=2.7.10.1;
DE   AltName: Full=Receptor tyrosine-protein kinase ErbB-1;
DE   Flags: Precursor;
GN   Name=EGFR; Synonyms=ERBB1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=84219729; PubMed=6328312; DOI=10.1038/309418a0;
RA   Ullrich A., Coussens L., Hayflick J.S., Dull T.J., Gray A., Tam A.W.,
RA   Lee J., Yarden Y., Libermann T.A., Schlessinger J., Downward J.,
RA   Mayes E.L.V., Whittle N., Waterfield M.D., Seeburg P.H.;
RT   "Human epidermal growth factor receptor cDNA sequence and aberrant
RT   expression of the amplified gene in A431 epidermoid carcinoma cells.";
RL   Nature 309:418-425(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Placenta;
RX   MEDLINE=95382957; PubMed=7654368; DOI=10.1002/mrd.1080410205;
RA   Ilekis J.V., Stark B.C., Scoccia B.;
RT   "Possible role of variant RNA transcripts in the regulation of
RT   epidermal growth factor receptor expression in human placenta.";
RL   Mol. Reprod. Dev. 41:149-156(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RC   TISSUE=Placenta;
RX   MEDLINE=97078686; PubMed=8918811; DOI=10.1093/nar/24.20.4050;
RA   Reiter J.L., Maihle N.J.;
RT   "A 1.8 kb alternative transcript from the human epidermal growth
RT   factor receptor gene encodes a truncated form of the receptor.";
RL   Nucleic Acids Res. 24:4050-4056(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 2).
RC   TISSUE=Placenta;
RX   MEDLINE=97256547; PubMed=9103388; DOI=10.1006/gyno.1996.4526;
RA   Ilekis J.V., Gariti J., Niederberger C., Scoccia B.;
RT   "Expression of a truncated epidermal growth factor receptor-like
RT   protein (TEGFR) in ovarian cancer.";
RL   Gynecol. Oncol. 65:36-41(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 3 AND 4).
RC   TISSUE=Placenta;
RX   MEDLINE=21100872; PubMed=11161793; DOI=10.1006/geno.2000.6341;
RA   Reiter J.L., Threadgill D.W., Eley G.D., Strunk K.E., Danielsen A.J.,
RA   Schehl Sinclair C., Pearsall R.S., Green P.J., Yee D., Lampland A.L.,
RA   Balasubramaniam S., Crossley T.D., Magnuson T.R., James C.D.,
RA   Maihle N.J.;
RT   "Comparative genomic sequence analysis and isolation of human and
RT   mouse alternative EGFR transcripts encoding truncated receptor
RT   isoforms.";
RL   Genomics 71:1-20(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Xu L., Hong A., He X.;
RT   "Cloning of the cDNA for a short EGF receptor from human placenta.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-98; ARG-266;
RP   LYS-521; ILE-674; GLY-962 AND PRO-988.
RG   NIEHS SNPs program;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 575-687.
RA   Reiter J.L., Threadgill D.W., Danielsen A.J., Schehl C.M.,
RA   Lampland A.L., Balasubramaniam S., Crossley T.O., Magnuson T.R.,
RA   Maihle N.J.;
RT   "Human and mouse alternative EGFR transcripts encoding only the
RT   extracellular domain of the receptor.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 713-924.
RX   MEDLINE=84196372; PubMed=6326261;
RA   Lin C.R., Chen W.S., Kruiger W., Stolarsky L.S., Weber W., Evans R.M.,
RA   Verma I.M., Gill G.N., Rosenfeld M.G.;
RT   "Expression cloning of human EGF receptor complementary DNA: gene
RT   amplification and three related messenger RNA products in A431
RT   cells.";
RL   Science 224:843-848(1984).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 150-962.
RX   MEDLINE=84245835; PubMed=6330563; DOI=10.1038/309806a0;
RA   Xu Y.H., Ishii S., Clark A.J.L., Sullivan M., Wilson R.K., Ma D.P.,
RA   Roe B.A., Merlino G.T., Pastan I.;
RT   "Human epidermal growth factor receptor cDNA is homologous to a
RT   variety of RNAs overproduced in A431 carcinoma cells.";
RL   Nature 309:806-810(1984).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1028-1210.
RX   MEDLINE=85046483; PubMed=6093780;
RA   Simmen F.A., Gope M.L., Schulz T.Z., Wright D.A., Carpenter G.,
RA   O'Malley B.W.;
RT   "Isolation of an evolutionarily conserved epidermal growth factor
RT   receptor cDNA from human A431 carcinoma cells.";
RL   Biochem. Biophys. Res. Commun. 124:125-132(1984).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX   MEDLINE=88217333; PubMed=3329716;
RA   Haley J.D., Whittle N., Bennett P., Kinchington D., Ullrich A.,
RA   Waterfield M.D.;
RT   "The human EGF receptor gene: structure of the 110 kb locus and
RT   identification of sequences regulating its transcription.";
RL   Oncogene Res. 1:375-396(1987).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX   MEDLINE=91107677; PubMed=1988448;
RA   Haley J.D., Waterfield M.D.;
RT   "Contributory effects of de novo transcription and premature
RT   transcript termination in the regulation of human epidermal growth
RT   factor receptor proto-oncogene RNA synthesis.";
RL   J. Biol. Chem. 266:1746-1753(1991).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX   MEDLINE=85270438; PubMed=2991899;
RA   Ishii S., Xu Y.H., Stratton R.H., Roe B.A., Merlino G.T., Pastan I.;
RT   "Characterization and sequence of the promoter region of the human
RT   epidermal growth factor receptor gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:4920-4924(1985).
RN   [15]
RP   NUCLEOTIDE SEQUENCE OF 25-49.
RX   MEDLINE=84172183; PubMed=6324343;
RA   Weber W., Gill G.N., Spiess J.;
RT   "Production of an epidermal growth factor receptor-related protein.";
RL   Science 224:294-297(1984).
RN   [16]
RP   PROTEIN SEQUENCE OF 540.
RA   Kohda D.;
RL   Submitted (SEP-1997) to UniProtKB.
RN   [17]
RP   PROTEIN SEQUENCE OF 687-705; 986-998; 1000-1023; 1026-1030 AND
RP   1068-1077, AND PHOSPHORYLATION AT THR-693; SER-695; SER-1070 AND
RP   SER-1071.
RX   MEDLINE=88330814; PubMed=3138233;
RA   Heisermann G.J., Gill G.N.;
RT   "Epidermal growth factor receptor threonine and serine residues
RT   phosphorylated in vivo.";
RL   J. Biol. Chem. 263:13152-13158(1988).
RN   [18]
RP   PROTEIN SEQUENCE OF 25-39.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally
RT   verified cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [19]
RP   PROTEIN SEQUENCE OF 740-744 AND 746-747.
RX   MEDLINE=85182650; PubMed=2985580;
RA   Russo M.W., Lukas T.J., Cohen S., Staros J.V.;
RT   "Identification of residues in the nucleotide binding site of the
RT   epidermal growth factor receptor/kinase.";
RL   J. Biol. Chem. 260:5205-5208(1985).
RN   [20]
RP   PROTEIN SEQUENCE OF 861-875 AND 914-932, UBIQUITINATION AT LYS-716;
RP   LYS-737; LYS-754; LYS-867; LYS-929 AND LYS-970, AND MASS SPECTROMETRY.
RX   PubMed=16543144; DOI=10.1016/j.molcel.2006.02.018;
RA   Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.;
RT   "Differential regulation of EGF receptor internalization and
RT   degradation by multiubiquitination within the kinase domain.";
RL   Mol. Cell 21:737-748(2006).
RN   [21]
RP   PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RX   MEDLINE=98225196; PubMed=9556602; DOI=10.1074/jbc.273.18.11150;
RA   Abe Y., Odaka M., Inagaki F., Lax I., Schlessinger J., Kohda D.;
RT   "Disulfide bond structure of human epidermal growth factor receptor.";
RL   J. Biol. Chem. 273:11150-11157(1998).
RN   [22]
RP   RECEPTOR ACTIVITY.
RX   MEDLINE=84191554; PubMed=6325948; DOI=10.1038/309270a0;
RA   Mroczkowski B., Mosig G., Cohen S.;
RT   "ATP-stimulated interaction between epidermal growth factor receptor
RT   and supercoiled DNA.";
RL   Nature 309:270-273(1984).
RN   [23]
RP   REVIEW.
RX   MEDLINE=87297456; PubMed=3039909;
RX   DOI=10.1146/annurev.bi.56.070187.004313;
RA   Carpenter G.;
RT   "Receptors for epidermal growth factor and other polypeptide
RT   mitogens.";
RL   Annu. Rev. Biochem. 56:881-914(1987).
RN   [24]
RP   LIGAND-BINDING.
RX   MEDLINE=90003233; PubMed=2790960; DOI=10.1016/0092-8674(89)90867-2;
RA   Chen W.S., Lazar C.S., Lund K.A., Welsh J.B., Chang C.P., Walton G.M.,
RA   Der C.J., Wiley H.S., Gill G.N., Rosenfeld M.G.;
RT   "Functional independence of the epidermal growth factor receptor from
RT   a domain required for ligand-induced internalization and calcium
RT   regulation.";
RL   Cell 59:33-43(1989).
RN   [25]
RP   PHOSPHORYLATION.
RX   MEDLINE=89278137; PubMed=2543678;
RA   Margolis B.L., Lax I., Kris R., Dombalagian M., Honegger A.M.,
RA   Howk R., Givol D., Ullrich A., Schlessinger J.;
RT   "All autophosphorylation sites of epidermal growth factor (EGF)
RT   receptor and HER2/neu are located in their carboxyl-terminal tails.
RT   Identification of a novel site in EGF receptor.";
RL   J. Biol. Chem. 264:10667-10671(1989).
RN   [26]
RP   INTERACTION WITH CBL.
RX   PubMed=7657591; DOI=10.1074/jbc.270.35.20242;
RA   Galisteo M.L., Dikic I., Batzer A.G., Langdon W.Y., Schlessinger J.;
RT   "Tyrosine phosphorylation of the c-cbl proto-oncogene protein product
RT   and association with epidermal growth factor (EGF) receptor upon EGF
RT   stimulation.";
RL   J. Biol. Chem. 270:20242-20245(1995).
RN   [27]
RP   GLYCOSYLATION AT ASN-128; ASN-175; ASN-413; ASN-444 AND ASN-528.
RX   MEDLINE=96398132; PubMed=8962717;
RA   Smith K.D., Davies M.J., Bailey D., Renouf D.V., Hounsell E.F.;
RT   "Analysis of the glycosylation patterns of the extracellular domain of
RT   the epidermal growth factor receptor expressed in Chinese hamster
RT   ovary fibroblasts.";
RL   Growth Factors 13:121-132(1996).
RN   [28]
RP   GLYCOSYLATION AT ASN-56; ASN-352; ASN-361; ASN-568 AND ASN-603.
RX   MEDLINE=20198209; PubMed=10731668;
RA   Sato C., Kim J.-H., Abe Y., Saito K., Yokoyama S., Kohda D.;
RT   "Characterization of the N-oligosaccharides attached to the atypical
RT   Asn-X-Cys sequence of recombinant human epidermal growth factor
RT   receptor.";
RL   J. Biochem. 127:65-72(2000).
RN   [29]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA   Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA   Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT   "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN   [30]
RP   IDENTIFICATION IN A COMPLEX WITH PIK3C2A AND ERBB2, IDENTIFICATION IN
RP   A COMPLEX WITH PIK3C2B AND ERBB2, INTERACTION WITH PIK3C2B, AND
RP   MUTAGENESIS OF TYR-1016; TYR-1092; TYR-1110; TYR-1172 AND TYR-1197.
RX   PubMed=10805725; DOI=10.1128/MCB.20.11.3817-3830.2000;
RA   Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D.,
RA   Domin J.;
RT   "Class II phosphoinositide 3-kinases are downstream targets of
RT   activated polypeptide growth factor receptors.";
RL   Mol. Cell. Biol. 20:3817-3830(2000).
RN   [31]
RP   INTERACTION WITH RIPK1.
RX   MEDLINE=21153697; PubMed=11116146; DOI=10.1074/jbc.M008458200;
RA   Habib A.A., Chatterjee S., Park S.-K., Ratan R.R., Lefebvre S.,
RA   Vartanian T.;
RT   "The epidermal growth factor receptor engages receptor interacting
RT   protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to
RT   activate NF-kappa B. Identification of a novel receptor-tyrosine
RT   kinase signalosome.";
RL   J. Biol. Chem. 276:8865-8874(2001).
RN   [32]
RP   INTERACTION WITH MUC1, AND FUNCTION.
RX   PubMed=11483589; DOI=10.1074/jbc.C100359200;
RA   Li Y., Ren J., Yu W., Li Q., Kuwahara H., Yin L., Carraway K.L. III,
RA   Kufe D.;
RT   "The epidermal growth factor receptor regulates interaction of the
RT   human DF3/MUC1 carcinoma antigen with c-Src and beta-catenin.";
RL   J. Biol. Chem. 276:35239-35242(2001).
RN   [33]
RP   GLYCOSYLATION AT ASN-56; ASN-128; ASN-175; ASN-196; ASN-352; ASN-361;
RP   ASN-413; ASN-444; ASN-528; ASN-568 AND ASN-603, PHOSPHORYLATION AT
RP   THR-693; SER-991 AND SER-1026, AND MASS SPECTROMETRY.
RX   PubMed=16083266; DOI=10.1021/pr050113n;
RA   Wu S.L., Kim J., Hancock W.S., Karger B.;
RT   "Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS
RT   platform for high sequence coverage of complex proteins with extensive
RT   post-translational modifications-comprehensive analysis of beta-casein
RT   and epidermal growth factor receptor (EGFR).";
RL   J. Proteome Res. 4:1155-1170(2005).
RN   [34]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-998; TYR-1069; TYR-1092;
RP   SER-1166 AND TYR-1172, AND MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=15951569; DOI=10.1074/mcp.M500089-MCP200;
RA   Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,
RA   Lauffenburger D.A., White F.M.;
RT   "Time-resolved mass spectrometry of tyrosine phosphorylation sites in
RT   the epidermal growth factor receptor signaling network reveals dynamic
RT   modules.";
RL   Mol. Cell. Proteomics 4:1240-1250(2005).
RN   [35]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-978, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Hepatocyte;
RX   PubMed=16097034; DOI=10.1002/pmic.200401217;
RA   Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,
RA   Demol H., Martens L., Goethals M., Vandekerckhove J.;
RT   "Global phosphoproteome analysis on human HepG2 hepatocytes using
RT   reversed-phase diagonal LC.";
RL   Proteomics 5:3589-3599(2005).
RN   [36]
RP   INTERACTION WITH PELP1.
RX   PubMed=16140940; DOI=10.1158/0008-5472.CAN-05-0614;
RA   Vadlamudi R.K., Manavathi B., Balasenthil S., Nair S.S., Yang Z.,
RA   Sahin A.A., Kumar R.;
RT   "Functional implications of altered subcellular localization of PELP1
RT   in breast cancer cells.";
RL   Cancer Res. 65:7724-7732(2005).
RN   [37]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-991; SER-995;
RP   TYR-998; SER-1064; TYR-1069; TYR-1092; TYR-1110; TYR-1138; TYR-1172
RP   AND TYR-1197, AND MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [38]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-869; TYR-1092; TYR-1172
RP   AND TYR-1197, AND MASS SPECTROMETRY.
RX   PubMed=18083107; DOI=10.1016/j.cell.2007.11.025;
RA   Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,
RA   Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,
RA   Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,
RA   Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,
RA   Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
RT   "Global survey of phosphotyrosine signaling identifies oncogenic
RT   kinases in lung cancer.";
RL   Cell 131:1190-1203(2007).
RN   [39]
RP   TISSUE SPECIFICITY.
RX   PubMed=17671655; DOI=10.1172/JCI31680;
RA   Groenestege W.M.T., Thebault S., van der Wijst J., van den Berg D.,
RA   Janssen R., Tejpar S., van den Heuvel L.P., van Cutsem E.,
RA   Hoenderop J.G., Knoers N.V., Bindels R.J.;
RT   "Impaired basolateral sorting of pro-EGF causes isolated recessive
RT   renal hypomagnesemia.";
RL   J. Clin. Invest. 117:2260-2267(2007).
RN   [40]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17192257; DOI=10.1074/mcp.T600062-MCP200;
RA   Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,
RA   Keri G., Wehland J., Daub H.;
RT   "Proteomics analysis of protein kinases by target class-selective
RT   prefractionation and tandem mass spectrometry.";
RL   Mol. Cell. Proteomics 6:537-547(2007).
RN   [41]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693 AND SER-991, AND
RP   MASS SPECTROMETRY.
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [42]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; THR-725;
RP   SER-991; SER-1025; SER-1026; SER-1037; SER-1039; SER-1042; SER-1064;
RP   SER-1081; SER-1166 AND TYR-1197, AND MASS SPECTROMETRY.
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [43]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; SER-991;
RP   THR-993; SER-995; TYR-998; SER-1039; THR-1041; SER-1042; SER-1045;
RP   SER-1064 AND SER-1166, AND MASS SPECTROMETRY.
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [44]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [45]
RP   VARIANTS LUNG CANCER SER-719 AND ARG-858.
RX   PubMed=15118125; DOI=10.1126/science.1099314;
RA   Paez J.G., Janne P.A., Lee J.C., Tracy S., Greulich H., Gabriel S.,
RA   Herman P., Kaye F.J., Lindeman N., Boggon T.J., Naoki K., Sasaki H.,
RA   Fujii Y., Eck M.J., Sellers W.R., Johnson B.E., Meyerson M.;
RT   "EGFR mutations in lung cancer: correlation with clinical response to
RT   gefitinib therapy.";
RL   Science 304:1497-1500(2004).
RN   [46]
RP   VARIANTS LUNG CANCER ALA-709; LYS-709; ALA-719; ASP-719; CYS-719;
RP   SER-719; SER-724; LYS-734; GLU-746 DEL; PHE-747; 747-LEU--GLU-749 DEL;
RP   PRO-748; 752-SER--ILE-759 DEL; ARG-787; MET-790; VAL-833; LEU-834;
RP   MET-858; ARG-858; GLN-861 AND GLU-873.
RX   PubMed=16533793; DOI=10.1158/1078-0432.CCR-05-1981;
RA   Tam I.Y.S., Chung L.P., Suen W.S., Wang E., Wong M.C.M., Ho K.K.,
RA   Lam W.K., Chiu S.W., Girard L., Minna J.D., Gazdar A.F., Wong M.P.;
RT   "Distinct epidermal growth factor receptor and KRAS mutation patterns
RT   in non-small cell lung cancer patients with different tobacco exposure
RT   and clinicopathologic features.";
RL   Clin. Cancer Res. 12:1647-1653(2006).
RN   [47]
RP   VARIANTS [LARGE SCALE ANALYSIS] LYS-521; ARG-1034 AND VAL-1210.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA   Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA   O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA   Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA   Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA   Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA   Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA   West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA   Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA   DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA   Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA   Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Receptor for EGF, but also for other members of the EGF
CC       family, as TGF-alpha, amphiregulin, betacellulin, heparin-binding
CC       EGF-like growth factor, GP30 and vaccinia virus growth factor. Is
CC       involved in the control of cell growth and differentiation.
CC       Phosphorylates MUC1 in breast cancer cells and increases the
CC       interaction of MUC1 with C-SRC and CTNNB1/beta-catenin.
CC   -!- FUNCTION: Isoform 2/truncated isoform may act as an antagonist.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Binds RIPK1. CBL interacts with the autophosphorylated C-
CC       terminal tail of the EGF receptor. Part of a complex with ERBB2
CC       and either PIK3C2A or PIK3C2B. The autophosphorylated form
CC       interacts with PIK3C2B, maybe indirectly. Interacts with PELP1.
CC       Binds MUC1.
CC   -!- INTERACTION:
CC       Self; NbExp=1; IntAct=EBI-297353, EBI-297353;
CC       Q29376:- (xeno); NbExp=1; IntAct=EBI-297353, EBI-1256881;
CC       P62157:CALM (xeno); NbExp=1; IntAct=EBI-297353, EBI-397403;
CC       P62158:CALM1; NbExp=1; IntAct=EBI-297353, EBI-397435;
CC       P62161:Calm1 (xeno); NbExp=2; IntAct=EBI-297353, EBI-397530;
CC       P62204:Calm1 (xeno); NbExp=1; IntAct=EBI-297353, EBI-397460;
CC       P22681:CBL; NbExp=1; IntAct=EBI-297353, EBI-518228;
CC       P22682:Cbl (xeno); NbExp=1; IntAct=EBI-297353, EBI-640919;
CC       P13987:CD59; NbExp=1; IntAct=EBI-297353, EBI-297972;
CC       P01133:EGF; NbExp=2; IntAct=EBI-297353, EBI-640857;
CC       P04626:ERBB2; NbExp=2; IntAct=EBI-297353, EBI-641062;
CC       P21860:ERBB3; NbExp=2; IntAct=EBI-297353, EBI-720706;
CC       Q15303:ERBB4; NbExp=2; IntAct=EBI-297353, EBI-80371;
CC       P62993:GRB2; NbExp=2; IntAct=EBI-297353, EBI-401755;
CC       O00750:PIK3C2B; NbExp=4; IntAct=EBI-297353, EBI-641107;
CC       Q9UJ41:RABGEF1; NbExp=2; IntAct=EBI-297353, EBI-913954;
CC       P98083:Shc1 (xeno); NbExp=1; IntAct=EBI-297353, EBI-300201;
CC       P13866:SLC5A1; NbExp=3; IntAct=EBI-297353, EBI-1772443;
CC       P63104:YWHAZ; NbExp=1; IntAct=EBI-297353, EBI-347088;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=p170;
CC         IsoId=P00533-1; Sequence=Displayed;
CC       Name=2; Synonyms=p60, Truncated, TEGFR;
CC         IsoId=P00533-2; Sequence=VSP_002887, VSP_002888;
CC       Name=3; Synonyms=p110;
CC         IsoId=P00533-3; Sequence=VSP_002889, VSP_002890;
CC       Name=4;
CC         IsoId=P00533-4; Sequence=VSP_002891, VSP_002892;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 2 is also
CC       expressed in ovarian cancers.
CC   -!- PTM: Phosphorylation of Ser-695 is partial and occurs only if Thr-
CC       693 is phosphorylated.
CC   -!- PTM: Monoubiquitinated and polyubiquitinated upon EGF stimulation;
CC       which does not affect tyrosine kinase activity or signaling
CC       capacity but may play a role in lysosomal targeting. Polyubiquitin
CC       linkage is mainly through 'Lys-63', but linkage through 'Lys-48',
CC       'Lys-11' and 'Lys-29' also occur.
CC   -!- DISEASE: Defects in EGFR are associated with lung cancer
CC       [MIM:211980].
CC   -!- MISCELLANEOUS: Binding of EGF to the receptor leads to
CC       dimerization, internalization of the EGF-receptor complex,
CC       induction of the tyrosine kinase activity, stimulation of cell DNA
CC       synthesis, and cell proliferation.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. EGF receptor subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.genetests.org/query?gene=EGFR";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/egfr/";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=EGFR entry;
CC       URL="http://en.wikipedia.org/wiki/Epidermal_growth_factor_receptor";
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DR   EMBL; X00588; CAA25240.1; -; mRNA.
DR   EMBL; U95089; AAB53063.1; -; mRNA.
DR   EMBL; U48722; AAC50802.1; -; mRNA.
DR   EMBL; U48723; AAC50804.1; -; Genomic_DNA.
DR   EMBL; U48724; AAC50796.1; -; Genomic_RNA.
DR   EMBL; U48725; AAC50797.1; -; Genomic_RNA.
DR   EMBL; U48726; AAC50798.1; -; Genomic_RNA.
DR   EMBL; U48727; AAC50799.1; -; Genomic_RNA.
DR   EMBL; U48728; AAC50800.1; -; Genomic_RNA.
DR   EMBL; U48729; AAC50801.1; -; Genomic_RNA.
DR   EMBL; AF288738; AAG35786.1; -; Genomic_DNA.
DR   EMBL; AF288738; AAG35787.1; -; Genomic_DNA.
DR   EMBL; AF288738; AAG35788.1; -; Genomic_DNA.
DR   EMBL; AF288738; AAG35789.1; -; Genomic_DNA.
DR   EMBL; AF288738; AAG35790.1; -; Genomic_DNA.
DR   EMBL; AY698024; AAT97979.1; -; mRNA.
DR   EMBL; AY588246; AAS83109.1; -; Genomic_DNA.
DR   EMBL; AF277897; AAK01080.1; -; mRNA.
DR   EMBL; AF125253; AAG43240.1; -; mRNA.
DR   EMBL; AF125539; AAG43243.1; -; Genomic_DNA.
DR   EMBL; AF125538; AAG43243.1; JOINED; Genomic_DNA.
DR   EMBL; X06370; CAA29668.1; -; Genomic_DNA.
DR   EMBL; X00663; CAA25282.1; -; mRNA.
DR   EMBL; M38425; AAA63171.1; -; Genomic_DNA.
DR   EMBL; M11234; AAA52370.1; -; Genomic_DNA.
DR   IPI; IPI00018274; -.
DR   IPI; IPI00221346; -.
DR   IPI; IPI00221347; -.
DR   IPI; IPI00221348; -.
DR   PIR; A00641; GQHUE.
DR   RefSeq; NP_005219.2; -.
DR   RefSeq; NP_958439.1; -.
DR   RefSeq; NP_958440.1; -.
DR   RefSeq; NP_958441.1; -.
DR   UniGene; Hs.488293; -.
DR   PDB; 1DNQ; Model; -; A=25-336.
DR   PDB; 1DNR; Model; -; A=337-645.
DR   PDB; 1IVO; X-ray; 3.30 A; A/B=25-646.
DR   PDB; 1M14; X-ray; 2.60 A; A=695-1022.
DR   PDB; 1M17; X-ray; 2.60 A; A=695-1022.
DR   PDB; 1MOX; X-ray; 2.50 A; A/B=25-525.
DR   PDB; 1NQL; X-ray; 2.80 A; A=25-642.
DR   PDB; 1XKK; X-ray; 2.40 A; A=695-1022.
DR   PDB; 1YY9; X-ray; 2.60 A; A=25-642.
DR   PDB; 1Z9I; NMR; -; A=669-721.
DR   PDB; 2EB2; X-ray; 2.50 A; A=695-1022.
DR   PDB; 2EB3; X-ray; 2.84 A; A=695-1022.
DR   PDB; 2EXP; Model; -; A=311-326.
DR   PDB; 2EXQ; Model; -; A=27-536.
DR   PDB; 2GS2; X-ray; 2.80 A; A=696-1022.
DR   PDB; 2GS6; X-ray; 2.60 A; A=696-1022.
DR   PDB; 2GS7; X-ray; 2.60 A; A/B=696-1022.
DR   PDB; 2ITN; X-ray; 2.47 A; A=696-1022.
DR   PDB; 2ITO; X-ray; 3.25 A; A=696-1022.
DR   PDB; 2ITP; X-ray; 2.74 A; A=696-1022.
DR   PDB; 2ITQ; X-ray; 2.68 A; A=696-1022.
DR   PDB; 2ITT; X-ray; 2.73 A; A=696-1022.
DR   PDB; 2ITU; X-ray; 2.80 A; A=696-1022.
DR   PDB; 2ITV; X-ray; 2.47 A; A=696-1022.
DR   PDB; 2ITW; X-ray; 2.88 A; A=696-1022.
DR   PDB; 2ITX; X-ray; 2.98 A; A=696-1022.
DR   PDB; 2ITY; X-ray; 3.42 A; A=696-1022.
DR   PDB; 2ITZ; X-ray; 2.72 A; A=696-1022.
DR   PDB; 2J5E; X-ray; 3.10 A; A=696-1022.
DR   PDB; 2J5F; X-ray; 3.00 A; A=696-1022.
DR   PDB; 2J6M; X-ray; 3.10 A; A=696-1022.
DR   PDB; 2JIT; X-ray; 3.10 A; A/B=696-1022.
DR   PDB; 2JIU; X-ray; 3.05 A; A/B=695-1022.
DR   PDB; 2JIV; X-ray; 3.50 A; A/B=695-1022.
DR   PDB; 2RF9; X-ray; 3.50 A; A/B=696-1022.
DR   PDB; 2RFD; X-ray; 3.60 A; A/B=702-1022.
DR   PDB; 2RFE; X-ray; 2.90 A; A/B/C/D=702-1022.
DR   PDB; 2RGP; X-ray; 2.00 A; A=702-1016.
DR   PDB; 3B2U; X-ray; 2.58 A; A/B/E/I/M/P/S/V=334-538.
DR   PDB; 3B2V; X-ray; 3.30 A; A=25-642.
DR   PDB; 3BEL; X-ray; 2.30 A; A=702-1016.
DR   PDB; 3BUO; X-ray; 2.60 A; A/C=1063-1075.
DR   PDB; 3C09; X-ray; 3.20 A; A/D=334-538.
DR   PDBsum; 1DNQ; -.
DR   PDBsum; 1DNR; -.
DR   PDBsum; 1IVO; -.
DR   PDBsum; 1M14; -.
DR   PDBsum; 1M17; -.
DR   PDBsum; 1MOX; -.
DR   PDBsum; 1NQL; -.
DR   PDBsum; 1XKK; -.
DR   PDBsum; 1YY9; -.
DR   PDBsum; 1Z9I; -.
DR   PDBsum; 2EB2; -.
DR   PDBsum; 2EB3; -.
DR   PDBsum; 2EXP; -.
DR   PDBsum; 2EXQ; -.
DR   PDBsum; 2GS2; -.
DR   PDBsum; 2GS6; -.
DR   PDBsum; 2GS7; -.
DR   PDBsum; 2ITN; -.
DR   PDBsum; 2ITO; -.
DR   PDBsum; 2ITP; -.
DR   PDBsum; 2ITQ; -.
DR   PDBsum; 2ITT; -.
DR   PDBsum; 2ITU; -.
DR   PDBsum; 2ITV; -.
DR   PDBsum; 2ITW; -.
DR   PDBsum; 2ITX; -.
DR   PDBsum; 2ITY; -.
DR   PDBsum; 2ITZ; -.
DR   PDBsum; 2J5E; -.
DR   PDBsum; 2J5F; -.
DR   PDBsum; 2J6M; -.
DR   PDBsum; 2JIT; -.
DR   PDBsum; 2JIU; -.
DR   PDBsum; 2JIV; -.
DR   PDBsum; 2RF9; -.
DR   PDBsum; 2RFD; -.
DR   PDBsum; 2RFE; -.
DR   PDBsum; 2RGP; -.
DR   PDBsum; 3B2U; -.
DR   PDBsum; 3B2V; -.
DR   PDBsum; 3BEL; -.
DR   PDBsum; 3BUO; -.
DR   PDBsum; 3C09; -.
DR   DisProt; DP00309; -.
DR   DIP; DIP:405N; -.
DR   IntAct; P00533; 107.
DR   GlycoSuiteDB; P00533; -.
DR   PhosphoSite; P00533; -.
DR   SWISS-2DPAGE; P00533; -.
DR   PeptideAtlas; P00533; -.
DR   PRIDE; P00533; -.
DR   Ensembl; ENSG00000146648; Homo sapiens.
DR   GeneID; 1956; -.
DR   KEGG; hsa:1956; -.
DR   GeneCards; GC07P055054; -.
DR   H-InvDB; HIX0025274; -.
DR   H-InvDB; HIX0025338; -.
DR   HGNC; HGNC:3236; EGFR.
DR   HPA; CAB000035; -.
DR   HPA; HPA001200; -.
DR   HPA; HPA018530; -.
DR   MIM; 131550; gene.
DR   MIM; 211980; phenotype.
DR   Orphanet; 360; Glioblastoma.
DR   PharmGKB; PA7360; -.
DR   HOVERGEN; P00533; -.
DR   BRENDA; 2.7.10.1; 247.
DR   Reactome; REACT_9417; Signaling by EGFR.
DR   DrugBank; DB00002; Cetuximab.
DR   DrugBank; DB00530; Erlotinib.
DR   DrugBank; DB00317; Gefitinib.
DR   DrugBank; DB01259; Lapatinib.
DR   DrugBank; DB00281; Lidocaine.
DR   DrugBank; DB01269; Panitumumab.
DR   DrugBank; DB00072; Trastuzumab.
DR   LinkHub; P00533; -.
DR   NextBio; 7931; -.
DR   ArrayExpress; P00533; -.
DR   Bgee; P00533; -.
DR   GermOnline; ENSG00000146648; Homo sapiens.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR   GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003690; F:double-stranded DNA binding; NAS:UniProtKB.
DR   GO; GO:0005006; F:epidermal growth factor receptor activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004710; F:MAP/ERK kinase kinase activity; NAS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR   GO; GO:0007202; P:activation of phospholipase C activity; TAS:UniProtKB.
DR   GO; GO:0043006; P:calcium-dependent phospholipase A2 activation; TAS:UniProtKB.
DR   GO; GO:0016337; P:cell-cell adhesion; IMP:UniProtKB.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling ...; IDA:UniProtKB.
DR   GO; GO:0031659; P:G1/S-specific positive regulation of cyclin...; IDA:UniProtKB.
DR   GO; GO:0045786; P:negative regulation of cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0001503; P:ossification; NAS:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR   GO; GO:0050679; P:positive regulation of epithelial cell prol...; IDA:UniProtKB.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynt...; IDA:UniProtKB.
DR   GO; GO:0042327; P:positive regulation of phosphorylation; IDA:UniProtKB.
DR   GO; GO:0051205; P:protein insertion into membrane; TAS:UniProtKB.
DR   GO; GO:0050999; P:regulation of nitric-oxide synthase activity; IDA:UniProtKB.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphoryla...; IMP:UniProtKB.
DR   GO; GO:0006950; P:response to stress; NAS:UniProtKB.
DR   InterPro; IPR000494; EGF_rcpt_L.
DR   InterPro; IPR006211; Furin-like.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_bd_CS.
DR   InterPro; IPR016245; Tyr_kinase_rcpt_EGF/ERB/XmrK.
DR   InterPro; IPR001245; Tyr_pkinase.
DR   InterPro; IPR008266; Tyr_pkinase_AS.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00261; FU; 3.
DR   SMART; SM00219; TyrKc; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Anti-oncogene; ATP-binding;
KW   Cell cycle; Cell membrane; Direct protein sequencing;
KW   Disease mutation; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Polymorphism; Receptor; Repeat; Secreted; Signal;
KW   Transferase; Transmembrane; Tyrosine-protein kinase; Ubl conjugation.
FT   SIGNAL        1     24
FT   CHAIN        25   1210       Epidermal growth factor receptor.
FT                                /FTId=PRO_0000016665.
FT   TOPO_DOM     25    645       Extracellular (Potential).
FT   TRANSMEM    646    668       Potential.
FT   TOPO_DOM    669   1210       Cytoplasmic (Potential).
FT   REPEAT       75    300       Approximate.
FT   REPEAT      390    600       Approximate.
FT   DOMAIN      712    979       Protein kinase.
FT   NP_BIND     718    726       ATP (By similarity).
FT   COMPBIAS   1025   1071       Ser-rich.
FT   ACT_SITE    837    837       Proton acceptor (By similarity).
FT   BINDING     745    745       ATP (By similarity).
FT   SITE       1016   1016       Important for interaction with PIK3C2B.
FT   MOD_RES     678    678       Phosphothreonine; by PKC.
FT   MOD_RES     693    693       Phosphothreonine.
FT   MOD_RES     695    695       Phosphoserine.
FT   MOD_RES     725    725       Phosphothreonine.
FT   MOD_RES     869    869       Phosphotyrosine.
FT   MOD_RES     978    978       Phosphotyrosine.
FT   MOD_RES     991    991       Phosphoserine.
FT   MOD_RES     993    993       Phosphothreonine.
FT   MOD_RES     995    995       Phosphoserine.
FT   MOD_RES     998    998       Phosphotyrosine.
FT   MOD_RES    1025   1025       Phosphoserine.
FT   MOD_RES    1026   1026       Phosphoserine.
FT   MOD_RES    1037   1037       Phosphoserine.
FT   MOD_RES    1039   1039       Phosphoserine.
FT   MOD_RES    1041   1041       Phosphothreonine.
FT   MOD_RES    1042   1042       Phosphoserine.
FT   MOD_RES    1045   1045       Phosphoserine.
FT   MOD_RES    1064   1064       Phosphoserine.
FT   MOD_RES    1069   1069       Phosphotyrosine.
FT   MOD_RES    1070   1070       Phosphoserine.
FT   MOD_RES    1071   1071       Phosphoserine.
FT   MOD_RES    1081   1081       Phosphoserine.
FT   MOD_RES    1092   1092       Phosphotyrosine; by autocatalysis.
FT   MOD_RES    1110   1110       Phosphotyrosine; by autocatalysis.
FT   MOD_RES    1138   1138       Phosphotyrosine.
FT   MOD_RES    1166   1166       Phosphoserine.
FT   MOD_RES    1172   1172       Phosphotyrosine; by autocatalysis.
FT   MOD_RES    1197   1197       Phosphotyrosine; by autocatalysis.
FT   CARBOHYD     56     56       N-linked (GlcNAc...) (complex); atypical;
FT                                partial.
FT                                /FTId=CAR_000227.
FT   CARBOHYD    128    128       N-linked (GlcNAc...).
FT   CARBOHYD    175    175       N-linked (GlcNAc...).
FT   CARBOHYD    196    196       N-linked (GlcNAc...).
FT   CARBOHYD    352    352       N-linked (GlcNAc...).
FT   CARBOHYD    361    361       N-linked (GlcNAc...).
FT   CARBOHYD    413    413       N-linked (GlcNAc...).
FT   CARBOHYD    444    444       N-linked (GlcNAc...).
FT   CARBOHYD    528    528       N-linked (GlcNAc...).
FT   CARBOHYD    568    568       N-linked (GlcNAc...); partial.
FT   CARBOHYD    603    603       N-linked (GlcNAc...); partial.
FT   DISULFID     31     58
FT   DISULFID    157    187
FT   DISULFID    190    199
FT   DISULFID    194    207
FT   DISULFID    215    223
FT   DISULFID    219    231
FT   DISULFID    232    240
FT   DISULFID    236    248
FT   DISULFID    251    260
FT   DISULFID    264    291
FT   DISULFID    295    307
FT   DISULFID    311    326
FT   DISULFID    329    333
FT   DISULFID    337    362
FT   DISULFID    470    499
FT   DISULFID    506    515
FT   DISULFID    510    523
FT   DISULFID    526    535
FT   DISULFID    539    555
FT   DISULFID    558    571
FT   DISULFID    562    579
FT   DISULFID    582    591
FT   DISULFID    595    617
FT   DISULFID    620    628
FT   DISULFID    624    636
FT   CROSSLNK    716    716       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK    737    737       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK    754    754       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK    867    867       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK    929    929       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK    970    970       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   VAR_SEQ     404    405       FL -> LS (in isoform 2).
FT                                /FTId=VSP_002887.
FT   VAR_SEQ     406   1210       Missing (in isoform 2).
FT                                /FTId=VSP_002888.
FT   VAR_SEQ     628    705       CTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFM
FT                                RRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLR ->
FT                                PGNESLKAMLFCLFKLSSCNQSNDGSVSHQSGSPAAQESCL
FT                                GWIPSLLPSEFQLGWGGCSHLHAWPSASVIITASSCH (in
FT                                isoform 3).
FT                                /FTId=VSP_002889.
FT   VAR_SEQ     628    628       C -> S (in isoform 4).
FT                                /FTId=VSP_002891.
FT   VAR_SEQ     629   1210       Missing (in isoform 4).
FT                                /FTId=VSP_002892.
FT   VAR_SEQ     706   1210       Missing (in isoform 3).
FT                                /FTId=VSP_002890.
FT   VARIANT      98     98       R -> Q (in dbSNP:rs17289589).
FT                                /FTId=VAR_019293.
FT   VARIANT     266    266       P -> R (in dbSNP:rs17336639).
FT                                /FTId=VAR_019294.
FT   VARIANT     521    521       R -> K (in dbSNP:rs2227983).
FT                                /FTId=VAR_019295.
FT   VARIANT     674    674       V -> I (in dbSNP:rs17337079).
FT                                /FTId=VAR_019296.
FT   VARIANT     709    709       E -> A (in lung cancer).
FT                                /FTId=VAR_026084.
FT   VARIANT     709    709       E -> K (in lung cancer).
FT                                /FTId=VAR_026085.
FT   VARIANT     719    719       G -> A (in lung cancer).
FT                                /FTId=VAR_026086.
FT   VARIANT     719    719       G -> C (in lung cancer;
FT                                dbSNP:rs28929495).
FT                                /FTId=VAR_026087.
FT   VARIANT     719    719       G -> D (in lung cancer).
FT                                /FTId=VAR_026088.
FT   VARIANT     719    719       G -> S (in lung cancer; somatic
FT                                mutation).
FT                                /FTId=VAR_019297.
FT   VARIANT     724    724       G -> S (in lung cancer).
FT                                /FTId=VAR_026089.
FT   VARIANT     734    734       E -> K (in lung cancer).
FT                                /FTId=VAR_026090.
FT   VARIANT     746    750       Missing (in lung cancer).
FT                                /FTId=VAR_026092.
FT   VARIANT     746    746       Missing (in lung cancer).
FT                                /FTId=VAR_026091.
FT   VARIANT     747    749       Missing (in lung cancer).
FT                                /FTId=VAR_026094.
FT   VARIANT     747    747       L -> F (in lung cancer).
FT                                /FTId=VAR_026093.
FT   VARIANT     748    748       R -> P (in lung cancer).
FT                                /FTId=VAR_026095.
FT   VARIANT     752    759       Missing (in lung cancer).
FT                                /FTId=VAR_026096.
FT   VARIANT     787    787       Q -> R (in lung cancer).
FT                                /FTId=VAR_026097.
FT   VARIANT     790    790       T -> M (in lung cancer).
FT                                /FTId=VAR_026098.
FT   VARIANT     833    833       L -> V (in lung cancer).
FT                                /FTId=VAR_026099.
FT   VARIANT     834    834       V -> L (in lung cancer).
FT                                /FTId=VAR_026100.
FT   VARIANT     858    858       L -> M (in lung cancer).
FT                                /FTId=VAR_026101.
FT   VARIANT     858    858       L -> R (in lung cancer; somatic
FT                                mutation).
FT                                /FTId=VAR_019298.
FT   VARIANT     861    861       L -> Q (in lung cancer).
FT                                /FTId=VAR_026102.
FT   VARIANT     873    873       G -> E (in lung cancer).
FT                                /FTId=VAR_026103.
FT   VARIANT     962    962       R -> G (in dbSNP:rs17337451).
FT                                /FTId=VAR_019299.
FT   VARIANT     988    988       H -> P (in dbSNP:rs17290699).
FT                                /FTId=VAR_019300.
FT   VARIANT    1034   1034       L -> R.
FT                                /FTId=VAR_042095.
FT   VARIANT    1210   1210       A -> V.
FT                                /FTId=VAR_042096.
FT   MUTAGEN    1016   1016       Y->F: 50% decrease in interaction with
FT                                PIK3C2B. 65% decrease in interaction with
FT                                PIK3C2B; when associated with F-1197.
FT                                Abolishes interaction with PIK3C2B; when
FT                                associated with F-1197 and F-1092.
FT   MUTAGEN    1092   1092       Y->F: No change in interaction with
FT                                PIK3C2B. Abolishes interaction with
FT                                PIK3C2B; when associated with F-1197 and
FT                                F-1016.
FT   MUTAGEN    1110   1110       Y->F: No change in interaction with
FT                                PIK3C2B.
FT   MUTAGEN    1172   1172       Y->F: No change in interaction with
FT                                PIK3C2B.
FT   MUTAGEN    1197   1197       Y->F: No change in interaction with
FT                                PIK3C2B. 65% decrease in interaction with
FT                                PIK3C2B; when associated with F-1016.
FT                                Abolishes interaction with PIK3C2B; when
FT                                associated with F-1092 and F-1016.
FT   CONFLICT    540    540       N -> K (in Ref. 1; CAA25240).
FT   STRAND       40     43
FT   HELIX        44     55
FT   STRAND       59     63
FT   STRAND       65     67
FT   HELIX        77     81
FT   STRAND       84     87
FT   STRAND       89     93
FT   HELIX       101    103
FT   TURN        114    116
FT   STRAND      117    122
FT   STRAND      145    152
FT   HELIX       159    161
FT   TURN        164    167
FT   TURN        173    175
FT   STRAND      195    197
FT   STRAND      200    202
FT   TURN        203    205
FT   STRAND      211    215
FT   STRAND      224    229
FT   STRAND      236    238
FT   STRAND      241    247
FT   STRAND      249    256
FT   STRAND      259    263
FT   STRAND      267    271
FT   TURN        272    275
FT   STRAND      276    279
FT   STRAND      285    287
FT   STRAND      290    294
FT   STRAND      299    301
FT   STRAND      305    309
FT   STRAND      321    323
FT   STRAND      330    332
FT   STRAND      340    342
FT   HELIX       343    345
FT   HELIX       353    355
FT   HELIX       357    359
FT   STRAND      363    367
FT   STRAND      369    371
FT   HELIX       373    377
FT   TURN        380    383
FT   HELIX       389    397
FT   STRAND      400    403
FT   STRAND      405    408
FT   HELIX       418    420
FT   TURN        433    435
FT   STRAND      436    442
FT   STRAND      458    464
FT   HELIX       472    474
FT   HELIX       477    480
FT   STRAND      492    494
FT   HELIX       496    498
FT   TURN        499    503
FT   TURN        507    509
FT   STRAND      515    519
FT   STRAND      522    525
FT   STRAND      540    543
FT   STRAND      548    557
FT   STRAND      571    575
FT   STRAND      579    587
FT   STRAND      590    594
FT   STRAND      597    600
FT   STRAND      602    611
FT   STRAND      616    619
FT   STRAND      629    632
FT   TURN        633    635
FT   STRAND      704    706
FT   TURN        709    711
FT   STRAND      712    720
FT   STRAND      722    731
FT   STRAND      740    747
FT   HELIX       756    768
FT   STRAND      777    791
FT   HELIX       798    804
FT   STRAND      806    808
FT   HELIX       811    830
FT   HELIX       840    842
FT   STRAND      843    847
FT   STRAND      850    853
FT   HELIX       858    861
FT   TURN        862    865
FT   TURN        878    880
FT   HELIX       883    888
FT   HELIX       893    908
FT   TURN        914    917
FT   HELIX       920    922
FT   HELIX       923    929
FT   HELIX       941    950
FT   HELIX       955    957
FT   HELIX       961    973
FT   HELIX       975    978
FT   TURN        982    986
FT   HELIX       996   1002
FT   HELIX      1013   1016
SQ   SEQUENCE   1210 AA;  134277 MW;  D8A2A50B4EFB6ED2 CRC64;
     MRPSGTAGAA LLALLAALCP ASRALEEKKV CQGTSNKLTQ LGTFEDHFLS LQRMFNNCEV
     VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN MYYENSYALA
     VLSNYDANKT GLKELPMRNL QEILHGAVRF SNNPALCNVE SIQWRDIVSS DFLSNMSMDF
     QNHLGSCQKC DPSCPNGSCW GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC
     TGPRESDCLV CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV
     VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDSLS INATNIKHFK
     NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE ITGFLLIQAW PENRTDLHAF
     ENLEIIRGRT KQHGQFSLAV VSLNITSLGL RSLKEISDGD VIISGNKNLC YANTINWKKL
     FGTSGQKTKI ISNRGENSCK ATGQVCHALC SPEGCWGPEP RDCVSCRNVS RGRECVDKCN
     LLEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM
     GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCPTNG PKIPSIATGM VGALLLLLVV
     ALGIGLFMRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN QALLRILKET EFKKIKVLGS
     GAFGTVYKGL WIPEGEKVKI PVAIKELREA TSPKANKEIL DEAYVMASVD NPHVCRLLGI
     CLTSTVQLIT QLMPFGCLLD YVREHKDNIG SQYLLNWCVQ IAKGMNYLED RRLVHRDLAA
     RNVLVKTPQH VKITDFGLAK LLGAEEKEYH AEGGKVPIKW MALESILHRI YTHQSDVWSY
     GVTVWELMTF GSKPYDGIPA SEISSILEKG ERLPQPPICT IDVYMIMVKC WMIDADSRPK
     FRELIIEFSK MARDPQRYLV IQGDERMHLP SPTDSNFYRA LMDEEDMDDV VDADEYLIPQ
     QGFFSSPSTS RTPLLSSLSA TSNNSTVACI DRNGLQSCPI KEDSFLQRYS SDPTGALTED
     SIDDTFLPVP EYINQSVPKR PAGSVQNPVY HNQPLNPAPS RDPHYQDPHS TAVGNPEYLN
     TVQPTCVNST FDSPAHWAQK GSHQISLDNP DYQQDFFPKE AKPNGIFKGS TAENAEYLRV
     APQSSEFIGA
//
ID   FENR_CYAPA              Reviewed;         363 AA.
AC   Q00598;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   20-JAN-2009, entry version 60.
DE   RecName: Full=Ferredoxin--NADP reductase, cyanelle;
DE            Short=FNR;
DE            EC=1.18.1.2;
DE   Flags: Precursor;
GN   Name=PETH;
OS   Cyanophora paradoxa.
OC   Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX   NCBI_TaxID=2762;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 66-90.
RC   STRAIN=UTEX LB 555 / Pringsheim;
RX   MEDLINE=93257619; PubMed=8490125; DOI=10.1007/BF00023600;
RA   Jakowitsch J., Bayer M.G., Maier T.L., Luettke A., Gebhart U.B.,
RA   Brandtner M., Hamilton B., Neumann-Spallart C., Michalowski C.B.,
RA   Bohnert H.J., Schenk H.E.A., Loeffelhardt W.;
RT   "Sequence analysis of pre-ferredoxin-NADP(+)-reductase cDNA from
RT   Cyanophora paradoxa specifying a precursor for a nucleus-encoded
RT   cyanelle polypeptide.";
RL   Plant Mol. Biol. 21:1023-1033(1993).
CC   -!- FUNCTION: May play a key role in regulating the relative amounts
CC       of cyclic and non-cyclic electron flow to meet the demands of the
CC       plant for ATP and reducing power.
CC   -!- CATALYTIC ACTIVITY: 2 reduced ferredoxin + NADP(+) + H(+) = 2
CC       oxidized ferredoxin + NADPH.
CC   -!- COFACTOR: FAD.
CC   -!- SUBCELLULAR LOCATION: Plastid, cyanelle stroma. Plastid, cyanelle
CC       thylakoid membrane; Peripheral membrane protein; Stromal side
CC       (Probable). Note=In the vicinity of the photosystem I (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1
CC       family.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
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DR   EMBL; X66372; CAA47015.1; -; mRNA.
DR   PIR; S33545; A56664.
DR   HSSP; P00455; 1FNC.
DR   BRENDA; 1.18.1.2; 11.
DR   GO; GO:0009842; C:cyanelle; IEA:UniProtKB-KW.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001834; Cyt_B5_reductase.
DR   InterPro; IPR001709; FPN_cyt_redctse.
DR   InterPro; IPR012146; Frd-NADP+_RD.
DR   InterPro; IPR015701; FRD_Red.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   PANTHER; PTHR19384:SF1; FRD_Red; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF000361; Frd-NADP+_RD; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00371; FPNCR.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   1: Evidence at protein level;
KW   Cyanelle; Direct protein sequencing; Electron transport; FAD;
KW   Flavoprotein; Membrane; NADP; Oxidoreductase; Photosynthesis; Plastid;
KW   Thylakoid; Transit peptide; Transport.
FT   TRANSIT       1     65       Cyanelle.
FT   CHAIN        66    363       Ferredoxin--NADP reductase, cyanelle.
FT                                /FTId=PRO_0000019418.
FT   DOMAIN       84    206       FAD-binding FR-type.
FT   NP_BIND     142    145       FAD (By similarity).
FT   NP_BIND     163    165       FAD (By similarity).
FT   NP_BIND     180    182       FAD (By similarity).
FT   NP_BIND     253    254       NADP (By similarity).
FT   NP_BIND     283    284       NADP (By similarity).
FT   NP_BIND     322    323       NADP (By similarity).
FT   BINDING     145    145       NADP (By similarity).
FT   BINDING     165    165       NADP (By similarity).
FT   BINDING     169    169       FAD (By similarity).
FT   BINDING     221    221       FAD (By similarity).
FT   BINDING     221    221       NADP; via amide nitrogen (By similarity).
FT   BINDING     293    293       NADP (By similarity).
FT   BINDING     361    361       NADP (By similarity).
SQ   SEQUENCE   363 AA;  40491 MW;  F5F5D1AEA91ADEBF CRC64;
     MAFVASVPVF ANASGLKTEA KVCQKPALKN SFFRGEEVTS RSFFASQAVS AKPATTFEVD
     TTIRAQAVDA KKKGDIPLNL FRPANPYIGK CIYNERIVGE GAPGETKHII FTHEGKVPYL
     EGQSIGIIPP GTDKDGKPHK LRLYSIASTR HGDFGDDKTV SLSVKRLEYT DANGNLVKGV
     CSNYLCDLKP GDEVMITGPV GTTMLMPEDQ SATIIMLATG TGIAPFRSFL RRMFEETHAD
     YKFNGLAWLF LGVPTSSTLL YREELEKMQK ANPNNFRLDY AISREQTDSK GEKMYIQNRI
     AEYANEFWNM IQKPNTFVYM CGLRGMEDGI QQCMEDIAKA NGTTWDAVVK GLKKEKRWHV
     ETY
//
ID   FMRF_LYMST              Reviewed;         306 AA.
AC   P19802;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-NOV-2008, entry version 51.
DE   RecName: Full=FMRFamide neuropeptides;
DE   Contains:
DE     RecName: Full=FLRF-amide 1;
DE   Contains:
DE     RecName: Full=QFYRI-amide;
DE   Contains:
DE     RecName: Full=FLRF-amide 2;
DE   Contains:
DE     RecName: Full=PN;
DE     AltName: Full=SEEPLY;
DE   Contains:
DE     RecName: Full=FMRF-amide 1;
DE   Contains:
DE     RecName: Full=FMRF-amide 2;
DE   Contains:
DE     RecName: Full=FMRF-amide 3;
DE   Contains:
DE     RecName: Full=FMRF-amide 4;
DE   Contains:
DE     RecName: Full=FMRF-amide 5;
DE   Contains:
DE     RecName: Full=FMRF-amide 6;
DE   Contains:
DE     RecName: Full=FMRF-amide 7;
DE   Contains:
DE     RecName: Full=FMRF-amide 8;
DE   Contains:
DE     RecName: Full=FMRF-amide 9;
DE   Contains:
DE     RecName: Full=EFLRI-amide;
DE   Flags: Precursor;
OS   Lymnaea stagnalis (Great pond snail).
OC   Eukaryota; Metazoa; Mollusca; Gastropoda; Pulmonata; Basommatophora;
OC   Lymnaeoidea; Lymnaeidae; Lymnaea.
OX   NCBI_TaxID=6523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=90155411; PubMed=1968092;
RA   Linacre A., Kellett E., Saunders S., Bright K., Benjamin P.R.,
RA   Burke J.F.;
RT   "Cardioactive neuropeptide Phe-Met-Arg-Phe-NH2 (FMRFamide) and novel
RT   related peptides are encoded in multiple copies by a single gene in
RT   the snail Lymnaea stagnalis.";
RL   J. Neurosci. 10:412-419(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=95054375; PubMed=7965060;
RA   Kellett E., Saunders S.E., Li K.W., Staddon J.W., Benjamin P.R.,
RA   Burke J.F.;
RT   "Genomic organization of the FMRFamide gene in Lymnaea: multiple exons
RT   encoding novel neuropeptides.";
RL   J. Neurosci. 14:6564-6570(1994).
RN   [3]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=CNS;
RX   MEDLINE=92185507; PubMed=1347559;
RA   Saunders S.E., Kellett E., Bright K., Benjamin P.R., Burke J.F.;
RT   "Cell-specific alternative RNA splicing of an FMRFamide gene
RT   transcript in the brain.";
RL   J. Neurosci. 12:1033-1039(1992).
RN   [4]
RP   PROTEIN SEQUENCE OF 82-103 (PN).
RC   TISSUE=CNS;
RX   MEDLINE=94108633; PubMed=7904219;
RA   Santama N., Li K.W., Bright K.E., Yeoman M., Geraerts W.P.M.,
RA   Benjamin P.R., Burke J.F.;
RT   "Processing of the FMRFamide precursor protein in the snail Lymnaea
RT   stagnalis: characterization and neuronal localization of a novel
RT   peptide, 'SEEPLY'.";
RL   Eur. J. Neurosci. 5:1003-1016(1993).
CC   -!- FUNCTION: FMRFamide induces contractions in visceral and somatic
CC       musculature as well as in the heart. May play a role as
CC       cotransmitters or modulators in a number of significant neuronal
CC       systems.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Isoform 1 and isoform 2 only share the N-terminal signal
CC         sequence;
CC       Name=1; Synonyms=FMRFamide;
CC         IsoId=P19802-1; Sequence=Displayed;
CC       Name=2; Synonyms=FMRFamide-related;
CC         IsoId=P42565-1; Sequence=External;
CC       Name=3;
CC         IsoId=P19802-2; Sequence=VSP_001564;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in 280 cells of the CNS including
CC       the EGP heart excitatory motoneurons.
CC   -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide)
CC       family.
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DR   EMBL; M37629; AAA63280.1; -; mRNA.
DR   EMBL; M87479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S38686; AAB21767.1; -; mRNA.
DR   EMBL; S94982; AAB21764.1; -; Genomic_DNA.
DR   PIR; A37016; A37016.
DR   PIR; F44840; F44840.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   InterPro; IPR002544; FMRFamid-related_peptide.
DR   Pfam; PF01581; FARP; 13.
PE   1: Evidence at protein level;
KW   Alternative splicing; Amidation; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Neuropeptide; Repeat; Secreted; Signal.
FT   SIGNAL        1     35       Potential.
FT   PROPEP       36     37
FT                                /FTId=PRO_0000009668.
FT   PEPTIDE      40     43       FLRF-amide 1.
FT                                /FTId=PRO_0000009669.
FT   PROPEP       46     56
FT                                /FTId=PRO_0000009670.
FT   PEPTIDE      59     63       QFYRI-amide.
FT                                /FTId=PRO_0000009671.
FT   PROPEP       66     73
FT                                /FTId=PRO_0000009672.
FT   PEPTIDE      76     79       FLRF-amide 2.
FT                                /FTId=PRO_0000009673.
FT   PEPTIDE      82    103       PN.
FT                                /FTId=PRO_0000009674.
FT   PROPEP      108    149
FT                                /FTId=PRO_0000009675.
FT   PEPTIDE     152    155       FMRF-amide 1.
FT                                /FTId=PRO_0000009676.
FT   PROPEP      158    163
FT                                /FTId=PRO_0000009677.
FT   PEPTIDE     166    169       FMRF-amide 2.
FT                                /FTId=PRO_0000009678.
FT   PROPEP      171    172
FT                                /FTId=PRO_0000009679.
FT   PEPTIDE     173    176       FMRF-amide 3.
FT                                /FTId=PRO_0000009680.
FT   PROPEP      179    184
FT                                /FTId=PRO_0000009681.
FT   PEPTIDE     187    190       FMRF-amide 4.
FT                                /FTId=PRO_0000009682.
FT   PEPTIDE     194    197       FMRF-amide 5.
FT                                /FTId=PRO_0000009683.
FT   PROPEP      200    204
FT                                /FTId=PRO_0000009684.
FT   PEPTIDE     207    210       FMRF-amide 6.
FT                                /FTId=PRO_0000009685.
FT   PROPEP      213    217
FT                                /FTId=PRO_0000009686.
FT   PEPTIDE     220    223       FMRF-amide 7.
FT                                /FTId=PRO_0000009687.
FT   PROPEP      226    251
FT                                /FTId=PRO_0000009688.
FT   PEPTIDE     254    257       FMRF-amide 8.
FT                                /FTId=PRO_0000009689.
FT   PROPEP      260    263
FT                                /FTId=PRO_0000009690.
FT   PEPTIDE     266    269       FMRF-amide 9.
FT                                /FTId=PRO_0000009691.
FT   PROPEP      272    278
FT                                /FTId=PRO_0000009692.
FT   PEPTIDE     281    285       EFLRI-amide.
FT                                /FTId=PRO_0000009693.
FT   PROPEP      289    306
FT                                /FTId=PRO_0000009694.
FT   MOD_RES      43     43       Phenylalanine amide.
FT   MOD_RES      63     63       Isoleucine amide.
FT   MOD_RES      79     79       Phenylalanine amide.
FT   MOD_RES     155    155       Phenylalanine amide.
FT   MOD_RES     169    169       Phenylalanine amide.
FT   MOD_RES     176    176       Phenylalanine amide.
FT   MOD_RES     190    190       Phenylalanine amide.
FT   MOD_RES     197    197       Phenylalanine amide.
FT   MOD_RES     210    210       Phenylalanine amide.
FT   MOD_RES     223    223       Phenylalanine amide.
FT   MOD_RES     257    257       Phenylalanine amide.
FT   MOD_RES     269    269       Phenylalanine amide.
FT   MOD_RES     285    285       Isoleucine amide.
FT   VAR_SEQ       1     36       MKTWSHVALLACLSIKWLTCVMADSIYCDDPDMCSM -> M
FT                                YSPTLIVCLSFFHSAVTKRFLRFGRALDTT (in
FT                                isoform 3).
FT                                /FTId=VSP_001564.
FT   CONFLICT     91     91       L -> P (in Ref. 1; AAA63280).
FT   CONFLICT    273    273       E -> Q (in Ref. 1; AAA63280).
SQ   SEQUENCE   306 AA;  36351 MW;  AB2361EFF2C4EF18 CRC64;
     MKTWSHVALL ACLSIKWLTC VMADSIYCDD PDMCSMTKRF LRFGRALDTT DPFIRLRRQF
     YRIGRGGYQP YQDKRFLRFG RSEQPDVDDY LRDVVLQSEE PLYRKRRSTE AGGQSEEMTH
     RTARSAPEPA AENREIMKRE TGAEDLDEEK RFMRFGRGDE EAEKRFMRFG KSFMRFGRDM
     SDVDKRFMRF GKRFMRFGRE PGTDKRFMRF GREPGADKRF MRFGKSFDGE EENDDDLYYN
     ESDADSNDDV DKRFMRFGKS AEEKRFMRFG KSEDASRDKK EFLRIGKRES RSAEVENNIQ
     IAAKQS
//
ID   GAC_YEAST               Reviewed;         106 AA.
AC   P33440;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   04-NOV-2008, entry version 26.
DE   RecName: Full=Glyoxalase I activity-enhancing protein GAC;
GN   Name=GAC;
OS   Saccharomyces cerevisiae (Baker's yeast).
OG   Plasmid 2-micron.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A364A D5;
RX   MEDLINE=81012161; PubMed=6251374; DOI=10.1038/286860a0;
RA   Hartley J.L., Donelson J.E.;
RT   "Nucleotide sequence of the yeast plasmid.";
RL   Nature 286:860-864(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GLOI-31;
RX   MEDLINE=90297911; PubMed=2193656;
RA   Inoue Y., Feng L., Bong-Young C., Ginya H., Murata K., Kimura A.;
RT   "Nucleotide sequence of a gene which enhances the activity of
RT   glyoxalase I in Saccharomyces cerevisiae.";
RL   Biotechnol. Appl. Biochem. 12:341-345(1990).
CC   -!- FUNCTION: Enhances the activity of glyoxalase I.
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DR   EMBL; J01347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S22872; S22872.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
PE   4: Predicted;
KW   Metal-binding; Plasmid; Zinc; Zinc-finger.
FT   CHAIN         1    106       Glyoxalase I activity-enhancing protein
FT                                GAC.
FT                                /FTId=PRO_0000087418.
FT   ZN_FING      76    102
FT   CONFLICT      9      9       R -> P (in Ref. 2).
FT   CONFLICT     82     82       Y -> T (in Ref. 2).
SQ   SEQUENCE   106 AA;  12868 MW;  638D06B216C1A02E CRC64;
     MYIYIQATRR YRCDVNSELY VRSSRCIFGS ARFRKRFEVP IPKFLFSRKY RNFRALLKTK
     SALKTHFQKT KNAPDCNELL KYCEYRFHKH CSKVSLCYIS LCYIPI
//
ID   GHRL_RAT                Reviewed;         117 AA.
AC   Q9QYH7; Q9ET69;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   10-FEB-2009, entry version 67.
DE   RecName: Full=Appetite-regulating hormone;
DE   AltName: Full=Growth hormone secretagogue;
DE   AltName: Full=Growth hormone-releasing peptide;
DE   AltName: Full=Motilin-related peptide;
DE   Contains:
DE     RecName: Full=Ghrelin;
DE   Contains:
DE     RecName: Full=Obestatin-23;
DE   Contains:
DE     RecName: Full=Obestatin-13;
DE   Flags: Precursor;
GN   Name=Ghrl;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 24-51,
RP   MASS SPECTROMETRY, AND ACYLATION AT SER-26.
RC   STRAIN=Sprague-Dawley; TISSUE=Stomach;
RX   MEDLINE=20067959; PubMed=10604470; DOI=10.1038/45230;
RA   Kojima M., Hosoda H., Date Y., Nakazato M., Matsuo H., Kangawa K.;
RT   "Ghrelin is a growth-hormone-releasing acylated peptide from
RT   stomach.";
RL   Nature 402:656-660(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF
RP   24-51, MASS SPECTROMETRY, AND ACYLATION AT SER-26.
RC   STRAIN=Sprague-Dawley; TISSUE=Stomach;
RX   MEDLINE=20357315; PubMed=10801861; DOI=10.1074/jbc.M002784200;
RA   Hosoda H., Kojima M., Matsuo H., Kangawa K.;
RT   "Purification and characterization of rat des-Gln14-ghrelin, a second
RT   endogenous ligand for the growth hormone secretagogue receptor.";
RL   J. Biol. Chem. 275:21995-22000(2000).
RN   [3]
RP   PROTEIN SEQUENCE OF 76-95, FUNCTION OF OBESTATIN, CHARACTERIZATION,
RP   AMIDATION, MASS SPECTROMETRY, AND INTERACTION WITH GPR39.
RX   PubMed=16284174; DOI=10.1126/science.1117255;
RA   Zhang J.V., Ren P.G., Avsian-Kretchmer O., Luo C.W., Rauch R.,
RA   Klein C., Hsueh A.J.;
RT   "Obestatin, a peptide encoded by the ghrelin gene, opposes ghrelin's
RT   effects on food intake.";
RL   Science 310:996-999(2005).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21092536; PubMed=11162448; DOI=10.1006/bbrc.2000.4039;
RA   Hosoda H., Kojima M., Matsuo H., Kangawa K.;
RT   "Ghrelin and des-acyl ghrelin: two major forms of rat ghrelin peptide
RT   in gastrointestinal tissue.";
RL   Biochem. Biophys. Res. Commun. 279:909-913(2000).
RN   [5]
RP   STRUCTURE-ACTIVITY RELATIONSHIP.
RX   MEDLINE=21433488; PubMed=11549267; DOI=10.1006/bbrc.2001.5553;
RA   Matsumoto M., Hosoda H., Kitajima Y., Morozumi N., Minamitake Y.,
RA   Tanaka S., Matsuo H., Kojima M., Hayashi Y., Kangawa K.;
RT   "Structure-activity relationship of ghrelin: pharmacological study of
RT   ghrelin peptides.";
RL   Biochem. Biophys. Res. Commun. 287:142-146(2001).
RN   [6]
RP   REVIEW.
RX   MEDLINE=21203998; PubMed=11306336; DOI=10.1016/S1043-2760(00)00362-3;
RA   Kojima M., Hosoda H., Matsuo H., Kangawa K.;
RT   "Ghrelin: discovery of the natural endogenous ligand for the growth
RT   hormone secretagogue receptor.";
RL   Trends Endocrinol. Metab. 12:118-122(2001).
RN   [7]
RP   FUNCTION OF OBESTATIN.
RX   PubMed=17289961; DOI=10.1126/science.1135047;
RA   Chartrel N., Alvear-Perez R., Leprince J., Iturrioz X.,
RA   Reaux-Le Goazigo A., Audinot V., Chomarat P., Coge F., Nosjean O.,
RA   Rodriguez M., Galizzi J.P., Boutin J.A., Vaudry H., Llorens-Cortes C.;
RT   "Comment on 'Obestatin, a peptide encoded by the ghrelin gene, opposes
RT   ghrelin's effects on food intake'.";
RL   Science 315:766-766(2007).
CC   -!- FUNCTION: Ghrelin is the ligand for growth hormone secretagogue
CC       receptor type 1 (GHSR). Induces the release of growth hormone from
CC       the pituitary. Has an appetite-stimulating effect, induces
CC       adiposity and stimulates gastric acid secretion. Involved in
CC       growth regulation.
CC   -!- FUNCTION: Obestatin may be the ligand for GPR39. May have an
CC       appetite-reducing effect resulting in decreased food intake. May
CC       reduce gastric emptying activity and jejunal motility.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Ghrelin;
CC         IsoId=Q9QYH7-1; Sequence=Displayed;
CC       Name=2; Synonyms=des-Gln14-ghrelin;
CC         IsoId=Q9QYH7-2; Sequence=VSP_003248;
CC   -!- TISSUE SPECIFICITY: Ghrelin is broadly expressed with higher
CC       expression in the stomach. Very low levels are detected in the
CC       hypothalamus, heart, lung, pancreas, intestine and adipose tissue.
CC       Obestatin is most highly expressed in jejunum, and also found in
CC       duodenum, stomach, pituitary, ileum, liver, hypothalamus and
CC       heart. Expressed in low levels in pancreas, cerebellum, cerebrum,
CC       kidney, testis, ovary colon and lung.
CC   -!- PTM: O-octanoylation is essential for ghrelin activity. The
CC       replacement of Ser-26 by aromatic tryptophan preserves ghrelin
CC       activity.
CC   -!- PTM: Amidation of Leu-98 is essential for obestatin activity.
CC   -!- MASS SPECTROMETRY: Mass=3314.9; Mass_error=0.7;
CC       Method=Electrospray; Range=24-51 (Q9QYH7-1);
CC       Source=PubMed:10604470;
CC   -!- MASS SPECTROMETRY: Mass=3187.1; Mass_error=0.6;
CC       Method=Electrospray; Range=24-50 (Q9QYH7-2);
CC       Source=PubMed:10801861;
CC   -!- MASS SPECTROMETRY: Mass=2516.3; Method=Unknown; Range=76-98;
CC       Source=PubMed:16284174;
CC   -!- SIMILARITY: Belongs to the motilin family.
CC   -!- CAUTION: PubMed:16284174 reports obestatin as ligand of GPR39.
CC       However, PubMed:17289961 and others are unable to reproduce these
CC       results. It also seems to be unclear whether obestatin has
CC       opposite effects on food intake compared with ghrelin.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Gut feelings - Issue 66
CC       of January 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt066.shtml";
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DR   EMBL; AB029433; BAA89370.1; -; mRNA.
DR   EMBL; AB035699; BAB11956.1; -; mRNA.
DR   IPI; IPI00214108; -.
DR   PIR; B59316; B59316.
DR   RefSeq; NP_067701.1; -.
DR   UniGene; Rn.42103; -.
DR   Ensembl; ENSRNOG00000010349; Rattus norvegicus.
DR   GeneID; 59301; -.
DR   KEGG; rno:59301; -.
DR   NMPDR; fig|10116.3.peg.21997; -.
DR   RGD; 632283; Ghrl.
DR   HOVERGEN; Q9QYH7; -.
DR   NextBio; 611837; -.
DR   ArrayExpress; Q9QYH7; -.
DR   GermOnline; ENSRNOG00000010349; Rattus norvegicus.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IC:UniProtKB.
DR   GO; GO:0001664; F:G-protein-coupled receptor binding; IPI:UniProtKB.
DR   GO; GO:0016608; F:growth hormone-releasing hormone activity; IDA:UniProtKB.
DR   GO; GO:0030296; F:protein tyrosine kinase activator activity; ISS:UniProtKB.
DR   GO; GO:0008154; P:actin polymerization or depolymerization; ISS:UniProtKB.
DR   GO; GO:0000187; P:activation of MAPK activity; ISS:UniProtKB.
DR   GO; GO:0008343; P:adult feeding behavior; ISS:HGNC.
DR   GO; GO:0006916; P:anti-apoptosis; IDA:UniProtKB.
DR   GO; GO:0046697; P:decidualization; ISS:UniProtKB.
DR   GO; GO:0007204; P:elevation of cytosolic calcium ion concentr...; IDA:UniProtKB.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signalin...; IDA:UniProtKB.
DR   GO; GO:0001696; P:gastric acid secretion; IDA:UniProtKB.
DR   GO; GO:0001937; P:negative regulation of endothelial cell pro...; ISS:UniProtKB.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; IDA:MGI.
DR   GO; GO:0032691; P:negative regulation of interleukin-1 beta p...; ISS:UniProtKB.
DR   GO; GO:0045409; P:negative regulation of interleukin-6 biosyn...; ISS:UniProtKB.
DR   GO; GO:0042536; P:negative regulation of tumor necrosis facto...; ISS:UniProtKB.
DR   GO; GO:0032100; P:positive regulation of appetite; ISS:HGNC.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IDA:UniProtKB.
DR   GO; GO:0043627; P:response to estrogen stimulus; ISS:UniProtKB.
DR   InterPro; IPR006737; Motilin_assoc.
DR   InterPro; IPR006738; Motilin_ghrelin.
DR   InterPro; IPR005441; Preproghrelin.
DR   PANTHER; PTHR14122; Preproghrelin; 1.
DR   Pfam; PF04643; Motilin_assoc; 1.
DR   Pfam; PF04644; Motilin_ghrelin; 1.
DR   PRINTS; PR01624; GHRELIN.
DR   ProDom; PD332162; Preproghrelin; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Amidation; Direct protein sequencing; Hormone;
KW   Lipoprotein; Secreted; Signal.
FT   SIGNAL        1     23
FT   PEPTIDE      24     51       Ghrelin.
FT                                /FTId=PRO_0000019209.
FT   PROPEP       52     75       Removed in mature form.
FT                                /FTId=PRO_0000019210.
FT   PEPTIDE      76     98       Obestatin-23.
FT                                /FTId=PRO_0000045146.
FT   PEPTIDE      86     98       Obestatin-13 (Probable).
FT                                /FTId=PRO_0000045147.
FT   PROPEP       99    117       Removed in mature form.
FT                                /FTId=PRO_0000045148.
FT   MOD_RES      98     98       Leucine amide.
FT   LIPID        26     26       O-octanoyl serine.
FT   VAR_SEQ      37     37       Missing (in isoform 2).
FT                                /FTId=VSP_003248.
SQ   SEQUENCE   117 AA;  13176 MW;  8857546FE51A7691 CRC64;
     MVSSATICSL LLLSMLWMDM AMAGSSFLSP EHQKAQQRKE SKKPPAKLQP RALEGWLHPE
     DRGQAEEAEE ELEIRFNAPF DVGIKLSGAQ YQQHGRALGK FLQDILWEEV KEAPANK
//
ID   MTBB1_METBA             Reviewed;         467 AA.
AC   O93661; Q9C4B8;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   25-NOV-2008, entry version 40.
DE   RecName: Full=Dimethylamine methyltransferase mtbB1;
DE            Short=DMA methyltransferase 1;
DE            Short=DMAMT 1;
DE            EC=2.1.1.-;
GN   Name=mtbB1;
OS   Methanosarcina barkeri.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20 AND
RP   460-467.
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   MEDLINE=20225851; PubMed=10762254;
RX   DOI=10.1128/JB.182.9.2520-2529.2000;
RA   Paul L., Ferguson D.J. Jr., Krzycki J.A.;
RT   "The trimethylamine methyltransferase gene and multiple dimethylamine
RT   methyltransferase genes of Methanosarcina barkeri contain in-frame and
RT   read-through amber codons.";
RL   J. Bacteriol. 182:2520-2529(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-467.
RA   Srinivasan G., Paul L., Lienard T., Gottschalk G., Krzycki J.A.;
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 1-20, AND CHARACTERIZATION.
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   MEDLINE=20435871; PubMed=10852929; DOI=10.1074/jbc.M910218199;
RA   Ferguson D.J. Jr., Gorlatova N., Grahame D.A., Krzycki J.A.;
RT   "Reconstitution of dimethylamine:coenzyme M methyl transfer with a
RT   discrete corrinoid protein and two methyltransferases purified from
RT   Methanosarcina barkeri.";
RL   J. Biol. Chem. 275:29053-29060(2000).
RN   [4]
RP   PYRROLYSINE AT PYL-356.
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=16096277; DOI=10.1074/jbc.M506402200;
RA   Soares J.A., Zhang L., Pitsch R.L., Kleinholz N.M., Jones R.B.,
RA   Wolff J.J., Amster J., Green-Church K.B., Krzycki J.A.;
RT   "The residue mass of L-pyrrolysine in three distinct methylamine
RT   methyltransferases.";
RL   J. Biol. Chem. 280:36962-36969(2005).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from
CC       dimethylamine to the corrinoid cofactor of mtbC.
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from dimethylamine.
CC   -!- SUBUNIT: May form homotetramers or homopentamers.
CC   -!- SIMILARITY: Belongs to the dimethylamine methyltransferase family.
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DR   EMBL; AF102623; AAD14633.1; -; Genomic_DNA.
DR   EMBL; AF337056; AAK29407.1; -; Genomic_DNA.
DR   BioCyc; MetaCyc:MON-12212; -.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR   GO; GO:0015948; P:methanogenesis; IEA:InterPro.
DR   InterPro; IPR012653; Dimeth_MeTrfase_PyL.
DR   TIGRFAMs; TIGR02368; dimeth_PyL; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Methanogenesis; Methyltransferase;
KW   Pyrrolysine; Transferase.
FT   CHAIN         1    467       Dimethylamine methyltransferase mtbB1.
FT                                /FTId=PRO_0000216558.
FT   NON_STD     356    356       Pyrrolysine.
SQ   SEQUENCE   467 AA;  50228 MW;  A865C10BF8E252BA CRC64;
     MATEYALRMG DGKRVYLTKE KIVSEIEAGT ADAADLGEIP ALSANEMDKL AEILMMPGKT
     VSVEQGMEIP VTHDIGTIRL DGDQGNSGVG IPSSRLVGCM THERAFGADT MELGHIDYSF
     KPVKPVVSNE CQAMEVCQQN MVIPLFYGAM PNMGLYYTPD GPFENPGDLM KAFKIQEAWE
     SMEHAAEHLT RDTVWVMQKL FASGADGVNF DTTGAAGDGD MYGTLHAIEA LRKEFPDMYI
     EAGMAGECVL GMHGNLQYDG VTLAGLWPHQ QAPLVAKAGA NVFGPVCNTN TSKTSAWNLA
     RAVTFMKAAV EASPIPCHVD MGMGVGGIPM LETPPIDAVT RASKAMVEIA GVDGIOIGVG
     DPLGMPIAHI MASGMTGMRA AGDLVARMEF SKNMRIGEAK EYVAKKLGVD KMDLVDEHVM
     RELREELDIG IITSVPGAAK GIAAKMNIEK LLDIKINSCN LFRKQIA
//
ID   NIFA_BRAJA              Reviewed;         582 AA.
AC   P05407;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2003, sequence version 4.
DT   25-NOV-2008, entry version 69.
DE   RecName: Full=Nif-specific regulatory protein;
GN   Name=nifA; OrderedLocusNames=blr2037;
OS   Bradyrhizobium japonicum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88040468; PubMed=3313281; DOI=10.1093/nar/15.20.8479;
RA   Thoeny B., Fischer H.-M., Anthamatten D., Bruderer T., Hennecke H.;
RT   "The symbiotic nitrogen fixation regulatory operon (fixRnifA) of
RT   Bradyrhizobium japonicum is expressed aerobically and is subject to a
RT   novel, nifA-independent type of activation.";
RL   Nucleic Acids Res. 15:8479-8499(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA 110;
RX   MEDLINE=22484998; PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T.,
RA   Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K.,
RA   Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M.,
RA   Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
RN   [3]
RP   METAL-BINDING.
RX   MEDLINE=88189813; PubMed=3357773; DOI=10.1093/nar/16.5.2207;
RA   Fischer H.-M., Bruderer T., Hennecke H.;
RT   "Essential and non-essential domains in the Bradyrhizobium japonicum
RT   NifA protein: identification of indispensable cysteine residues
RT   potentially involved in redox reactivity and/or metal binding.";
RL   Nucleic Acids Res. 16:2207-2224(1988).
RN   [4]
RP   METAL-BINDING.
RX   MEDLINE=90005957; PubMed=2792368; DOI=10.1016/0014-5793(89)81083-X;
RA   Fischer H.-M., Fritsche S., Herzog B., Hennecke H.;
RT   "Critical spacing between two essential cysteine residues in the
RT   interdomain linker of the Bradyrhizobium japonicum NifA protein.";
RL   FEBS Lett. 255:167-171(1989).
CC   -!- FUNCTION: Required for activation of most nif operons, which are
CC       directly involved in nitrogen fixation.
CC   -!- SUBUNIT: Interacts with sigma-54.
CC   -!- SIMILARITY: Contains 1 GAF domain.
CC   -!- SIMILARITY: Contains 1 sigma-54 factor interaction domain.
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DR   EMBL; X06167; CAA29532.1; -; Genomic_DNA.
DR   EMBL; X06167; CAA29531.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000040; BAC47302.1; ALT_INIT; Genomic_DNA.
DR   PIR; S01066; S01066.
DR   RefSeq; NP_768677.1; -.
DR   GeneID; 1055528; -.
DR   GenomeReviews; BA000040_GR; blr2037.
DR   KEGG; bja:blr2037; -.
DR   HOGENOM; P05407; -.
DR   BioCyc; BJAP224911:BLR2037-MON; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0016563; F:transcription activator activity; IEA:InterPro.
DR   GO; GO:0003700; F:transcription factor activity; IEA:InterPro.
DR   GO; GO:0008134; F:transcription factor binding; IEA:InterPro.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0000160; P:two-component signal transduction system (p...; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; AAA+_ATPase_core.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR010113; Nif-specific_regulatory_prot.
DR   InterPro; IPR002078; RNA_pol_sigma_54_int.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   PRINTS; PR01590; HTHFIS.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00065; GAF; 1.
DR   TIGRFAMs; TIGR01817; nifA; 1.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   1: Evidence at protein level;
KW   Activator; ATP-binding; Complete proteome; DNA-binding; Metal-binding;
KW   Nitrogen fixation; Nucleotide-binding; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN         1    582       Nif-specific regulatory protein.
FT                                /FTId=PRO_0000081305.
FT   DOMAIN       46    188       GAF.
FT   DOMAIN      230    458       Sigma-54 factor interaction.
FT   NP_BIND     258    265       ATP (Potential).
FT   NP_BIND     321    330       ATP (Potential).
FT   DNA_BIND    554    573       H-T-H motif (By similarity).
FT   REGION      459    539       Inter-domain linker.
FT   REGION      540    582       C-terminal DNA-binding domain.
FT   METAL       472    472
FT   METAL       477    477
FT   CONFLICT    223    224       KQ -> NE (in Ref. 1; CAA29532/CAA29531).
SQ   SEQUENCE   582 AA;  63098 MW;  D3083178139EB812 CRC64;
     MLHIPSSSER PASQPEPERA PPGEPSHESA LAGIYEISKI LNAPGRLEVT LANVLGLLQS
     FVQMRHGLVS LFNDDGVPEL TVGAGWSEGT DERYRTCVPQ KAIHEIVATG RSLMVENVAA
     ETAFSAADRE VLGASDSIPV AFIGVPIRVD STVVGTLTID RIPEGSSSLL EYDARLLAMV
     ANVIGQTIKL HRLFAGDREQ SLVDKDRLEK QTVDRGPPAR ERKQLQAHGI IGDSPALSAL
     LEKIVVVARS NSTVLLRGES GTGKELVAKA IHESSVRAKR PFVKLNCAAL PETVLESELF
     GHEKGAFTGA VSARKGRFEL ADKGTLFLDE IGEISPPFQA KLLRVLQEQE FERVGSNHTI
     KVDVRVIAAT NRNLEEAVAR SEFRADLYYR ISVVPLLLPP LRERRSDIPL LAREFLRKFN
     SENGRSLTLE ASAIDVLMSC KFPGNVRELE NCIERTATLS AGTSIVRSDF ACSQGQCLST
     TLWKSTSYGK TDPAAPMQPV PAKSIIPLAE TAPPPQAVCE PGSLAPSGTV LVSGARMADR
     ERVVAAMEKS GWVQAKAARL LGLTPRQVGY ALRKYGIEIK RF
//
ID   UBX_DROME               Reviewed;         389 AA.
AC   P83949; P02834; Q9TX83; Q9VER4; Q9VER5;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   20-JAN-2009, entry version 61.
DE   RecName: Full=Homeotic protein ultrabithorax;
GN   Name=Ubx; ORFNames=CG10388;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Canton-S;
RA   Weinzierl R., Axton J.M., Ghysen A., Akam M.;
RT   "Ultrabithorax mutations in constant and variable regions of the
RT   protein coding sequence.";
RL   Genes Dev. 1:386-397(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IA; IB; IIA; IIB; IVA AND IVB).
RX   MEDLINE=89232720; PubMed=2565858;
RA   Kornfeld K., Saint R.B., Beachy P.A., Harte P.J., Peattie D.A.,
RA   Hogness D.S.;
RT   "Structure and expression of a family of Ultrabithorax mRNAs generated
RT   by alternative splicing and polyadenylation in Drosophila.";
RL   Genes Dev. 3:243-258(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS IA; IB; IIA; IIB AND IVA).
RC   STRAIN=Canton-S;
RX   MEDLINE=95396803; PubMed=7667301;
RA   Martin C.H., Mayeda C.A., Davis C.A., Ericsson C.L., Knafels J.D.,
RA   Mathog D.R., Celniker S.E., Lewis E.B., Palazzolo M.J.;
RT   "Complete sequence of the bithorax complex of Drosophila.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:8398-8402(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [5]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RX   MEDLINE=22426069; PubMed=12537572;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IA).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
RA   Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA   George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA   Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA   Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA   Celniker S.E.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 290-389.
RX   MEDLINE=84205674; PubMed=6327065; DOI=10.1016/0092-8674(84)90370-2;
RA   McGinnis W., Garber R.L., Wirz J., Kuroiwa A., Gehring W.J.;
RT   "A homologous protein-coding sequence in Drosophila homeotic genes and
RT   its conservation in other metazoans.";
RL   Cell 37:403-408(1984).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 290-384.
RX   MEDLINE=84248068; PubMed=6330741;
RA   Scott M.P., Weiner A.J.;
RT   "Structural relationships among genes that control development:
RT   sequence homology between the Antennapedia, Ultrabithorax, and fushi
RT   tarazu loci of Drosophila.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:4115-4119(1984).
RN   [9]
RP   NUCLEOTIDE SEQUENCE OF 294-355.
RX   MEDLINE=93259465; PubMed=8098307;
RA   Chan S.K., Mann R.S.;
RT   "The segment identity functions of Ultrabithorax are contained within
RT   its homeo domain and carboxy-terminal sequences.";
RL   Genes Dev. 7:796-811(1993).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RX   PubMed=16453777;
RA   Saari G., Bienz M.;
RT   "The structure of the ultrabithorax promoter of Drosophila
RT   melanogaster.";
RL   EMBO J. 6:1775-1779(1987).
RN   [11]
RP   DNA-BINDING.
RX   MEDLINE=91216112; PubMed=1673656;
RA   Ekker S.C., Young K.E., von Kessler D.P., Beachy P.A.;
RT   "Optimal DNA sequence recognition by the Ultrabithorax homeodomain of
RT   Drosophila.";
RL   EMBO J. 10:1179-1186(1991).
RN   [12]
RP   ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC   STRAIN=Oregon-R; TISSUE=Embryo;
RX   MEDLINE=94274046; PubMed=7911773;
RA   Bomze H.M., Lopez A.J.;
RT   "Evolutionary conservation of the structure and expression of
RT   alternatively spliced Ultrabithorax isoforms from Drosophila.";
RL   Genetics 136:965-977(1994).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170; SER-174 AND
RP   SER-177, AND MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 233-356 IN COMPLEX WITH EXD.
RX   MEDLINE=99165220; PubMed=10067897; DOI=10.1038/17833;
RA   Passner J.M., Ryoo H.-D., Shen L., Mann R.S., Aggarwal A.K.;
RT   "Structure of a DNA-bound Ultrabithorax-Extradenticle homeodomain
RT   complex.";
RL   Nature 397:714-719(1999).
CC   -!- FUNCTION: Sequence-specific transcription factor which is part of
CC       a developmental regulatory system that provides cells with
CC       specific positional identities on the anterior-posterior axis.
CC       Binds the consensus region 5'-TTAAT[GT][GA]-3'. This homeotic
CC       protein controls development of the cells in the posterior
CC       thoracic and first abdominal segments. It activates the synthesis
CC       of the decapentaplegic (DPP) growth factor.
CC   -!- INTERACTION:
CC       Q06453:al; NbExp=1; IntAct=EBI-202590, EBI-188244;
CC       Q9U980:Cbp80; NbExp=1; IntAct=EBI-202590, EBI-499094;
CC       Q961D1:CycK; NbExp=1; IntAct=EBI-202590, EBI-130995;
CC       Q9TW27:DIP1; NbExp=5; IntAct=EBI-202571, EBI-443968;
CC       P40427:exd; NbExp=1; IntAct=EBI-202590, EBI-101537;
CC       P14003:h; NbExp=1; IntAct=EBI-202590, EBI-123011;
CC       Q23993:nmo; NbExp=1; IntAct=EBI-202590, EBI-876224;
CC       O96660:Smox; NbExp=1; IntAct=EBI-202590, EBI-145058;
CC       Q9V435:yuri; NbExp=1; IntAct=EBI-202571, EBI-175266;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=IB; Synonyms=A;
CC         IsoId=P83949-1, P02834-1;
CC         Sequence=Displayed;
CC       Name=IA; Synonyms=E;
CC         IsoId=P83949-2, P02834-2;
CC         Sequence=VSP_002405;
CC       Name=IIA; Synonyms=D;
CC         IsoId=P83949-3, P02834-3;
CC         Sequence=VSP_002406;
CC       Name=IIB; Synonyms=C;
CC         IsoId=P83949-4, P02834-4;
CC         Sequence=VSP_002408;
CC       Name=IVA; Synonyms=B;
CC         IsoId=P83949-5, P02834-5;
CC         Sequence=VSP_002407;
CC       Name=IVB; Synonyms=F;
CC         IsoId=P83949-6, P02834-6;
CC         Sequence=VSP_002409;
CC   -!- TISSUE SPECIFICITY: In the embryo, expression is seen in the
CC       epidermis, somatic and visceral mesoderm, and the peripheral and
CC       central nervous system.
CC   -!- DOMAIN: The QA motif is able to mediate transcriptional repression
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the Antp homeobox family.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
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DR   EMBL; X05723; CAA29194.1; -; Genomic_DNA.
DR   EMBL; X05724; CAA29194.1; JOINED; Genomic_DNA.
DR   EMBL; X05725; CAA29194.1; JOINED; Genomic_DNA.
DR   EMBL; X05727; CAA29194.1; JOINED; Genomic_DNA.
DR   EMBL; X76210; CAA53803.1; -; mRNA.
DR   EMBL; U31961; AAA84412.1; -; Genomic_DNA.
DR   EMBL; U31961; AAA84411.1; -; Genomic_DNA.
DR   EMBL; U31961; AAA84410.1; -; Genomic_DNA.
DR   EMBL; U31961; AAA84409.1; -; Genomic_DNA.
DR   EMBL; U31961; AAA84408.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF55355.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAF55356.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13717.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13718.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13719.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAS65158.1; -; Genomic_DNA.
DR   EMBL; BT010241; AAQ23559.1; -; mRNA.
DR   EMBL; K01963; AAA29008.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; K01959; AAA28615.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X05427; CAA29009.1; -; Genomic_DNA.
DR   PIR; B27867; B27867.
DR   PIR; D26995; D26995.
DR   RefSeq; NP_536748.1; -.
DR   RefSeq; NP_536752.1; -.
DR   RefSeq; NP_732171.1; -.
DR   RefSeq; NP_732172.1; -.
DR   RefSeq; NP_732173.1; -.
DR   RefSeq; NP_996219.1; -.
DR   UniGene; Dm.21668; -.
DR   PDB; 1B8I; X-ray; 2.40 A; A=290-356.
DR   PDBsum; 1B8I; -.
DR   IntAct; P83949; 26.
DR   Ensembl; CG10388; Drosophila melanogaster.
DR   GeneID; 42034; -.
DR   KEGG; dme:Dmel_CG10388; -.
DR   NMPDR; fig|7227.3.peg.13195; -.
DR   FlyBase; FBgn0003944; Ubx.
DR   HOGENOM; P83949; -.
DR   BioCyc; DMEL-XXX-02:DMEL-XXX-02-011979-MON; -.
DR   NextBio; 826845; -.
DR   ArrayExpress; P83949; -.
DR   GermOnline; CG10388; Drosophila melanogaster.
DR   GO; GO:0005667; C:transcription factor complex; NAS:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:transcription factor activity; IEA:InterPro.
DR   GO; GO:0035052; P:dorsal vessel aortic cell fate commitment; TAS:FlyBase.
DR   GO; GO:0001706; P:endoderm formation; TAS:FlyBase.
DR   GO; GO:0007482; P:haltere development; IMP:FlyBase.
DR   GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR   GO; GO:0007501; P:mesodermal cell fate specification; IMP:FlyBase.
DR   GO; GO:0007494; P:midgut development; TAS:FlyBase.
DR   GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR   GO; GO:0045570; P:regulation of imaginal disc growth; IMP:FlyBase.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0010092; P:specification of organ identity; IMP:FlyBase.
DR   GO; GO:0007384; P:specification of segmental identity, thorax; IMP:FlyBase.
DR   InterPro; IPR001827; Antennapedia.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Pfam; PF00046; Homeobox; 1.
DR   PRINTS; PR00025; ANTENNAPEDIA.
DR   PRINTS; PR00024; HOMEOBOX.
DR   ProDom; PD000010; Homeobox; 1.
DR   SMART; SM00389; HOX; 1.
DR   PROSITE; PS00032; ANTENNAPEDIA; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Complete proteome;
KW   Developmental protein; DNA-binding; Homeobox; Nucleus; Phosphoprotein;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN         1    389       Homeotic protein ultrabithorax.
FT                                /FTId=PRO_0000200268.
FT   DNA_BIND    295    354       Homeobox.
FT   MOTIF       239    244       Antp-type hexapeptide.
FT   MOTIF       368    383       QA.
FT   COMPBIAS     33     39       Poly-Ala.
FT   COMPBIAS    111    129       Poly-Gly.
FT   COMPBIAS    322    325       Poly-Arg.
FT   MOD_RES     170    170       Phosphothreonine.
FT   MOD_RES     174    174       Phosphoserine.
FT   MOD_RES     177    177       Phosphoserine.
FT   VAR_SEQ     248    290       Missing (in isoform IVA).
FT                                /FTId=VSP_002407.
FT   VAR_SEQ     248    273       Missing (in isoform IIA).
FT                                /FTId=VSP_002406.
FT   VAR_SEQ     248    256       Missing (in isoform IA).
FT                                /FTId=VSP_002405.
FT   VAR_SEQ     257    290       Missing (in isoform IVB).
FT                                /FTId=VSP_002409.
FT   VAR_SEQ     258    274       Missing (in isoform IIB).
FT                                /FTId=VSP_002408.
FT   CONFLICT     75     75       N -> Y (in Ref. 3; AAA84412/AAA84411/
FT                                AAA84410/AAA84409/AAA84408).
FT   CONFLICT    330    330       H -> Y (in Ref. 7; AAA28615).
FT   CONFLICT    340    340       K -> E (in Ref. 7; AAA28615).
FT   HELIX       304    316
FT   HELIX       322    331
FT   HELIX       336    351
SQ   SEQUENCE   389 AA;  40040 MW;  D452E8FFE55D8F53 CRC64;
     MNSYFEQASG FYGHPHQATG MAMGSGGHHD QTASAAAAAY RGFPLSLGMS PYANHHLQRT
     TQDSPYDASI TAACNKIYGD GAGAYKQDCL NIKADAVNGY KDIWNTGGSN GGGGGGGGGG
     GGGAGGTGGA GNANGGNAAN ANGQNNPAGG MPVRPSACTP DSRVGGYLDT SGGSPVSHRG
     GSAGGNVSVS GGNGNAGGVQ SGVGVAGAGT AWNANCTISG AAAQTAAASS LHQASNHTFY
     PWMAIAGECP EDPTKSKIRS DLTQYGGIST DMGKRYSESL AGSLLPDWLG TNGLRRRGRQ
     TYTRYQTLEL EKEFHTNHYL TRRRRIEMAH ALCLTERQIK IWFQNRRMKL KKEIQAIKEL
     NEQEKQAQAQ KAAAAAAAAA AVQGGHLDQ
//