ID   LAMA1_HUMAN             Reviewed;        3075 AA.
AC   P25391;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 2.
DT   27-MAR-2024, entry version 225.
DE   RecName: Full=Laminin subunit alpha-1;
DE   AltName: Full=Laminin A chain;
DE   AltName: Full=Laminin-1 subunit alpha;
DE   AltName: Full=Laminin-3 subunit alpha;
DE   AltName: Full=S-laminin subunit alpha;
DE            Short=S-LAM alpha;
DE   Flags: Precursor;
GN   Name=LAMA1; Synonyms=LAMA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-674; VAL-1340; THR-1876 AND
RP   GLU-2002.
RX   PubMed=1714537; DOI=10.1016/s0934-8832(11)80153-8;
RA   Haaparanta T., Uitto J., Ruoslahti E., Engvall E.;
RT   "Molecular cloning of the cDNA encoding human laminin A chain.";
RL   Matrix 11:151-160(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177791; DOI=10.1038/nature03983;
RA   Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA   Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA   Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA   Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA   Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA   Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA   Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA   Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 18.";
RL   Nature 437:551-555(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-2628, AND VARIANTS THR-674; THR-1876 AND
RP   GLU-2002.
RX   PubMed=2049067; DOI=10.1042/bj2760369;
RA   Nissinen M., Vuolteenaho R., Boot-Handford R., Kallunki P., Tryggvason K.;
RT   "Primary structure of the human laminin A chain. Limited expression in
RT   human tissues.";
RL   Biochem. J. 276:369-379(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2397-3072.
RX   PubMed=2733383;
RA   Olsen D., Nagayoshi T., Fazio M., Peltonen J., Jaakkola S., Sanborn D.,
RA   Sasaki T., Kuivaniemi H., Chu M.-L., Deutzmann R., Timpl R., Uitto J.;
RT   "Human laminin: cloning and sequence analysis of cDNAs encoding A, B1 and
RT   B2 chains, and expression of the corresponding genes in human skin and
RT   cultured cells.";
RL   Lab. Invest. 60:772-782(1989).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2243.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [6]
RP   INVOLVEMENT IN PTBHS.
RX   PubMed=25105227; DOI=10.1016/j.ajhg.2014.07.007;
RG   University of Washington Center for Mendelian Genomics;
RG   Care4Rare Canada;
RA   Aldinger K.A., Mosca S.J., Tetreault M., Dempsey J.C., Ishak G.E.,
RA   Hartley T., Phelps I.G., Lamont R.E., O'Day D.R., Basel D., Gripp K.W.,
RA   Baker L., Stephan M.J., Bernier F.P., Boycott K.M., Majewski J.,
RA   Parboosingh J.S., Innes A.M., Doherty D.;
RT   "Mutations in LAMA1 cause cerebellar dysplasia and cysts with and without
RT   retinal dystrophy.";
RL   Am. J. Hum. Genet. 95:227-234(2014).
RN   [7]
RP   PHOSPHORYLATION.
RX   PubMed=25171405; DOI=10.1016/j.cell.2014.06.048;
RA   Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr.,
RA   Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L., Asara J.M.,
RA   Dixon J.E., Yeo C.Y., Whitman M.;
RT   "A secreted tyrosine kinase acts in the extracellular environment.";
RL   Cell 158:1033-1044(2014).
CC   -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC       thought to mediate the attachment, migration and organization of cells
CC       into tissues during embryonic development by interacting with other
CC       extracellular matrix components.
CC   -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC       different polypeptide chains (alpha, beta, gamma), which are bound to
CC       each other by disulfide bonds into a cross-shaped molecule comprising
CC       one long and three short arms with globules at each end. Alpha-1 is a
CC       subunit of laminin-1 (laminin-111 or EHS laminin) and laminin-3
CC       (laminin-121 or S-laminin).
CC   -!- INTERACTION:
CC       P25391; Q8BDF8: p4c; Xeno; NbExp=2; IntAct=EBI-2529668, EBI-7167339;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane. Note=Major component.
CC   -!- DOMAIN: The alpha-helical domains I and II are thought to interact with
CC       other laminin chains to form a coiled coil structure.
CC   -!- DOMAIN: Domains VI, IV and G are globular.
CC   -!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
CC       {ECO:0000269|PubMed:25171405}.
CC   -!- DISEASE: Poretti-Boltshauser syndrome (PTBHS) [MIM:615960]: An
CC       autosomal recessive disorder characterized by cerebellar dysplasia,
CC       cerebellar vermis atrophy, cerebellar cysts in most patients, high
CC       myopia, variable retinal dystrophy, and eye movement abnormalities
CC       including strabismus, ocular apraxia, nystagmus. Affected individuals
CC       have ataxia, delayed motor development, language impairment, and
CC       intellectual disability with variable severity.
CC       {ECO:0000269|PubMed:25105227}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
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DR   EMBL; AP002409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP005062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP005210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X58531; CAA41418.1; -; mRNA.
DR   CCDS; CCDS32787.1; -.
DR   PIR; S14458; S14458.
DR   RefSeq; NP_005550.2; NM_005559.3.
DR   SMR; P25391; -.
DR   BioGRID; 129792; 61.
DR   ComplexPortal; CPX-1770; Laminin-111 complex.
DR   ComplexPortal; CPX-1772; Laminin-121 complex.
DR   DIP; DIP-29324N; -.
DR   IntAct; P25391; 36.
DR   MINT; P25391; -.
DR   STRING; 9606.ENSP00000374309; -.
DR   ChEMBL; CHEMBL4523594; -.
DR   DrugBank; DB06245; Lanoteplase.
DR   GlyConnect; 1438; 11 N-Linked glycans (1 site).
DR   GlyCosmos; P25391; 7 sites, 11 glycans.
DR   GlyGen; P25391; 12 sites, 11 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P25391; -.
DR   PhosphoSitePlus; P25391; -.
DR   BioMuta; LAMA1; -.
DR   DMDM; 281185471; -.
DR   EPD; P25391; -.
DR   jPOST; P25391; -.
DR   MassIVE; P25391; -.
DR   MaxQB; P25391; -.
DR   PaxDb; 9606-ENSP00000374309; -.
DR   PeptideAtlas; P25391; -.
DR   ProteomicsDB; 54269; -.
DR   Pumba; P25391; -.
DR   Antibodypedia; 4123; 364 antibodies from 30 providers.
DR   DNASU; 284217; -.
DR   Ensembl; ENST00000389658.4; ENSP00000374309.3; ENSG00000101680.16.
DR   GeneID; 284217; -.
DR   KEGG; hsa:284217; -.
DR   MANE-Select; ENST00000389658.4; ENSP00000374309.3; NM_005559.4; NP_005550.2.
DR   UCSC; uc002knm.3; human.
DR   AGR; HGNC:6481; -.
DR   CTD; 284217; -.
DR   DisGeNET; 284217; -.
DR   GeneCards; LAMA1; -.
DR   HGNC; HGNC:6481; LAMA1.
DR   HPA; ENSG00000101680; Tissue enhanced (ovary, testis).
DR   MalaCards; LAMA1; -.
DR   MIM; 150320; gene.
DR   MIM; 615960; phenotype.
DR   neXtProt; NX_P25391; -.
DR   OpenTargets; ENSG00000101680; -.
DR   Orphanet; 370022; Ataxia-intellectual disability-oculomotor apraxia-cerebellar cysts syndrome.
DR   PharmGKB; PA30270; -.
DR   VEuPathDB; HostDB:ENSG00000101680; -.
DR   eggNOG; KOG1836; Eukaryota.
DR   GeneTree; ENSGT00940000157124; -.
DR   HOGENOM; CLU_000301_0_0_1; -.
DR   InParanoid; P25391; -.
DR   OMA; TVRQHVH; -.
DR   OrthoDB; 90222at2759; -.
DR   PhylomeDB; P25391; -.
DR   TreeFam; TF335359; -.
DR   PathwayCommons; P25391; -.
DR   Reactome; R-HSA-3000157; Laminin interactions.
DR   Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   Reactome; R-HSA-373760; L1CAM interactions.
DR   Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR   SignaLink; P25391; -.
DR   SIGNOR; P25391; -.
DR   BioGRID-ORCS; 284217; 11 hits in 1148 CRISPR screens.
DR   ChiTaRS; LAMA1; human.
DR   GeneWiki; Laminin,_alpha_1; -.
DR   GenomeRNAi; 284217; -.
DR   Pharos; P25391; Tbio.
DR   PRO; PR:P25391; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; P25391; Protein.
DR   Bgee; ENSG00000101680; Expressed in ventricular zone and 106 other cell types or tissues.
DR   ExpressionAtlas; P25391; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR   GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005606; C:laminin-1 complex; IDA:UniProtKB.
DR   GO; GO:0005608; C:laminin-3 complex; IPI:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:CAFA.
DR   GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; NAS:ComplexPortal.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; ISS:UniProtKB.
DR   GO; GO:0043208; F:glycosphingolipid binding; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
DR   GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
DR   GO; GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; NAS:ComplexPortal.
DR   GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; NAS:ComplexPortal.
DR   GO; GO:0051149; P:positive regulation of muscle cell differentiation; NAS:ComplexPortal.
DR   GO; GO:0110011; P:regulation of basement membrane organization; NAS:ComplexPortal.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR   GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR   GO; GO:0061304; P:retinal blood vessel morphogenesis; IEA:Ensembl.
DR   CDD; cd00055; EGF_Lam; 14.
DR   CDD; cd00110; LamG; 5.
DR   Gene3D; 2.60.120.200; -; 5.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 14.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009254; Laminin_aI.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10574:SF443; -; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00052; Laminin_B; 2.
DR   Pfam; PF00053; Laminin_EGF; 17.
DR   Pfam; PF00054; Laminin_G_1; 5.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 12.
DR   SMART; SM00180; EGF_Lam; 17.
DR   SMART; SM00281; LamB; 2.
DR   SMART; SM00282; LamG; 5.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 15.
DR   PROSITE; PS00022; EGF_1; 11.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 15.
DR   PROSITE; PS50027; EGF_LAM_2; 15.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR   PROSITE; PS51115; LAMININ_IVA; 2.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
DR   Genevisible; P25391; HS.
PE   1: Evidence at protein level;
KW   Basement membrane; Cell adhesion; Coiled coil; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW   Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..3075
FT                   /note="Laminin subunit alpha-1"
FT                   /id="PRO_0000017054"
FT   DOMAIN          18..269
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT   DOMAIN          270..326
FT                   /note="Laminin EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          327..396
FT                   /note="Laminin EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          397..453
FT                   /note="Laminin EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          454..502
FT                   /note="Laminin EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          503..512
FT                   /note="Laminin EGF-like 5; first part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          516..708
FT                   /note="Laminin IV type A 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT   DOMAIN          709..741
FT                   /note="Laminin EGF-like 5; second part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          742..790
FT                   /note="Laminin EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          791..848
FT                   /note="Laminin EGF-like 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          849..901
FT                   /note="Laminin EGF-like 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          902..950
FT                   /note="Laminin EGF-like 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          951..997
FT                   /note="Laminin EGF-like 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          998..1043
FT                   /note="Laminin EGF-like 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1044..1089
FT                   /note="Laminin EGF-like 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1090..1149
FT                   /note="Laminin EGF-like 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1150..1159
FT                   /note="Laminin EGF-like 14; first part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1170..1361
FT                   /note="Laminin IV type A 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT   DOMAIN          1362..1402
FT                   /note="Laminin EGF-like 14; second part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1403..1451
FT                   /note="Laminin EGF-like 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1452..1508
FT                   /note="Laminin EGF-like 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1509..1555
FT                   /note="Laminin EGF-like 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          2117..2297
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          2305..2481
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          2486..2673
FT                   /note="Laminin G-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          2713..2885
FT                   /note="Laminin G-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          2890..3070
FT                   /note="Laminin G-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   REGION          1556..2116
FT                   /note="Domain II and I"
FT   COILED          1706..1783
FT                   /evidence="ECO:0000255"
FT   MOTIF           2534..2536
FT                   /note="Cell attachment site"
FT   CARBOHYD        665
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1579
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1689
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1717
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2047
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2243
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   DISULFID        270..279
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        272..290
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        292..301
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        304..324
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        327..336
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        329..361
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        364..373
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        376..394
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        397..409
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        399..427
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        429..438
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        441..451
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        454..467
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        456..471
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        473..482
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        485..500
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        742..751
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        744..757
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        760..769
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        772..788
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        791..806
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        793..816
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        819..828
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        831..846
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        849..863
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        851..870
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        873..882
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        885..899
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        902..914
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        904..921
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        923..932
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        935..948
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        951..963
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        953..969
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        971..980
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        983..995
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        998..1007
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1000..1014
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1016..1025
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1028..1041
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1044..1056
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1046..1063
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1065..1074
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1077..1087
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1090..1102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1092..1118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1120..1129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1132..1147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1403..1412
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1405..1419
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1422..1431
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1434..1449
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1452..1466
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1454..1476
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1479..1488
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1491..1506
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1509..1521
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1511..1528
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1530..1539
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1542..1553
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1556
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        1560
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        2271..2297
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DISULFID        2457..2481
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DISULFID        2646..2673
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DISULFID        2860..2885
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DISULFID        3039..3070
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   VARIANT         349
FT                   /note="L -> S (in dbSNP:rs9950267)"
FT                   /id="VAR_056132"
FT   VARIANT         559
FT                   /note="V -> I (in dbSNP:rs16951079)"
FT                   /id="VAR_056133"
FT   VARIANT         674
FT                   /note="N -> T (in dbSNP:rs566655)"
FT                   /evidence="ECO:0000269|PubMed:1714537,
FT                   ECO:0000269|PubMed:2049067"
FT                   /id="VAR_060785"
FT   VARIANT         1340
FT                   /note="M -> V (in dbSNP:rs662471)"
FT                   /evidence="ECO:0000269|PubMed:1714537"
FT                   /id="VAR_060786"
FT   VARIANT         1577
FT                   /note="S -> A (in dbSNP:rs12961939)"
FT                   /id="VAR_056134"
FT   VARIANT         1591
FT                   /note="L -> V (in dbSNP:rs596315)"
FT                   /id="VAR_056135"
FT   VARIANT         1632
FT                   /note="K -> E (in dbSNP:rs11872364)"
FT                   /id="VAR_056136"
FT   VARIANT         1682
FT                   /note="D -> V (in dbSNP:rs16950981)"
FT                   /id="VAR_056137"
FT   VARIANT         1876
FT                   /note="A -> T (in dbSNP:rs11664063)"
FT                   /evidence="ECO:0000269|PubMed:1714537,
FT                   ECO:0000269|PubMed:2049067"
FT                   /id="VAR_060787"
FT   VARIANT         2002
FT                   /note="K -> E (in dbSNP:rs607230)"
FT                   /evidence="ECO:0000269|PubMed:1714537,
FT                   ECO:0000269|PubMed:2049067"
FT                   /id="VAR_060788"
FT   VARIANT         2076
FT                   /note="I -> T (in dbSNP:rs671871)"
FT                   /id="VAR_056138"
FT   VARIANT         2511
FT                   /note="L -> M (in dbSNP:rs60009920)"
FT                   /id="VAR_061347"
FT   VARIANT         2611
FT                   /note="T -> A (in dbSNP:rs543355)"
FT                   /id="VAR_056139"
FT   CONFLICT        228..229
FT                   /note="LQ -> FE (in Ref. 3; CAA41418)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        252..254
FT                   /note="IVT -> MLP (in Ref. 3; CAA41418)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        419
FT                   /note="H -> E (in Ref. 3; CAA41418)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        519
FT                   /note="V -> L (in Ref. 3; CAA41418)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1023
FT                   /note="V -> G (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1075
FT                   /note="D -> V (in Ref. 3; CAA41418)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1513
FT                   /note="P -> R (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1659
FT                   /note="I -> V (in Ref. 1; no nucleotide entry and 3;
FT                   CAA41418)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2079..2080
FT                   /note="NL -> KV (in Ref. 3; CAA41418)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2692
FT                   /note="P -> R (in Ref. 1; no nucleotide entry and 4; no
FT                   nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2746
FT                   /note="F -> L (in Ref. 4; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2962
FT                   /note="A -> P (in Ref. 1; no nucleotide entry and 4; no
FT                   nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3054
FT                   /note="F -> L (in Ref. 4; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3075 AA;  337084 MW;  941167F8FE534745 CRC64;
     MRGGVLLVLL LCVAAQCRQR GLFPAILNLA SNAHISTNAT CGEKGPEMFC KLVEHVPGRP
     VRNPQCRICD GNSANPRERH PISHAIDGTN NWWQSPSIQN GREYHWVTIT LDLRQVFQVA
     YVIIKAANAP RPGNWILERS LDGTTFSPWQ YYAVSDSECL SRYNITPRRG PPTYRADDEV
     ICTSYYSRLV PLEHGEIHTS LINGRPSADD LSPKLLEFTS ARYIRLRLQR IRTLNADLMT
     LSHREPKELD PIVTRRYYYS IKDISVGGMC ICYGHASSCP WDETTKKLQC QCEHNTCGES
     CNRCCPGYHQ QPWRPGTVSS GNTCEACNCH NKAKDCYYDE SVAKQKKSLN TAGQFRGGGV
     CINCLQNTMG INCETCIDGY YRPHKVSPYE DEPCRPCNCD PVGSLSSVCI KDDLHSDLHN
     GKQPGQCPCK EGYTGEKCDR CQLGYKDYPT CVSCGCNPVG SASDEPCTGP CVCKENVEGK
     ACDRCKPGFY NLKEKNPRGC SECFCFGVSD VCSSLSWPVG QVNSMSGWLV TDLISPRKIP
     SQQDALGGRH QVSINNTAVM QRLAPKYYWA APEAYLGNKL TAFGGFLKYT VSYDIPVETV
     DSNLMSHADV IIKGNGLTLS TQAEGLSLQP YEEYLNVVRL VPENFQDFHS KRQIDRDQLM
     TVLANVTHLL IRANYNSAKM ALYRLESVSL DIASSNAIDL VVAADVEHCE CPQGYTGTSC
     ESCLSGYYRV DGILFGGICQ PCECHGHAAE CNVHGVCIAC AHNTTGVHCE QCLPGFYGEP
     SRGTPGDCQP CACPLTIASN NFSPTCHLND GDEVVCDWCA PGYSGAWCER CADGYYGNPT
     VPGESCVPCD CSGNVDPSEA GHCDSVTGEC LKCLGNTDGA HCERCADGFY GDAVTAKNCR
     ACECHVKGSH SAVCHLETGL CDCKPNVTGQ QCDQCLHGYY GLDSGHGCRP CNCSVAGSVS
     DGCTDEGQCH CVPGVAGKRC DRCAHGFYAY QDGSCTPCDC PHTQNTCDPE TGECVCPPHT
     QGVKCEECED GHWGYDAEVG CQACNCSLVG STHHRCDVVT GHCQCKSKFG GRACDQCSLG
     YRDFPDCVPC DCDLRGTSGD ACNLEQGLCG CVEETGACPC KENVFGPQCN ECREGTFALR
     ADNPLGCSPC FCSGLSHLCS ELEDYVRTPV TLGSDQPLLR VVSQSNLRGT TEGVYYQAPD
     FLLDAATVRQ HIRAEPFYWR LPQQFQGDQL MAYGGKLKYS VAFYSLDGVG TSNFEPQVLI
     KGGRIRKQVI YMDAPAPENG VRQEQEVAMR ENFWKYFNSV SEKPVTREDF MSVLSDIEYI
     LIKASYGQGL QQSRISDISM EVGRKAEKLH PEEEVASLLE NCVCPPGTVG FSCQDCAPGY
     HRGKLPAGSD RGPRPLVAPC VPCSCNNHSD TCDPNTGKCL NCGDNTAGDH CDVCTSGYYG
     KVTGSASDCA LCACPHSPPA SFSPTCVLEG DHDFRCDACL LGYEGKHCER CSSSYYGNPQ
     TPGGSCQKCD CNPHGSVHGD CDRTSGQCVC RLGASGLRCD ECEPRHILME TDCVSCDDEC
     VGVLLNDLDE IGDAVLSLNL TGIIPVPYGI LSNLENTTKY LQESLLKENM QKDLGKIKLE
     GVAEETDNLQ KKLTRMLAST QKVNRATERI FKESQDLAIA IERLQMSITE IMEKTTLNQT
     LDEDFLLPNS TLQNMQQNGT SLLEIMQIRD FTQLHQNATL ELKAAEDLLS QIQENYQKPL
     EELEVLKEAA SHVLSKHNNE LKAAEALVRE AEAKMQESNH LLLMVNANLR EFSDKKLHVQ
     EEQNLTSELI VQGRGLIDAA AAQTDAVQDA LEHLEDHQDK LLLWSAKIRH HIDDLVMHMS
     QRNAVDLVYR AEDHAAEFQR LADVLYSGLE NIRNVSLNAT SAAYVHYNIQ SLIEESEELA
     RDAHRTVTET SLLSESLVSN GKAAVQRSSR FLKEGNNLSR KLPGIALELS ELRNKTNRFQ
     ENAVEITRQT NESLLILRAI PKGIRDKGAK TKELATSASQ SAVSTLRDVA GLSQELLNTS
     ASLSRVNTTL RETHQLLQDS TMATLLAGRK VKDVEIQANL LFDRLKPLKM LEENLSRNLS
     EIKLLISQAR KQAASIKVAV SADRDCIRAY QPQISSTNYN TLTLNVKTQE PDNLLFYLGS
     STASDFLAVE MRRGRVAFLW DLGSGSTRLE FPDFPIDDNR WHSIHVARFG NIGSLSVKEM
     SSNQKSPTKT SKSPGTANVL DVNNSTLMFV GGLGGQIKKS PAVKVTHFKG CLGEAFLNGK
     SIGLWNYIER EGKCRGCFGS SQNEDPSFHF DGSGYSVVEK SLPATVTQII MLFNTFSPNG
     LLLYLGSYGT KDFLSIELFR GRVKVMTDLG SGPITLLTDR RYNNGTWYKI AFQRNRKQGV
     LAVIDAYNTS NKETKQGETP GASSDLNRLD KDPIYVGGLP RSRVVRRGVT TKSFVGCIKN
     LEISRSTFDL LRNSYGVRKG CLLEPIRSVS FLKGGYIELP PKSLSPESEW LVTFATTNSS
     GIILAALGGD VEKRGDREEA HVPFFSVMLI GGNIEVHVNP GDGTGLRKAL LHAPTGTCSD
     GQAHSISLVR NRRIITVQLD ENNPVEMKLG TLVESRTINV SNLYVGGIPE GEGTSLLTMR
     RSFHGCIKNL IFNLELLDFN SAVGHEQVDL DTCWLSERPK LAPDAEDSKL LPEPRAFPEQ
     CVVDAALEYV PGAHQFGLTQ NSHFILPFNQ SAVRKKLSVE LSIRTFASSG LIYYMAHQNQ
     ADYAVLQLHG GRLHFMFDLG KGRTKVSHPA LLSDGKWHTV KTDYVKRKGF ITVDGRESPM
     VTVVGDGTML DVEGLFYLGG LPSQYQARKI GNITHSIPAC IGDVTVNSKQ LDKDSPVSAF
     TVNRCYAVAQ EGTYFDGSGY AALVKEGYKV QSDVNITLEF RTSSQNGVLL GISTAKVDAI
     GLELVDGKVL FHVNNGAGRI TAAYEPKTAT VLCDGKWHTL QANKSKHRIT LIVDGNAVGA
     ESPHTQSTSV DTNNPIYVGG YPAGVKQKCL RSQTSFRGCL RKLALIKSPQ VQSFDFSRAF
     ELHGVFLHSC PGTES
//