GenomeNet

Database: UniProt
Entry: Q16363
LinkDB: Q16363
Original site: Q16363 
ID   LAMA4_HUMAN             Reviewed;        1823 AA.
AC   Q16363; Q14731; Q14735; Q15335; Q4LE44; Q5SZG8; Q9BTB8; Q9UE18;
AC   Q9UJN9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 4.
DT   13-FEB-2019, entry version 191.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS SER-1117 AND
RP   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
RT   chain.";
RL   FEBS Lett. 365:183-188(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS HIS-498;
RP   SER-1117; 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
RT   the 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.,
RA   Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
RT   "Preparation of a set of expression-ready clones of mammalian long
RT   cDNAs 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
RT   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.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   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.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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
RT   project: 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
RT   alpha4.";
RL   Eur. J. Biochem. 248:15-23(1997).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 236-1823 (ISOFORM 2), AND VARIANTS
RP   HIS-498; 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
RT   a 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;
RP   ASN-742; 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
RT   multiple 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
RP   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
RT   endothelial cells.";
RL   Circulation 116:515-525(2007).
CC   -!- FUNCTION: Binding to cells via a high affinity receptor, laminin
CC       is thought to mediate the attachment, migration and organization
CC       of cells into tissues during embryonic development by interacting
CC       with other extracellular matrix components.
CC   -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC       different polypeptide chains (alpha, beta, gamma), which are bound
CC       to each other by disulfide bonds into a cross-shaped molecule
CC       comprising one long and three short arms with globules at each
CC       end. Alpha-4 is a subunit of laminin-8 (laminin-411), laminin-9
CC       (laminin-421) and laminin-14 (laminin-423).
CC   -!- INTERACTION:
CC       P04637:TP53; NbExp=2; IntAct=EBI-711505, EBI-366083;
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,
CC       ovary small and large intestines, placenta, liver; weak or no
CC       expression in skeletal muscle, kidney, pancreas, testis, prostate,
CC       brain. High expression in fetal lung and kidney. Expression in
CC       fetal and newborn tissues is observed in certain mesenchymal cells
CC       in tissues such as smooth muscle and dermis.
CC   -!- DOMAIN: The alpha-helical domains I and II are thought to interact
CC       with other laminin chains to form a coiled coil structure.
CC   -!- DOMAIN: Domain G is globular.
CC   -!- DISEASE: Cardiomyopathy, dilated 1JJ (CMD1JJ) [MIM:615235]: A
CC       disorder characterized by ventricular dilation and impaired
CC       systolic function, resulting in congestive heart failure and
CC       arrhythmia. Patients are at risk of premature death.
CC       {ECO:0000269|PubMed:17646580}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- CAUTION: Gene LAMA4 was formerly called LAMA3. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE06109.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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   UniGene; Hs.654572; -.
DR   ProteinModelPortal; Q16363; -.
DR   SMR; Q16363; -.
DR   BioGrid; 110104; 24.
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; 21.
DR   MINT; Q16363; -.
DR   STRING; 9606.ENSP00000230538; -.
DR   ChEMBL; CHEMBL2364187; -.
DR   GlyConnect; 1440; -.
DR   iPTMnet; Q16363; -.
DR   PhosphoSitePlus; Q16363; -.
DR   SwissPalm; Q16363; -.
DR   BioMuta; LAMA4; -.
DR   DMDM; 292495093; -.
DR   EPD; Q16363; -.
DR   jPOST; Q16363; -.
DR   MaxQB; Q16363; -.
DR   PaxDb; Q16363; -.
DR   PeptideAtlas; Q16363; -.
DR   PRIDE; Q16363; -.
DR   ProteomicsDB; 60862; -.
DR   ProteomicsDB; 60863; -. [Q16363-2]
DR   ProteomicsDB; 60864; -. [Q16363-3]
DR   DNASU; 3910; -.
DR   Ensembl; ENST00000368638; ENSP00000357627; ENSG00000112769. [Q16363-3]
DR   Ensembl; ENST00000453937; ENSP00000398226; ENSG00000112769. [Q16363-3]
DR   Ensembl; ENST00000455073; ENSP00000408604; ENSG00000112769. [Q16363-3]
DR   GeneID; 3910; -.
DR   KEGG; hsa:3910; -.
DR   UCSC; uc010kdz.3; human. [Q16363-1]
DR   CTD; 3910; -.
DR   DisGeNET; 3910; -.
DR   EuPathDB; HostDB:ENSG00000112769.18; -.
DR   GeneCards; LAMA4; -.
DR   HGNC; HGNC:6484; LAMA4.
DR   HPA; CAB078156; -.
DR   HPA; HPA015693; -.
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   eggNOG; ENOG410IP6G; Eukaryota.
DR   eggNOG; ENOG410Z3D5; LUCA.
DR   GeneTree; ENSGT00940000159970; -.
DR   HOVERGEN; HBG052299; -.
DR   InParanoid; Q16363; -.
DR   KO; K06241; -.
DR   OrthoDB; 2342at2759; -.
DR   PhylomeDB; Q16363; -.
DR   TreeFam; TF335359; -.
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   SIGNOR; Q16363; -.
DR   ChiTaRS; LAMA4; human.
DR   GeneWiki; Laminin,_alpha_4; -.
DR   GenomeRNAi; 3910; -.
DR   PRO; PR:Q16363; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000112769; Expressed in 221 organ(s), highest expression level in lung.
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; HDA: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:0030198; P:extracellular matrix organization; TAS:Reactome.
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   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; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
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;
KW   Cell adhesion; Coiled coil; Complete proteome; Disease mutation;
KW   Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Laminin EGF-like domain; Polymorphism; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25   1823       Laminin subunit alpha-4.
FT                                /FTId=PRO_0000017060.
FT   DOMAIN       82    131       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      132    186       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      187    240       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      241    255       Laminin EGF-like 4; truncated.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      833   1035       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1047   1227       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1234   1402       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1469   1640       Laminin G-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1647   1820       Laminin G-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   REGION      256    832       Domain II and I.
FT   COILED      320    403       {ECO:0000255}.
FT   COILED      473    528       {ECO:0000255}.
FT   COILED      581    614       {ECO:0000255}.
FT   COILED      662    724       {ECO:0000255}.
FT   COILED      777    806       {ECO:0000255}.
FT   MOTIF       724    726       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD    104    104       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    215    215       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    315    315       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    465    465       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    531    531       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    557    557       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    578    578       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    581    581       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    638    638       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    646    646       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    742    742       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    758    758       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    761    761       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    787    787       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    810    810       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   1093   1093       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1288   1288       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1366   1366       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1418   1418       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     82     91       {ECO:0000250}.
FT   DISULFID     84     98       {ECO:0000250}.
FT   DISULFID    101    110       {ECO:0000250}.
FT   DISULFID    113    129       {ECO:0000250}.
FT   DISULFID    132    146       {ECO:0000250}.
FT   DISULFID    134    155       {ECO:0000250}.
FT   DISULFID    157    166       {ECO:0000250}.
FT   DISULFID    169    184       {ECO:0000250}.
FT   DISULFID    187    202       {ECO:0000250}.
FT   DISULFID    189    209       {ECO:0000250}.
FT   DISULFID    212    221       {ECO:0000250}.
FT   DISULFID    224    238       {ECO:0000250}.
FT   DISULFID    273    273       Interchain. {ECO:0000305}.
FT   DISULFID    276    276       Interchain. {ECO:0000305}.
FT   DISULFID   1005   1035       {ECO:0000250}.
FT   DISULFID   1201   1227       {ECO:0000250}.
FT   DISULFID   1370   1402       {ECO:0000250}.
FT   DISULFID   1617   1640       {ECO:0000250}.
FT   DISULFID   1792   1820       {ECO:0000250}.
FT   VAR_SEQ      66    120       KCNAGFFHTLSGECVPCDCNGNSNECLDGSGYCVHCQRNTT
FT                                GEHCEKCLDGYIGD -> VQCPCHCHPAGAPAPPRAVPHSS
FT                                FSLSPPLSSPQCLESFTWARSVRKLEIKSFPL (in
FT                                isoform 3). {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.4}.
FT                                /FTId=VSP_038853.
FT   VAR_SEQ     121   1823       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.4}.
FT                                /FTId=VSP_038854.
FT   VAR_SEQ     266    272       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:7781776,
FT                                ECO:0000303|PubMed:7959779,
FT                                ECO:0000303|PubMed:8706685}.
FT                                /FTId=VSP_017542.
FT   VARIANT      94     94       G -> S (in dbSNP:rs35349917).
FT                                /FTId=VAR_056140.
FT   VARIANT     154    154       R -> W (in dbSNP:rs11757455).
FT                                /FTId=VAR_056141.
FT   VARIANT     283    283       A -> E (in dbSNP:rs9400522).
FT                                /FTId=VAR_061348.
FT   VARIANT     492    492       L -> H (in dbSNP:rs3752579).
FT                                /FTId=VAR_056142.
FT   VARIANT     498    498       Y -> H (in dbSNP:rs1050348).
FT                                {ECO:0000269|PubMed:7959779,
FT                                ECO:0000269|PubMed:8706685}.
FT                                /FTId=VAR_025550.
FT   VARIANT     950    950       P -> L (in CMD1JJ; loss of integrin-
FT                                binding capacity).
FT                                {ECO:0000269|PubMed:17646580}.
FT                                /FTId=VAR_069708.
FT   VARIANT    1117   1117       G -> S (in dbSNP:rs2032567).
FT                                {ECO:0000269|PubMed:7781776,
FT                                ECO:0000269|PubMed:7959779,
FT                                ECO:0000269|PubMed:8706685}.
FT                                /FTId=VAR_025551.
FT   VARIANT    1119   1119       P -> R (in dbSNP:rs1050349).
FT                                {ECO:0000269|PubMed:7781776,
FT                                ECO:0000269|PubMed:7959779,
FT                                ECO:0000269|PubMed:8706685}.
FT                                /FTId=VAR_025552.
FT   VARIANT    1549   1549       N -> S (in dbSNP:rs12110554).
FT                                {ECO:0000269|PubMed:8706685}.
FT                                /FTId=VAR_056143.
FT   VARIANT    1815   1815       V -> I (in dbSNP:rs3734292).
FT                                /FTId=VAR_056144.
FT   CONFLICT    143    143       A -> P (in Ref. 1; AAB34635).
FT                                {ECO:0000305}.
FT   CONFLICT    178    178       L -> F (in Ref. 1; AAB34635).
FT                                {ECO:0000305}.
FT   CONFLICT    283    283       A -> D (in Ref. 1; AAB34635, 2; CAA62596,
FT                                3; BAE06109 and 8; CAA54258).
FT                                {ECO:0000305}.
FT   CONFLICT   1064   1064       T -> P (in Ref. 1; AAB34635).
FT                                {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
//
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