LAMA1_HUMAN
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 03-AUG-2022, entry version 216.
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; 58.
DR ComplexPortal; CPX-1770; Laminin-111 complex.
DR ComplexPortal; CPX-1772; Laminin-121 complex.
DR DIP; DIP-29324N; -.
DR IntAct; P25391; 35.
DR MINT; P25391; -.
DR STRING; 9606.ENSP00000374309; -.
DR ChEMBL; CHEMBL4523594; -.
DR DrugBank; DB06245; Lanoteplase.
DR GlyConnect; 1438; 11 N-Linked glycans (1 site).
DR GlyGen; P25391; 11 sites, 11 N-linked glycans (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; P25391; -.
DR PeptideAtlas; P25391; -.
DR PRIDE; P25391; -.
DR ProteomicsDB; 54269; -.
DR Antibodypedia; 4123; 339 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 CTD; 284217; -.
DR DisGeNET; 284217; -.
DR GeneCards; LAMA1; -.
DR HGNC; HGNC:6481; LAMA1.
DR HPA; ENSG00000101680; Tissue enhanced (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; WVAARCQ; -.
DR OrthoDB; 128982at2759; -.
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 1068 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 104 other tissues.
DR ExpressionAtlas; P25391; baseline and differential.
DR Genevisible; P25391; HS.
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; IC:ComplexPortal.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:UniProtKB.
DR GO; GO:0043208; F:glycosphingolipid binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:CAFA.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0048514; P:blood vessel morphogenesis; IBA:GO_Central.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
DR GO; GO:0043010; P:camera-type eye development; IBA:GO_Central.
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:0045785; P:positive regulation of cell adhesion; IC:ComplexPortal.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IC:ComplexPortal.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IC:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0110011; P:regulation of basement membrane organization; IC: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 GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 15.
DR CDD; cd00110; LamG; 5.
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 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 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; SSF49899; 5.
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.
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
