LAMA4_HUMAN
ID LAMA4_HUMAN Reviewed; 1823 AA.
AC Q16363; Q14731; Q14735; Q15335; Q4LE44; Q5SZG8; Q9BTB8; Q9UE18; Q9UJN9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 4.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Laminin subunit alpha-4;
DE AltName: Full=Laminin-14 subunit alpha;
DE AltName: Full=Laminin-8 subunit alpha;
DE AltName: Full=Laminin-9 subunit alpha;
DE Flags: Precursor;
GN Name=LAMA4;
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] (ISOFORM 2), AND VARIANTS SER-1117 AND ARG-1119.
RC TISSUE=Fetal lung;
RX PubMed=7781776; DOI=10.1016/0014-5793(95)00462-i;
RA Iivanainen A., Sainio K., Sariola H., Tryggvason K.;
RT "Primary structure and expression of a novel human laminin alpha 4 chain.";
RL FEBS Lett. 365:183-188(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS HIS-498; SER-1117;
RP ARG-1119 AND SER-1549.
RX PubMed=8706685; DOI=10.1111/j.1432-1033.1996.0813w.x;
RA Richards A.J., Al-Imara L., Pope F.M.;
RT "The complete cDNA sequence of laminin alpha 4 and its relationship to the
RT other human laminin alpha chains.";
RL Eur. J. Biochem. 238:813-821(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Pancreas;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
RC TISSUE=Heart;
RX PubMed=9310354; DOI=10.1111/j.1432-1033.1997.t01-1-00015.x;
RA Richards A.J., Luccarini C., Pope F.M.;
RT "The structural organisation of LAMA4, the gene encoding laminin alpha4.";
RL Eur. J. Biochem. 248:15-23(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 236-1823 (ISOFORM 2), AND VARIANTS HIS-498;
RP SER-1117 AND ARG-1119.
RC TISSUE=Heart;
RX PubMed=7959779; DOI=10.1006/geno.1994.1372;
RA Richards A.J., Al-Imara L., Carter N.P., Lloyd J.C., Leversha M.A.,
RA Pope F.M.;
RT "Localization of the gene (LAMA4) to chromosome 6q21 and isolation of a
RT partial cDNA encoding a variant laminin A chain.";
RL Genomics 22:237-239(1994).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-557; ASN-578; ASN-581; ASN-742;
RP ASN-787 AND ASN-810.
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 [10]
RP VARIANT CMD1JJ LEU-950, AND CHARACTERIZATION OF VARIANT CMD1JJ LEU-950.
RX PubMed=17646580; DOI=10.1161/circulationaha.107.689984;
RA Knoell R., Postel R., Wang J., Kraetzner R., Hennecke G., Vacaru A.M.,
RA Vakeel P., Schubert C., Murthy K., Rana B.K., Kube D., Knoell G.,
RA Schaefer K., Hayashi T., Holm T., Kimura A., Schork N., Toliat M.R.,
RA Nuernberg P., Schultheiss H.P., Schaper W., Schaper J., Bos E.,
RA Den Hertog J., van Eeden F.J., Peters P.J., Hasenfuss G., Chien K.R.,
RA Bakkers J.;
RT "Laminin-alpha4 and integrin-linked kinase mutations cause human
RT cardiomyopathy via simultaneous defects in cardiomyocytes and endothelial
RT cells.";
RL Circulation 116:515-525(2007).
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-4 is a
CC subunit of laminin-8 (laminin-411), laminin-9 (laminin-421) and
CC laminin-14 (laminin-423).
CC -!- INTERACTION:
CC Q16363-3; P05067: APP; NbExp=3; IntAct=EBI-17719490, EBI-77613;
CC Q16363-3; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-17719490, EBI-10244780;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Note=Major component.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q16363-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16363-2; Sequence=VSP_017542;
CC Name=3;
CC IsoId=Q16363-3; Sequence=VSP_038853, VSP_038854;
CC -!- TISSUE SPECIFICITY: In adult, strong expression in heart, lung, ovary
CC small and large intestines, placenta, liver; weak or no expression in
CC skeletal muscle, kidney, pancreas, testis, prostate, brain. High
CC expression in fetal lung and kidney. Expression in fetal and newborn
CC tissues is observed in certain mesenchymal cells in tissues such as
CC smooth muscle and dermis.
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: Domain G is globular.
CC -!- DISEASE: Cardiomyopathy, dilated 1JJ (CMD1JJ) [MIM:615235]: A disorder
CC characterized by ventricular dilation and impaired systolic function,
CC resulting in congestive heart failure and arrhythmia. Patients are at
CC risk of premature death. {ECO:0000269|PubMed:17646580}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- CAUTION: Gene LAMA4 was formerly called LAMA3. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE06109.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S78569; AAB34635.1; -; mRNA.
DR EMBL; X91171; CAA62596.1; -; mRNA.
DR EMBL; X70904; CAA50261.1; -; mRNA.
DR EMBL; AB210027; BAE06109.1; ALT_INIT; mRNA.
DR EMBL; BT006690; AAP35336.1; -; mRNA.
DR EMBL; AL590106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z99289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004241; AAH04241.1; -; mRNA.
DR EMBL; Y14240; CAA74636.1; -; Genomic_DNA.
DR EMBL; X76939; CAA54258.1; -; mRNA.
DR CCDS; CCDS34514.1; -. [Q16363-2]
DR CCDS; CCDS43491.1; -. [Q16363-1]
DR CCDS; CCDS43492.1; -. [Q16363-3]
DR PIR; S68960; S68960.
DR RefSeq; NP_001098676.2; NM_001105206.2.
DR RefSeq; NP_001098677.2; NM_001105207.2.
DR RefSeq; NP_001098678.1; NM_001105208.2. [Q16363-3]
DR RefSeq; NP_001098679.1; NM_001105209.2. [Q16363-3]
DR RefSeq; NP_002281.3; NM_002290.4.
DR RefSeq; XP_005267040.2; XM_005266983.3.
DR RefSeq; XP_005267041.2; XM_005266984.3.
DR AlphaFoldDB; Q16363; -.
DR SMR; Q16363; -.
DR BioGRID; 110104; 35.
DR ComplexPortal; CPX-1777; Laminin-411 complex.
DR ComplexPortal; CPX-1778; Laminin-421 complex.
DR ComplexPortal; CPX-1782; Laminin-423 complex.
DR CORUM; Q16363; -.
DR IntAct; Q16363; 28.
DR MINT; Q16363; -.
DR STRING; 9606.ENSP00000230538; -.
DR ChEMBL; CHEMBL2364187; -.
DR GlyConnect; 1440; 42 N-Linked glycans (10 sites).
DR GlyGen; Q16363; 20 sites, 42 N-linked glycans (10 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q16363; -.
DR PhosphoSitePlus; Q16363; -.
DR SwissPalm; Q16363; -.
DR BioMuta; LAMA4; -.
DR DMDM; 292495093; -.
DR EPD; Q16363; -.
DR jPOST; Q16363; -.
DR MassIVE; Q16363; -.
DR MaxQB; Q16363; -.
DR PaxDb; Q16363; -.
DR PeptideAtlas; Q16363; -.
DR PRIDE; Q16363; -.
DR ProteomicsDB; 60862; -. [Q16363-1]
DR ProteomicsDB; 60863; -. [Q16363-2]
DR ProteomicsDB; 60864; -. [Q16363-3]
DR Antibodypedia; 2846; 350 antibodies from 29 providers.
DR DNASU; 3910; -.
DR Ensembl; ENST00000368638.5; ENSP00000357627.4; ENSG00000112769.20. [Q16363-3]
DR Ensembl; ENST00000453937.2; ENSP00000398226.2; ENSG00000112769.20. [Q16363-3]
DR Ensembl; ENST00000455073.1; ENSP00000408604.1; ENSG00000112769.20. [Q16363-3]
DR GeneID; 3910; -.
DR KEGG; hsa:3910; -.
DR UCSC; uc010kdz.3; human. [Q16363-1]
DR CTD; 3910; -.
DR DisGeNET; 3910; -.
DR GeneCards; LAMA4; -.
DR HGNC; HGNC:6484; LAMA4.
DR HPA; ENSG00000112769; Low tissue specificity.
DR MalaCards; LAMA4; -.
DR MIM; 600133; gene.
DR MIM; 615235; phenotype.
DR neXtProt; NX_Q16363; -.
DR OpenTargets; ENSG00000112769; -.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR PharmGKB; PA30273; -.
DR VEuPathDB; HostDB:ENSG00000112769; -.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000159970; -.
DR HOGENOM; CLU_2095989_0_0_1; -.
DR InParanoid; Q16363; -.
DR OrthoDB; 2342at2759; -.
DR PhylomeDB; Q16363; -.
DR TreeFam; TF335359; -.
DR PathwayCommons; Q16363; -.
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-8874081; MET activates PTK2 signaling.
DR SignaLink; Q16363; -.
DR SIGNOR; Q16363; -.
DR BioGRID-ORCS; 3910; 12 hits in 1075 CRISPR screens.
DR ChiTaRS; LAMA4; human.
DR GeneWiki; Laminin,_alpha_4; -.
DR GenomeRNAi; 3910; -.
DR Pharos; Q16363; Tbio.
DR PRO; PR:Q16363; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q16363; protein.
DR Bgee; ENSG00000112769; Expressed in lower esophagus muscularis layer and 181 other tissues.
DR ExpressionAtlas; Q16363; baseline and differential.
DR Genevisible; Q16363; HS.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
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 CDD; cd00055; EGF_Lam; 3.
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; IPR002049; LE_dom.
DR Pfam; PF00053; Laminin_EGF; 3.
DR Pfam; PF02210; Laminin_G_2; 5.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF06009; Laminin_II; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00180; EGF_Lam; 3.
DR SMART; SM00282; LamG; 5.
DR SUPFAM; SSF49899; SSF49899; 5.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Cardiomyopathy; Cell adhesion;
KW Coiled coil; Disease variant; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Laminin EGF-like domain; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1823
FT /note="Laminin subunit alpha-4"
FT /id="PRO_0000017060"
FT DOMAIN 82..131
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 132..186
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 187..240
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 241..255
FT /note="Laminin EGF-like 4; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 833..1035
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1047..1227
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1234..1402
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1469..1640
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1647..1820
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 256..832
FT /note="Domain II and I"
FT REGION 1419..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 320..403
FT /evidence="ECO:0000255"
FT COILED 473..528
FT /evidence="ECO:0000255"
FT COILED 581..614
FT /evidence="ECO:0000255"
FT COILED 662..724
FT /evidence="ECO:0000255"
FT COILED 777..806
FT /evidence="ECO:0000255"
FT MOTIF 724..726
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 742
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 1093
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..91
FT /evidence="ECO:0000250"
FT DISULFID 84..98
FT /evidence="ECO:0000250"
FT DISULFID 101..110
FT /evidence="ECO:0000250"
FT DISULFID 113..129
FT /evidence="ECO:0000250"
FT DISULFID 132..146
FT /evidence="ECO:0000250"
FT DISULFID 134..155
FT /evidence="ECO:0000250"
FT DISULFID 157..166
FT /evidence="ECO:0000250"
FT DISULFID 169..184
FT /evidence="ECO:0000250"
FT DISULFID 187..202
FT /evidence="ECO:0000250"
FT DISULFID 189..209
FT /evidence="ECO:0000250"
FT DISULFID 212..221
FT /evidence="ECO:0000250"
FT DISULFID 224..238
FT /evidence="ECO:0000250"
FT DISULFID 273
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 276
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1005..1035
FT /evidence="ECO:0000250"
FT DISULFID 1201..1227
FT /evidence="ECO:0000250"
FT DISULFID 1370..1402
FT /evidence="ECO:0000250"
FT DISULFID 1617..1640
FT /evidence="ECO:0000250"
FT DISULFID 1792..1820
FT /evidence="ECO:0000250"
FT VAR_SEQ 66..120
FT /note="KCNAGFFHTLSGECVPCDCNGNSNECLDGSGYCVHCQRNTTGEHCEKCLDGY
FT IGD -> VQCPCHCHPAGAPAPPRAVPHSSFSLSPPLSSPQCLESFTWARSVRKLEIKS
FT FPL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_038853"
FT VAR_SEQ 121..1823
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_038854"
FT VAR_SEQ 266..272
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7781776,
FT ECO:0000303|PubMed:7959779, ECO:0000303|PubMed:8706685"
FT /id="VSP_017542"
FT VARIANT 94
FT /note="G -> S (in dbSNP:rs35349917)"
FT /id="VAR_056140"
FT VARIANT 154
FT /note="R -> W (in dbSNP:rs11757455)"
FT /id="VAR_056141"
FT VARIANT 283
FT /note="A -> E (in dbSNP:rs9400522)"
FT /id="VAR_061348"
FT VARIANT 492
FT /note="L -> H (in dbSNP:rs3752579)"
FT /id="VAR_056142"
FT VARIANT 498
FT /note="Y -> H (in dbSNP:rs1050348)"
FT /evidence="ECO:0000269|PubMed:7959779,
FT ECO:0000269|PubMed:8706685"
FT /id="VAR_025550"
FT VARIANT 950
FT /note="P -> L (in CMD1JJ; loss of integrin-binding
FT capacity)"
FT /evidence="ECO:0000269|PubMed:17646580"
FT /id="VAR_069708"
FT VARIANT 1117
FT /note="G -> S (in dbSNP:rs2032567)"
FT /evidence="ECO:0000269|PubMed:7781776,
FT ECO:0000269|PubMed:7959779, ECO:0000269|PubMed:8706685"
FT /id="VAR_025551"
FT VARIANT 1119
FT /note="P -> R (in dbSNP:rs1050349)"
FT /evidence="ECO:0000269|PubMed:7781776,
FT ECO:0000269|PubMed:7959779, ECO:0000269|PubMed:8706685"
FT /id="VAR_025552"
FT VARIANT 1549
FT /note="N -> S (in dbSNP:rs12110554)"
FT /evidence="ECO:0000269|PubMed:8706685"
FT /id="VAR_056143"
FT VARIANT 1815
FT /note="V -> I (in dbSNP:rs3734292)"
FT /id="VAR_056144"
FT CONFLICT 143
FT /note="A -> P (in Ref. 1; AAB34635)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="L -> F (in Ref. 1; AAB34635)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="A -> D (in Ref. 1; AAB34635, 2; CAA62596, 3;
FT BAE06109 and 8; CAA54258)"
FT /evidence="ECO:0000305"
FT CONFLICT 1064
FT /note="T -> P (in Ref. 1; AAB34635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1823 AA; 202524 MW; 25BFB6120C2A86F1 CRC64;
MALSSAWRSV LPLWLLWSAA CSRAASGDDN AFPFDIEGSS AVGRQDPPET SEPRVALGRL
PPAAEKCNAG FFHTLSGECV PCDCNGNSNE CLDGSGYCVH CQRNTTGEHC EKCLDGYIGD
SIRGAPQFCQ PCPCPLPHLA NFAESCYRKN GAVRCICNEN YAGPNCERCA PGYYGNPLLI
GSTCKKCDCS GNSDPNLIFE DCDEVTGQCR NCLRNTTGFK CERCAPGYYG DARIAKNCAV
CNCGGGPCDS VTGECLEEGF EPPTGMDCPT ISCDKCVWDL TDALRLAALS IEEGKSGVLS
VSSGAAAHRH VNEINATIYL LKTKLSEREN QYALRKIQIN NAENTMKSLL SDVEELVEKE
NQASRKGQLV QKESMDTINH ASQLVEQAHD MRDKIQEINN KMLYYGEEHE LSPKEISEKL
VLAQKMLEEI RSRQPFFTQR ELVDEEADEA YELLSQAESW QRLHNETRTL FPVVLEQLDD
YNAKLSDLQE ALDQALNYVR DAEDMNRATA ARQRDHEKQQ ERVREQMEVV NMSLSTSADS
LTTPRLTLSE LDDIIKNASG IYAEIDGAKS ELQVKLSNLS NLSHDLVQEA IDHAQDLQQE
ANELSRKLHS SDMNGLVQKA LDASNVYENI VNYVSEANET AEFALNTTDR IYDAVSGIDT
QIIYHKDESE NLLNQARELQ AKAESSSDEA VADTSRRVGG ALARKSALKT RLSDAVKQLQ
AAERGDAQQR LGQSRLITEE ANRTTMEVQQ ATAPMANNLT NWSQNLQHFD SSAYNTAVNS
ARDAVRNLTE VVPQLLDQLR TVEQKRPASN VSASIQRIRE LIAQTRSVAS KIQVSMMFDG
QSAVEVHSRT SMDDLKAFTS LSLYMKPPVK RPELTETADQ FILYLGSKNA KKEYMGLAIK
NDNLVYVYNL GTKDVEIPLD SKPVSSWPAY FSIVKIERVG KHGKVFLTVP SLSSTAEEKF
IKKGEFSGDD SLLDLDPEDT VFYVGGVPSN FKLPTSLNLP GFVGCLELAT LNNDVISLYN
FKHIYNMDPS TSVPCARDKL AFTQSRAASY FFDGSGYAVV RDITRRGKFG QVTRFDIEVR
TPADNGLILL MVNGSMFFRL EMRNGYLHVF YDFGFSGGPV HLEDTLKKAQ INDAKYHEIS
IIYHNDKKMI LVVDRRHVKS MDNEKMKIPF TDIYIGGAPP EILQSRALRA HLPLDINFRG
CMKGFQFQKK DFNLLEQTET LGVGYGCPED SLISRRAYFN GQSFIASIQK ISFFDGFEGG
FNFRTLQPNG LLFYYASGSD VFSISLDNGT VIMDVKGIKV QSVDKQYNDG LSHFVISSVS
PTRYELIVDK SRVGSKNPTK GKIEQTQASE KKFYFGGSPI SAQYANFTGC ISNAYFTRVD
RDVEVEDFQR YTEKVHTSLY ECPIESSPLF LLHKKGKNLS KPKASQNKKG GKSKDAPSWD
PVALKLPERN TPRNSHCHLS NSPRAIEHAY QYGGTANSRQ EFEHLKGDFG AKSQFSIRLR
TRSSHGMIFY VSDQEENDFM TLFLAHGRLV YMFNVGHKKL KIRSQEKYND GLWHDVIFIR
ERSSGRLVID GLRVLEESLP PTEATWKIKG PIYLGGVAPG KAVKNVQINS IYSFSGCLSN
LQLNGASITS ASQTFSVTPC FEGPMETGTY FSTEGGYVVL DESFNIGLKF EIAFEVRPRS
SSGTLVHGHS VNGEYLNVHM KNGQVIVKVN NGIRDFSTSV TPKQSLCDGR WHRITVIRDS
NVVQLDVDSE VNHVVGPLNP KPIDHREPVF VGGVPESLLT PRLAPSKPFT GCIRHFVIDG
HPVSFSKAAL VSGAVSINSC PAA
