LAMA3_MOUSE
ID LAMA3_MOUSE Reviewed; 3330 AA.
AC Q61789; E9PUR4; O08751; Q61788; Q61966; Q9JHQ7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 4.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Laminin subunit alpha-3;
DE AltName: Full=Epiligrin subunit alpha;
DE AltName: Full=Kalinin subunit alpha;
DE AltName: Full=Laminin-5 subunit alpha;
DE AltName: Full=Laminin-6 subunit alpha;
DE AltName: Full=Laminin-7 subunit alpha;
DE AltName: Full=Nicein subunit alpha;
DE Flags: Precursor;
GN Name=Lama3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 765-3330 (ISOFORM B).
RC STRAIN=BALB/cJ; TISSUE=Lung;
RX PubMed=7665604; DOI=10.1074/jbc.270.37.21820;
RA Galliano M.-F., Aberdam D., Aguzzi A., Ortonne J.-P., Meneguzzi G.;
RT "Cloning and complete primary structure of the mouse laminin alpha 3 chain.
RT Distinct expression pattern of the laminin alpha 3A and alpha 3B chain
RT isoforms.";
RL J. Biol. Chem. 270:21820-21826(1995).
RN [2]
RP SEQUENCE REVISION.
RA Aberdam D.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-58 (ISOFORM B), AND PROTEIN SEQUENCE OF
RP 32-38.
RX PubMed=11829758; DOI=10.1042/0264-6021:3620213;
RA Garbe J.H., Gohring W., Mann K., Timpl R., Sasaki T.;
RT "Complete sequence, recombinant analysis and binding to laminins and
RT sulphated ligands of the N-terminal domains of laminin alpha3B and alpha5
RT chains.";
RL Biochem. J. 362:213-221(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 50-776 (ISOFORM B).
RC STRAIN=ICR;
RX PubMed=9151674; DOI=10.1083/jcb.137.3.685;
RA Miner J.H., Patton B.L., Lentz S.I., Gilbert D.J., Snider W.D.,
RA Jenkins N.A., Copeland N.G., Sanes J.R.;
RT "The laminin alpha chains: expression, developmental transitions, and
RT chromosomal locations of alpha1-5, identification of heterotrimeric
RT laminins 8-11, and cloning of a novel alpha3 isoform.";
RL J. Cell Biol. 137:685-701(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1813-2531 (ISOFORM B).
RC TISSUE=Lung;
RX PubMed=8012114; DOI=10.1007/bf00360551;
RA Aberdam D., Galliano M.-F., Mattei M.-G., Pisani-Spadafora A.,
RA Ortonne J.-P., Meneguzzi G.;
RT "Assignment of mouse nicein genes to chromosomes 1 and 18.";
RL Mamm. Genome 5:229-233(1994).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- FUNCTION: Laminin-5 is thought to be involved in (1) cell adhesion via
CC integrin alpha-3/beta-1 in focal adhesion and integrin alpha-6/beta-4
CC in hemidesmosomes, (2) signal transduction via tyrosine phosphorylation
CC of pp125-FAK and p80, (3) differentiation of keratinocytes.
CC {ECO:0000250}.
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-3 is a
CC subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein),
CC laminin-6 (laminin-311 or K-laminin) and laminin-7 (laminin-321 or KS-
CC laminin).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Note=Major component.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=Q61789-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q61789-2; Sequence=VSP_003038, VSP_003039;
CC -!- TISSUE SPECIFICITY: Basal membrane of the upper alimentary tract and
CC urinary and nasal epithelia, salivary glands and teeth (both variants).
CC Isoform A is predominantly expressed in skin, hair follicles and
CC developing neurons of the trigeminal ganglion. Isoform B was found in
CC bronchi, alveoli, stomach, intestinal crypts, whisker pads, CNS,
CC telencephalic neuroectoderm, thalamus, Rathke pouch and periventricular
CC subependymal germinal layer.
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 IV and G are globular.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA58837.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X84013; CAA58836.1; -; mRNA.
DR EMBL; X84014; CAA58837.1; ALT_FRAME; mRNA.
DR EMBL; AC102131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC102248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC157909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ293592; CAB99254.2; -; mRNA.
DR EMBL; U88353; AAC53179.1; -; mRNA.
DR EMBL; L20478; AAA68091.1; -; mRNA.
DR CCDS; CCDS50222.1; -. [Q61789-1]
DR CCDS; CCDS84360.1; -. [Q61789-2]
DR RefSeq; NP_001334390.1; NM_001347461.1. [Q61789-2]
DR RefSeq; NP_034810.1; NM_010680.1. [Q61789-1]
DR SMR; Q61789; -.
DR BioGRID; 201098; 8.
DR ComplexPortal; CPX-3012; Laminin-332 complex variant A. [Q61789-2]
DR ComplexPortal; CPX-3013; Laminin-311 complex variant A. [Q61789-2]
DR ComplexPortal; CPX-3014; Laminin-321 complex. [Q61789-2]
DR ComplexPortal; CPX-3164; Laminin-332 complex variant B. [Q61789-1]
DR ComplexPortal; CPX-3167; Laminin-311 complex variant B. [Q61789-1]
DR IntAct; Q61789; 1.
DR MINT; Q61789; -.
DR STRING; 10090.ENSMUSP00000089703; -.
DR GlyGen; Q61789; 13 sites.
DR iPTMnet; Q61789; -.
DR PhosphoSitePlus; Q61789; -.
DR MaxQB; Q61789; -.
DR PaxDb; Q61789; -.
DR PeptideAtlas; Q61789; -.
DR PRIDE; Q61789; -.
DR ProteomicsDB; 264908; -. [Q61789-1]
DR ProteomicsDB; 264909; -. [Q61789-2]
DR Antibodypedia; 1948; 191 antibodies from 30 providers.
DR Ensembl; ENSMUST00000092070; ENSMUSP00000089703; ENSMUSG00000024421. [Q61789-1]
DR Ensembl; ENSMUST00000188815; ENSMUSP00000140104; ENSMUSG00000024421. [Q61789-2]
DR GeneID; 16774; -.
DR KEGG; mmu:16774; -.
DR UCSC; uc008ecf.2; mouse. [Q61789-1]
DR UCSC; uc008ech.1; mouse. [Q61789-2]
DR CTD; 3909; -.
DR MGI; MGI:99909; Lama3.
DR VEuPathDB; HostDB:ENSMUSG00000024421; -.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000155638; -.
DR HOGENOM; CLU_000301_1_0_1; -.
DR InParanoid; Q61789; -.
DR OMA; GECKCLT; -.
DR OrthoDB; 2342at2759; -.
DR PhylomeDB; Q61789; -.
DR TreeFam; TF335359; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-2214320; Anchoring fibril formation.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-446107; Type I hemidesmosome assembly.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR BioGRID-ORCS; 16774; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Lama3; mouse.
DR PRO; PR:Q61789; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q61789; protein.
DR Bgee; ENSMUSG00000024421; Expressed in molar tooth and 121 other tissues.
DR Genevisible; Q61789; MM.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0030056; C:hemidesmosome; IEA:Ensembl.
DR GO; GO:0005608; C:laminin-3 complex; IEA:Ensembl.
DR GO; GO:0005610; C:laminin-5 complex; IDA:MGI.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0031581; P:hemidesmosome assembly; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IBA:GO_Central.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
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:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 13.
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; 1.
DR Pfam; PF00053; Laminin_EGF; 12.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 14.
DR SMART; SM00281; LamB; 1.
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; 1.
DR PROSITE; PS01248; EGF_LAM_1; 12.
DR PROSITE; PS50027; EGF_LAM_2; 13.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Cell adhesion; Coiled coil;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Laminin EGF-like domain; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:11829758"
FT CHAIN 32..3330
FT /note="Laminin subunit alpha-3"
FT /id="PRO_0000017059"
FT DOMAIN 40..295
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 296..350
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 353..420
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 423..464
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 488..530
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 533..576
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 582..625
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 628..678
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 681..725
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1309..1352
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1353..1401
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1402..1452
FT /note="Laminin EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1453..1462
FT /note="Laminin EGF-like 12; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1466..1650
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 1651..1683
FT /note="Laminin EGF-like 12; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1684..1730
FT /note="Laminin EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1731..1783
FT /note="Laminin EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1784..1818
FT /note="Laminin EGF-like 15; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2386..2587
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2594..2756
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2763..2923
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2983..3147
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3154..3327
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 295..725
FT /note="Domain V"
FT REGION 793..1262
FT /note="Domain IV 1 (domain IV B)"
FT REGION 1263..1462
FT /note="Domain III B"
FT REGION 1651..1818
FT /note="Domain III A"
FT REGION 1819..2385
FT /note="Domain II and I"
FT COILED 1851..1980
FT /evidence="ECO:0000255"
FT COILED 2012..2057
FT /evidence="ECO:0000255"
FT COILED 2088..2165
FT /evidence="ECO:0000255"
FT COILED 2211..2238
FT /evidence="ECO:0000255"
FT COILED 2318..2383
FT /evidence="ECO:0000255"
FT MOTIF 2274..2276
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3094
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 296..305
FT /evidence="ECO:0000250"
FT DISULFID 298..316
FT /evidence="ECO:0000250"
FT DISULFID 318..327
FT /evidence="ECO:0000250"
FT DISULFID 330..350
FT /evidence="ECO:0000250"
FT DISULFID 353..362
FT /evidence="ECO:0000250"
FT DISULFID 355..387
FT /evidence="ECO:0000250"
FT DISULFID 390..399
FT /evidence="ECO:0000250"
FT DISULFID 402..420
FT /evidence="ECO:0000250"
FT DISULFID 423..433
FT /evidence="ECO:0000250"
FT DISULFID 425..440
FT /evidence="ECO:0000250"
FT DISULFID 442..451
FT /evidence="ECO:0000250"
FT DISULFID 454..464
FT /evidence="ECO:0000250"
FT DISULFID 488..500
FT /evidence="ECO:0000250"
FT DISULFID 490..506
FT /evidence="ECO:0000250"
FT DISULFID 508..517
FT /evidence="ECO:0000250"
FT DISULFID 520..530
FT /evidence="ECO:0000250"
FT DISULFID 533..545
FT /evidence="ECO:0000250"
FT DISULFID 535..552
FT /evidence="ECO:0000250"
FT DISULFID 554..563
FT /evidence="ECO:0000250"
FT DISULFID 566..583
FT /evidence="ECO:0000250"
FT DISULFID 628..642
FT /evidence="ECO:0000250"
FT DISULFID 630..649
FT /evidence="ECO:0000250"
FT DISULFID 651..660
FT /evidence="ECO:0000250"
FT DISULFID 663..678
FT /evidence="ECO:0000250"
FT DISULFID 681..693
FT /evidence="ECO:0000250"
FT DISULFID 683..700
FT /evidence="ECO:0000250"
FT DISULFID 702..711
FT /evidence="ECO:0000250"
FT DISULFID 1309..1316
FT /evidence="ECO:0000250"
FT DISULFID 1311..1323
FT /evidence="ECO:0000250"
FT DISULFID 1325..1334
FT /evidence="ECO:0000250"
FT DISULFID 1337..1350
FT /evidence="ECO:0000250"
FT DISULFID 1353..1368
FT /evidence="ECO:0000250"
FT DISULFID 1355..1375
FT /evidence="ECO:0000250"
FT DISULFID 1377..1386
FT /evidence="ECO:0000250"
FT DISULFID 1389..1399
FT /evidence="ECO:0000250"
FT DISULFID 1402..1414
FT /evidence="ECO:0000250"
FT DISULFID 1404..1421
FT /evidence="ECO:0000250"
FT DISULFID 1423..1432
FT /evidence="ECO:0000250"
FT DISULFID 1435..1450
FT /evidence="ECO:0000250"
FT DISULFID 1684..1693
FT /evidence="ECO:0000250"
FT DISULFID 1686..1700
FT /evidence="ECO:0000250"
FT DISULFID 1703..1712
FT /evidence="ECO:0000250"
FT DISULFID 1715..1728
FT /evidence="ECO:0000250"
FT DISULFID 1731..1743
FT /evidence="ECO:0000250"
FT DISULFID 1733..1752
FT /evidence="ECO:0000250"
FT DISULFID 1754..1763
FT /evidence="ECO:0000250"
FT DISULFID 1766..1781
FT /evidence="ECO:0000250"
FT DISULFID 1819
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1822
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 2557..2587
FT /evidence="ECO:0000250"
FT DISULFID 2733..2756
FT /evidence="ECO:0000250"
FT DISULFID 2891..2923
FT /evidence="ECO:0000250"
FT DISULFID 3124..3147
FT /evidence="ECO:0000250"
FT DISULFID 3299..3327
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1619
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:7665604"
FT /id="VSP_003038"
FT VAR_SEQ 1620..1662
FT /note="FTETQRLTLGEVGLEEASDTGSGPRAHLVEMCACPPDYTGDSC -> MLPAV
FT RWSAWSTGWLWIFGAALGQCLGYGSEQQRVAFLQRPSQNHLQASYMELRPS (in
FT isoform A)"
FT /evidence="ECO:0000303|PubMed:7665604"
FT /id="VSP_003039"
FT CONFLICT 982
FT /note="A -> R (in Ref. 1; CAA58837)"
FT /evidence="ECO:0000305"
FT CONFLICT 1150
FT /note="W -> R (in Ref. 1; CAA58837)"
FT /evidence="ECO:0000305"
FT CONFLICT 1224
FT /note="E -> K (in Ref. 1; CAA58837)"
FT /evidence="ECO:0000305"
FT CONFLICT 1272
FT /note="G -> GH (in Ref. 1; CAA58837)"
FT /evidence="ECO:0000305"
FT CONFLICT 1291
FT /note="R -> S (in Ref. 1; CAA58837)"
FT /evidence="ECO:0000305"
FT CONFLICT 1398
FT /note="E -> K (in Ref. 1; CAA58837)"
FT /evidence="ECO:0000305"
FT CONFLICT 1466
FT /note="H -> R (in Ref. 1; CAA58837)"
FT /evidence="ECO:0000305"
FT CONFLICT 1479
FT /note="R -> V (in Ref. 1; CAA58837)"
FT /evidence="ECO:0000305"
FT CONFLICT 1488
FT /note="V -> F (in Ref. 1; CAA58837)"
FT /evidence="ECO:0000305"
FT CONFLICT 1527..1528
FT /note="SS -> II (in Ref. 1; CAA58837)"
FT /evidence="ECO:0000305"
FT CONFLICT 1608
FT /note="S -> P (in Ref. 1; CAA58837)"
FT /evidence="ECO:0000305"
FT CONFLICT 1983..1984
FT /note="KK -> QN (in Ref. 1; CAA58836/CAA58837 and 6;
FT AAA68091)"
FT /evidence="ECO:0000305"
FT CONFLICT 1987
FT /note="Q -> G (in Ref. 1; CAA58836/CAA58837 and 6;
FT AAA68091)"
FT /evidence="ECO:0000305"
FT CONFLICT 2463
FT /note="R -> G (in Ref. 1; CAA58836/CAA58837 and 6;
FT AAA68091)"
FT /evidence="ECO:0000305"
FT CONFLICT 2488
FT /note="F -> S (in Ref. 1; CAA58836/CAA58837 and 6;
FT AAA68091)"
FT /evidence="ECO:0000305"
FT CONFLICT 2617..2620
FT /note="NFMQ -> KLSW (in Ref. 1; CAA58836/CAA58837)"
FT /evidence="ECO:0000305"
FT CONFLICT 2724..2725
FT /note="NI -> PL (in Ref. 1; CAA58836/CAA58837)"
FT /evidence="ECO:0000305"
FT CONFLICT 3257
FT /note="D -> Y (in Ref. 1; CAA58836/CAA58837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3330 AA; 366227 MW; 993EB20BACDD6C59 CRC64;
MAVALGRAPR SLPLLLTLLL LLLLRMSPSW SVVGQDHPMS SRSLHPPYFN LAQAARIWAT
ATCGERDPEV SRPRPELFCK LVGGPAAQGS GHTIQGQFCD YCNSEDSRKA HPASHAIDGS
ERWWQSPPLS SGTQYNQVNL TLDLGQLFHV AYILIKFANS PRPDLWILER SVDFGSTYSP
WQYFAHSRRD CVEQFGQEAN MAITQDDQML CVTEYSRIVP LENGEIVVSL INGRPGAKKF
AFSDTLREFT KATNIRLRFL RTNTLLGHLI SKAERDPTVT RRYYYSIKDI SVGGRCVCNG
HAEACSADNP EKQFRCECQH HTCGDTCNRC CAGYNQRRWQ PAGQEQHNEC EACNCHGHAV
DCYYDPDVEH QQASLNSKGV YAGGGVCINC QHNTAGVNCE KCAKGYFRPH GVPVDALHGC
IPCSCDPERA DDCDQGSGHC HCKPNFSGDY CETCADGYYN FPFCLRIPVF PNYTPSPEDP
VAGNIKGCDC NLEGVLPEIC DDRGRCLCRP GVEGPQCDSC RSGSYSFPIC QACQCSTIGS
YPVPCDPGNG QCDCLPGITG RQCDRCLSGA YDFPYCQGSG SVCHPAGTLD SSLGYCQCKQ
HVASPTCSVC KPLYWNLAKE NPRGCSECQC HEAGTLSGIG ECGQEDGDCS CKAHVTGDAC
DTCEDGFFSL EKSNYFGCQG CQCDIGGALT TMCSGPSGVC QCREHVEGKQ CQRPENNYYF
PDLHHMKYEV EDGTGPNGRN LRFGFDPLVF PEFSWRGYAP MTSVQNEVRV RLSVRQSSLS
LFRIVLRYIS PGTEAISGRI TLYSSQGDSD ALQSRKITFP PSKEPAFVTV PGNGFAGPFS
ITPGTWIACI QVEGVLLDYL VLLPRDYYEA FTLQVPVTEP CAHTGSPQDN CLLYQHLPLT
AFSCTLACEA RHFLLDGELR PLAMRQPTPT HPAMVDLSGR EVELQLRLRV PQVGHYVVLL
EYATEVEQLF VVDVNLKSSG SALAGQVNIY SCKYSIPCRS VVIDSLSRTA VHELLADADI
QLKAHMAHFL LYHICIIPAE EFSTEYLRPQ VHCIASYRQH ANPSASCVSL AHETPPTASI
LDATSRGLFS ALPHEPSSPA DGVTLKAPQS QVTLKGLIPH LGRHVFVIHF YQAEHPGFPT
EVIVNGGRQW SGSFLASFCP HLLGCRDQVI SDGQVEFDIS EAEVAVTVKI PDGKSLTLVR
VLVVPAENYD YQILHKTTVD KSSEFISSCG GDSFYIDPQA ASGFCKNSAR SLVAFYHNGA
IPCECDPAGT AGHHCSPEGG QCPCRPNVIG RQCSRCATGY YGFPYCKPCN CGRRLCEEVT
GKCLCPPHTV RPQCEVCEMN SFNFHPVAGC DVCNCSRKGT IEAAVSECDR DSGQCRCKPR
VTGQQCDKCA PGFYQFPECV PCSCNRDGTE PSVCDPETGA CMCKENVEGP QCQLCREGSF
YLDPTNPKGC TKCFCFGVNT DCQSSHKQRA KFVDMMGWRL ETADGVDVPV SFNPGSNSMV
ADLQELPPSV HSASWVAPPS YLGDKVSSYG GYLTYHAKSF GLPGDMVLLG KQPDVQLTGQ
HMSLIHKEPS DPRPDRLHHG RVQVIEGNFR HEGSSAPVSR EELMTVLSRL ERLHIRGLHF
TETQRLTLGE VGLEEASDTG SGPRAHLVEM CACPPDYTGD SCQGCRPGYY WDNKSLPVGR
CVPCNCNGHS NRCQDGSGIC INCQHNTAGE HCERCQAGHY GNAIHGSCRV CPCPHTNSFA
TGCAVDGGAV RCACKPGYTG TQCERCAPGY FGNPQKFGGS CQPCNCNSNG QLGPCDPLTG
DCVNQEPKDG SPAEECDDCD SCVMTLLNDL ASMGEELRLV KSKLQGLSVS TGALEQIRHM
ETQAKDLRNQ LLGFRSATSS HGSKMDDLEK ELSHLNREFE TLQEKAQVNS RKAQTLYNNI
DQTIQSAKEL DMKIKNIVQN VHILLKQMAR PGGEGTDLPV GDWSRELAEA QRMMRDLRSR
DFKKHLQEAE AEKMEAQLLL HRIRTWLESH QVENNGLLKN IRDSLNDYED KLQDLRSILQ
EAAAQAKQAT GINHENEGVL GAIQRQMKEM DSLKNDFTKY LATADSSLLQ TNNLLQQMDK
SQKEYESLAA ALNGARQELS DRVRELSRSG GKAPLVVEAE KHAQSLQELA KQLEEIKRNT
SGDELVRCAV DAATAYENIL NAIRAAEDAA SKATSASKSA FQTVIKEDLP KRAKTLSSDS
EELLNEAKMT QKRLQQVSPA LNSLQQTLKT VSVQKDLLDA NLTVARDDLH GIQRGDIDSV
VIGAKSMVRE ANGITSEVLD GLNPIQTDLG RIKDSYESAR REDFSKALVD ANNSVKKLTR
KLPDLFIKIE SINQQLLPLG NISDNVDRIR ELIQQARDAA NKVAIPMRFN GKSGVEVRLP
NDLEDLKGYT SLSLFLQRPD LRENGGTEDM FVMYLGNKDA SKDYIGMAVV DGQLTCVYNL
GDREAEVQID QVLTESESQE AVMDRVKFQR IYQFAKLNYT KEATSTKPKA PGVYDMESAS
SNTLLNLDPE NAVFYVGGYP PGFELPRRLR FPPYKGCIEL DDLNENVLSL YNFKTTFNLN
TTEVEPCRRR KEESDKNYFE GTGYARIPTQ PNAPFPNFMQ TIQTTVDRGL LFFAENQDNF
ISLNIEDGNL MVKYKLNSEP PKEKGIRDTI NNGRDHMILI SIGKSQKRML INMNKHSIII
EGEIFDFSTY YLGGIPIAIR ERFNISTPAF QGCMKNLKKT SGVVRLNDTV GVTKKCSEDW
KLVRTASFSR GGQMSFTNLD VPSLDRFQLS FGFQTFQPSG TLLNHQTRTS SLLVTLEDGH
IALSTRDSSS PIFKSPGTYM DGLLHHVSVI SDTSGLRLLI DDQVLRRNQR LASFSNAQQS
LSMGGGYFEG CISNVFVQRM SQSPEVLDMA SKSTKRDAFL GGCSLNKPPF LMLFKSPKGF
NKARSFNVNQ LLQDAPQAAR SIEAWQDGKS CLPPLNTKAT HRALQFGDSP TSHLLFKLPQ
ELLKPRLQFS LDIQTTSSRG LVFHTGTRDS FVALYLSEGH VIFALGAGGK KLRLRSKERY
HDGKWHSVVF GLSGRKVHLV VDGLRAQEGS LPGNSTISPR EQVYLGLSPS RKSKSLPQHS
FVGCLRNFQL DSKPLDSPSA RSGVSPCLGG SLEKGIYFSQ GGGHVVLANS VSLEPALTLT
LSIRPRSLTG VLIHIASQSG EHLSVYMEAG KVTTSMNSEA GGTVTSITPK RSLCDGQWHS
VTVSIKQHTL HLELDTDNSY TAGQLSFPPN STRGSLHIGG VPDKLKMLTL PVWNSFFGCL
KNIQVNHIPV PITEATDVQG SVSLNGCPDH
