GenomeNet

Database: UniProt
Entry: Q16787
LinkDB: Q16787
Original site: Q16787 
ID   LAMA3_HUMAN             Reviewed;        3333 AA.
AC   Q16787; B0YJ33; Q13679; Q13680; Q6VU67; Q6VU68; Q6VU69; Q76E14;
AC   Q96TG0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   13-FEB-2019, entry version 189.
DE   RecName: Full=Laminin subunit alpha-3;
DE   AltName: Full=Epiligrin 170 kDa subunit;
DE            Short=E170;
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; Synonyms=LAMNA;
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] (ISOFORMS 2; 3 AND 4), AND DISEASE.
RX   PubMed=12915477; DOI=10.1093/hmg/ddg234;
RA   McLean W.H.I., Irvine A.D., Hamill K.J., Whittock N.V.,
RA   Coleman-Campbell C.M., Mellerio J.E., Ashton G.S.,
RA   Dopping-Hepenstal P.J.H., Eady R.A.J., Jamil T., Phillips R.J.,
RA   Shabbir S.G., Haroon T.S., Khurshid K., Moore J.E., Page B.,
RA   Darling J., Atherton D.J., Van Steensel M.A.M., Munro C.S.,
RA   Smith F.J.D., McGrath J.A.;
RT   "An unusual N-terminal deletion of the laminin alpha3a isoform leads
RT   to the chronic granulation tissue disorder laryngo-onycho-cutaneous
RT   syndrome.";
RL   Hum. Mol. Genet. 12:2395-2409(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND VARIANT GLY-2834.
RX   PubMed=15044476; DOI=10.1074/jbc.M400670200;
RA   Kariya Y., Yasuda C., Nakashima Y., Ishida K., Tsubota Y.,
RA   Miyazaki K.;
RT   "Characterization of laminin 5B and NH2-terminal proteolytic fragment
RT   of its alpha3B chain: promotion of cellular adhesion, migration, and
RT   proliferation.";
RL   J. Biol. Chem. 279:24774-24784(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Stockwell T.B., Busam D.A., Ferriera S.M., Brownley A.N.,
RA   Strausberg R.L., Kirkness E.F., Rogers Y.-H., Levy S.;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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.,
RA   Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA   Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA   Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA   Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA   Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA   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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-2858 (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [MRNA] OF 1528-2858 (ISOFORMS 1/2).
RC   TISSUE=Keratinocyte;
RX   PubMed=8586427; DOI=10.1006/geno.1995.9877;
RA   Vidal F., Baudoin C., Miquel C., Galliano M.-F., Christiano A.M.,
RA   Uitto J., Ortonne J.-P., Meneguzzi G.;
RT   "Cloning of the laminin alpha 3 chain gene (LAMA3) and identification
RT   of a homozygous deletion in a patient with Herlitz junctional
RT   epidermolysis bullosa.";
RL   Genomics 30:273-280(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1528-3333 (ISOFORMS 1/2), AND VARIANT
RP   GLY-2834.
RA   Aberdam D., Vidal F., Baudoin C., Miquel C., Ortonne J.-P.,
RA   Meneguzzi G.;
RT   "Mutation in LAMA3 gene in a patient affected by H-Jeb.";
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-2834.
RC   TISSUE=Keratinocyte;
RX   PubMed=8077230;
RA   Ryan M.C., Tizard R., Vandevanter D.R., Carter W.G.;
RT   "Cloning of the LamA3 gene encoding the alpha 3 chain of the adhesive
RT   ligand epiligrin. Expression in wound repair.";
RL   J. Biol. Chem. 269:22779-22787(1994).
RN   [8]
RP   INVOLVEMENT IN H-JEB.
RX   PubMed=8530087; DOI=10.1006/geno.1995.1246;
RA   McGrath J.A., Kivirikko S., Ciatti S., Moss C., Dunnill G.S.,
RA   Eady R.A., Rodeck C.H., Christiano A.M., Uitto J.;
RT   "A homozygous nonsense mutation in the alpha 3 chain gene of laminin 5
RT   (LAMA3) in Herlitz junctional epidermolysis bullosa: prenatal
RT   exclusion in a fetus at risk.";
RL   Genomics 29:282-284(1995).
RN   [9]
RP   INVOLVEMENT IN H-JEB.
RX   PubMed=7633458; DOI=10.1093/hmg/4.5.959;
RA   Kivirikko S., McGrath J.A., Baudoin C., Aberdam D., Ciatti S.,
RA   Dunnill M.G., McMillan J.R., Eady R.A., Ortonne J.P., Meneguzzi G.;
RT   "A homozygous nonsense mutation in the alpha 3 chain gene of laminin 5
RT   (LAMA3) in lethal (Herlitz) junctional epidermolysis bullosa.";
RL   Hum. Mol. Genet. 4:959-962(1995).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
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   -!- FUNCTION: Laminin-5 is thought to be involved in (1) cell adhesion
CC       via integrin alpha-3/beta-1 in focal adhesion and integrin alpha-
CC       6/beta-4 in hemidesmosomes, (2) signal transduction via tyrosine
CC       phosphorylation of pp125-FAK and p80, (3) differentiation of
CC       keratinocytes.
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-3 is a subunit of laminin-5 (laminin-332 or
CC       epiligrin/kalinin/nicein), laminin-6 (laminin-311 or K-laminin)
CC       and laminin-7 (laminin-321 or KS-laminin).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane. Note=Major component.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=2; Synonyms=B;
CC         IsoId=Q16787-2; Sequence=Displayed;
CC       Name=1; Synonyms=A;
CC         IsoId=Q16787-1; Sequence=VSP_035738, VSP_035739;
CC       Name=3;
CC         IsoId=Q16787-3; Sequence=VSP_043487;
CC       Name=4;
CC         IsoId=Q16787-4; Sequence=VSP_047079, VSP_047080, VSP_043487;
CC   -!- TISSUE SPECIFICITY: Skin; respiratory, urinary, and digestive
CC       epithelia and in other specialized tissues with prominent
CC       secretory or protective functions. Epithelial basement membrane,
CC       and epithelial cell tongue that migrates into a wound bed. A
CC       differential and focal expression of the subunit alpha-3 is
CC       observed in the CNS.
CC   -!- INDUCTION: Laminin-5 is up-regulated in wound sites of human skin.
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: Epidermolysis bullosa, junctional, Herlitz type (H-JEB)
CC       [MIM:226700]: An infantile and lethal form of junctional
CC       epidermolysis bullosa, a group of blistering skin diseases
CC       characterized by tissue separation which occurs within the dermo-
CC       epidermal basement In the Herlitz type, death occurs usually
CC       within the first six months of life. Occasionally, children
CC       survive to teens. It is marked by bullous lesions at birth and
CC       extensive denudation of skin and mucous membranes that may be
CC       hemorrhagic. {ECO:0000269|PubMed:7633458,
CC       ECO:0000269|PubMed:8530087}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Laryngoonychocutaneous syndrome (LOCS) [MIM:245660]:
CC       Autosomal recessive epithelial disorder confined to the Punjabi
CC       Muslim population. The condition is characterized by cutaneous
CC       erosions, nail dystrophy and exuberant vascular granulation tissue
CC       in certain epithelia, especially conjunctiva and larynx.
CC       {ECO:0000269|PubMed:12915477}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
DR   EMBL; AY327114; AAQ72569.1; -; mRNA.
DR   EMBL; AY327115; AAQ72570.1; -; mRNA.
DR   EMBL; AY327116; AAQ72571.1; -; mRNA.
DR   EMBL; AB107369; BAD13428.1; -; Genomic_DNA.
DR   EMBL; EF444992; ACA06011.1; -; Genomic_DNA.
DR   EMBL; AC010754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC067796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X85107; CAA59428.1; -; mRNA.
DR   EMBL; X85108; CAA59429.1; -; mRNA.
DR   EMBL; X84900; CAA59325.1; -; mRNA.
DR   EMBL; L34155; AAA59483.1; -; mRNA.
DR   CCDS; CCDS11880.1; -. [Q16787-1]
DR   CCDS; CCDS42419.1; -. [Q16787-2]
DR   CCDS; CCDS45838.1; -. [Q16787-3]
DR   CCDS; CCDS59307.1; -. [Q16787-4]
DR   PIR; A55347; A55347.
DR   RefSeq; NP_000218.3; NM_000227.4.
DR   RefSeq; NP_001121189.2; NM_001127717.2.
DR   RefSeq; NP_001121190.2; NM_001127718.2.
DR   RefSeq; NP_001289925.1; NM_001302996.1.
DR   RefSeq; NP_937762.2; NM_198129.2.
DR   UniGene; Hs.436367; -.
DR   ProteinModelPortal; Q16787; -.
DR   SMR; Q16787; -.
DR   BioGrid; 110103; 25.
DR   ComplexPortal; CPX-1774; Laminin-332 complex variant A. [Q16787-1]
DR   ComplexPortal; CPX-1775; Laminin-311 complex variant A. [Q16787-1]
DR   ComplexPortal; CPX-1776; Laminin-321 complex. [Q16787-1]
DR   ComplexPortal; CPX-3165; Laminin-332 complex variant B. [Q16787-2]
DR   ComplexPortal; CPX-3166; Laminin-311 complex variant B. [Q16787-2]
DR   CORUM; Q16787; -.
DR   IntAct; Q16787; 5.
DR   MINT; Q16787; -.
DR   STRING; 9606.ENSP00000324532; -.
DR   ChEMBL; CHEMBL2364187; -.
DR   iPTMnet; Q16787; -.
DR   PhosphoSitePlus; Q16787; -.
DR   SwissPalm; Q16787; -.
DR   BioMuta; LAMA3; -.
DR   DMDM; 215274012; -.
DR   EPD; Q16787; -.
DR   jPOST; Q16787; -.
DR   PaxDb; Q16787; -.
DR   PeptideAtlas; Q16787; -.
DR   PRIDE; Q16787; -.
DR   ProteomicsDB; 61068; -.
DR   ProteomicsDB; 61069; -. [Q16787-1]
DR   ProteomicsDB; 61070; -. [Q16787-3]
DR   DNASU; 3909; -.
DR   Ensembl; ENST00000313654; ENSP00000324532; ENSG00000053747.
DR   GeneID; 3909; -.
DR   KEGG; hsa:3909; -.
DR   UCSC; uc002kuq.4; human. [Q16787-2]
DR   CTD; 3909; -.
DR   DisGeNET; 3909; -.
DR   EuPathDB; HostDB:ENSG00000053747.15; -.
DR   GeneCards; LAMA3; -.
DR   GeneReviews; LAMA3; -.
DR   HGNC; HGNC:6483; LAMA3.
DR   HPA; CAB010757; -.
DR   HPA; HPA009309; -.
DR   MalaCards; LAMA3; -.
DR   MIM; 226700; phenotype.
DR   MIM; 245660; phenotype.
DR   MIM; 600805; gene.
DR   neXtProt; NX_Q16787; -.
DR   Orphanet; 79402; Junctional epidermolysis bullosa, generalized intermediate.
DR   Orphanet; 79404; Junctional epidermolysis bullosa, generalized severe.
DR   Orphanet; 2407; LOC syndrome.
DR   PharmGKB; PA30272; -.
DR   eggNOG; KOG1836; Eukaryota.
DR   eggNOG; ENOG410XRDC; LUCA.
DR   HOGENOM; HOG000231235; -.
DR   HOVERGEN; HBG052300; -.
DR   InParanoid; Q16787; -.
DR   KO; K06240; -.
DR   OrthoDB; 2342at2759; -.
DR   PhylomeDB; Q16787; -.
DR   TreeFam; TF335359; -.
DR   Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; R-HSA-2214320; Anchoring fibril formation.
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-446107; Type I hemidesmosome assembly.
DR   Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR   SIGNOR; Q16787; -.
DR   ChiTaRS; LAMA3; human.
DR   GeneWiki; Laminin,_alpha_3; -.
DR   GenomeRNAi; 3909; -.
DR   PRO; PR:Q16787; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   Bgee; ENSG00000053747; Expressed in 173 organ(s), highest expression level in ectocervix.
DR   ExpressionAtlas; Q16787; baseline and differential.
DR   Genevisible; Q16787; HS.
DR   GO; GO:0005604; C:basement membrane; TAS:ProtInc.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005610; C:laminin-5 complex; IEA:Ensembl.
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:0005198; F:structural molecule activity; NAS:ProtInc.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
DR   GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0031581; P:hemidesmosome assembly; TAS:Reactome.
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   Gene3D; 2.60.120.1490; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013032; EGF-like_CS.
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   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 12.
DR   Pfam; PF02210; Laminin_G_2; 5.
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; 12.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 13.
DR   PROSITE; PS50027; EGF_LAM_2; 14.
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   Complete proteome; Disulfide bond; Epidermolysis bullosa;
KW   Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW   Polymorphism; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     35       {ECO:0000255}.
FT   CHAIN        36   3333       Laminin subunit alpha-3.
FT                                /FTId=PRO_0000017058.
FT   DOMAIN       43    298       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      299    355       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      356    425       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      426    469       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      491    535       Laminin EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      536    588       Laminin EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      590    630       Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      631    683       Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      684    728       Laminin EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1266   1311       Laminin EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1312   1355       Laminin EGF-like 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1356   1404       Laminin EGF-like 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1405   1455       Laminin EGF-like 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1476   1653       Laminin IV type A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00458}.
FT   DOMAIN     1687   1733       Laminin EGF-like 13.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1734   1786       Laminin EGF-like 14.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1787   1821       Laminin EGF-like 15; truncated.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     2390   2591       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     2598   2760       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     2767   2927       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     2986   3150       Laminin G-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     3157   3330       Laminin G-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   REGION      298    728       Domain V.
FT   REGION      796   1265       Domain IV 1 (domain IV B).
FT   REGION     1266   1465       Domain III B.
FT   REGION     1654   1821       Domain III A.
FT   REGION     1822   2389       Domain II and I.
FT   COILED     1852   1941       {ECO:0000255}.
FT   COILED     1987   2169       {ECO:0000255}.
FT   COILED     2322   2388       {ECO:0000255}.
FT   MOTIF      2278   2280       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD    142    142       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    242    242       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2365   2365       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2502   2502       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2584   2584       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    299    308       {ECO:0000250}.
FT   DISULFID    301    319       {ECO:0000250}.
FT   DISULFID    321    330       {ECO:0000250}.
FT   DISULFID    333    353       {ECO:0000250}.
FT   DISULFID    356    365       {ECO:0000250}.
FT   DISULFID    358    390       {ECO:0000250}.
FT   DISULFID    393    402       {ECO:0000250}.
FT   DISULFID    405    423       {ECO:0000250}.
FT   DISULFID    426    436       {ECO:0000250}.
FT   DISULFID    428    443       {ECO:0000250}.
FT   DISULFID    445    454       {ECO:0000250}.
FT   DISULFID    457    467       {ECO:0000250}.
FT   DISULFID    491    503       {ECO:0000250}.
FT   DISULFID    493    509       {ECO:0000250}.
FT   DISULFID    511    520       {ECO:0000250}.
FT   DISULFID    523    533       {ECO:0000250}.
FT   DISULFID    536    548       {ECO:0000250}.
FT   DISULFID    538    555       {ECO:0000250}.
FT   DISULFID    557    566       {ECO:0000250}.
FT   DISULFID    569    586       {ECO:0000250}.
FT   DISULFID    601    610       {ECO:0000250}.
FT   DISULFID    613    628       {ECO:0000250}.
FT   DISULFID    631    645       {ECO:0000250}.
FT   DISULFID    633    652       {ECO:0000250}.
FT   DISULFID    654    663       {ECO:0000250}.
FT   DISULFID    666    681       {ECO:0000250}.
FT   DISULFID    684    696       {ECO:0000250}.
FT   DISULFID    686    703       {ECO:0000250}.
FT   DISULFID    705    714       {ECO:0000250}.
FT   DISULFID   1266   1278       {ECO:0000250}.
FT   DISULFID   1268   1285       {ECO:0000250}.
FT   DISULFID   1287   1296       {ECO:0000250}.
FT   DISULFID   1299   1309       {ECO:0000250}.
FT   DISULFID   1312   1319       {ECO:0000250}.
FT   DISULFID   1314   1326       {ECO:0000250}.
FT   DISULFID   1328   1337       {ECO:0000250}.
FT   DISULFID   1340   1353       {ECO:0000250}.
FT   DISULFID   1356   1371       {ECO:0000250}.
FT   DISULFID   1358   1378       {ECO:0000250}.
FT   DISULFID   1380   1389       {ECO:0000250}.
FT   DISULFID   1392   1402       {ECO:0000250}.
FT   DISULFID   1405   1417       {ECO:0000250}.
FT   DISULFID   1407   1424       {ECO:0000250}.
FT   DISULFID   1426   1435       {ECO:0000250}.
FT   DISULFID   1438   1453       {ECO:0000250}.
FT   DISULFID   1687   1696       {ECO:0000250}.
FT   DISULFID   1689   1703       {ECO:0000250}.
FT   DISULFID   1706   1715       {ECO:0000250}.
FT   DISULFID   1718   1731       {ECO:0000250}.
FT   DISULFID   1734   1746       {ECO:0000250}.
FT   DISULFID   1736   1755       {ECO:0000250}.
FT   DISULFID   1757   1766       {ECO:0000250}.
FT   DISULFID   1769   1784       {ECO:0000250}.
FT   DISULFID   1822   1822       Interchain. {ECO:0000305}.
FT   DISULFID   1825   1825       Interchain. {ECO:0000305}.
FT   DISULFID   2561   2591       {ECO:0000250}.
FT   DISULFID   2737   2760       {ECO:0000250}.
FT   DISULFID   2895   2927       {ECO:0000250}.
FT   DISULFID   3127   3150       {ECO:0000250}.
FT   DISULFID   3302   3330       {ECO:0000250}.
FT   VAR_SEQ       1   1620       Missing (in isoform 1).
FT                                {ECO:0000303|PubMed:8586427}.
FT                                /FTId=VSP_035738.
FT   VAR_SEQ       1   1609       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:12915477}.
FT                                /FTId=VSP_047079.
FT   VAR_SEQ    1610   1665       LSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALA
FT                                VEICACPPAYAGDSC -> MPPAVRRSACSMGWLWIFGAAL
FT                                GQCLGYSSQQQRVPFLQPPGQSQLQASYVEFRPS (in
FT                                isoform 4).
FT                                {ECO:0000303|PubMed:12915477}.
FT                                /FTId=VSP_047080.
FT   VAR_SEQ    1621   1665       LYFTETQRLTLSEVGLEEASDTGSGRIALAVEICACPPAYA
FT                                GDSC -> MPPAVRRSACSMGWLWIFGAALGQCLGYSSQQQ
FT                                RVPFLQPPGQSQLQASYVEFRPS (in isoform 1).
FT                                {ECO:0000303|PubMed:8586427}.
FT                                /FTId=VSP_035739.
FT   VAR_SEQ    1946   2002       ILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFG
FT                                KHLREAEADKRESQLL -> M (in isoform 3 and
FT                                isoform 4).
FT                                {ECO:0000303|PubMed:12915477}.
FT                                /FTId=VSP_043487.
FT   VARIANT     796    796       T -> N (in dbSNP:rs17187262).
FT                                /FTId=VAR_050078.
FT   VARIANT    1206   1206       V -> A (in dbSNP:rs12457323).
FT                                /FTId=VAR_050079.
FT   VARIANT    1208   1208       P -> T (in dbSNP:rs17202961).
FT                                /FTId=VAR_050080.
FT   VARIANT    1774   1774       F -> L (in dbSNP:rs958631).
FT                                /FTId=VAR_059444.
FT   VARIANT    2702   2702       T -> A (in dbSNP:rs9952370).
FT                                /FTId=VAR_047374.
FT   VARIANT    2815   2815       N -> K (in dbSNP:rs1154232).
FT                                /FTId=VAR_047375.
FT   VARIANT    2834   2834       S -> G (in dbSNP:rs1154233).
FT                                {ECO:0000269|PubMed:15044476,
FT                                ECO:0000269|PubMed:8077230,
FT                                ECO:0000269|Ref.6}.
FT                                /FTId=VAR_059445.
FT   CONFLICT   1544   1544       G -> A (in Ref. 5; CAA59429 and 6;
FT                                CAA59325). {ECO:0000305}.
FT   CONFLICT   1743   1745       ATG -> GMC (in Ref. 5; CAA59428/
FT                                CAA59429). {ECO:0000305}.
FT   CONFLICT   2101   2101       M -> K (in Ref. 5; CAA59428/CAA59429).
FT                                {ECO:0000305}.
FT   CONFLICT   2374   2374       R -> L (in Ref. 5; CAA59428/CAA59429).
FT                                {ECO:0000305}.
FT   CONFLICT   2589   2589       E -> Q (in Ref. 5; CAA59428/CAA59429).
FT                                {ECO:0000305}.
FT   CONFLICT   2672   2672       D -> A (in Ref. 5; CAA59428/CAA59429).
FT                                {ECO:0000305}.
FT   CONFLICT   2804   2804       G -> A (in Ref. 5; CAA59428/CAA59429).
FT                                {ECO:0000305}.
SQ   SEQUENCE   3333 AA;  366649 MW;  9F99AF49B8EF27DD CRC64;
     MAAAARPRGR ALGPVLPPTP LLLLVLRVLP ACGATARDPG AAAGLSLHPT YFNLAEAARI
     WATATCGERG PGEGRPQPEL YCKLVGGPTA PGSGHTIQGQ FCDYCNSEDP RKAHPVTNAI
     DGSERWWQSP PLSSGTQYNR VNLTLDLGQL FHVAYILIKF ANSPRPDLWV LERSVDFGST
     YSPWQYFAHS KVDCLKEFGR EANMAVTRDD DVLCVTEYSR IVPLENGEVV VSLINGRPGA
     KNFTFSHTLR EFTKATNIRL RFLRTNTLLG HLISKAQRDP TVTRRYYYSI KDISIGGQCV
     CNGHAEVCNI NNPEKLFRCE CQHHTCGETC DRCCTGYNQR RWRPAAWEQS HECEACNCHG
     HASNCYYDPD VERQQASLNT QGIYAGGGVC INCQHNTAGV NCEQCAKGYY RPYGVPVDAP
     DGCIPCSCDP EHADGCEQGS GRCHCKPNFH GDNCEKCAIG YYNFPFCLRI PIFPVSTPSS
     EDPVAGDIKG CDCNLEGVLP EICDAHGRCL CRPGVEGPRC DTCRSGFYSF PICQACWCSA
     LGSYQMPCSS VTGQCECRPG VTGQRCDRCL SGAYDFPHCQ GSSSACDPAG TINSNLGYCQ
     CKLHVEGPTC SRCKLLYWNL DKENPSGCSE CKCHKAGTVS GTGECRQGDG DCHCKSHVGG
     DSCDTCEDGY FALEKSNYFG CQGCQCDIGG ALSSMCSGPS GVCQCREHVV GKVCQRPENN
     YYFPDLHHMK YEIEDGSTPN GRDLRFGFDP LAFPEFSWRG YAQMTSVQND VRITLNVGKS
     SGSLFRVILR YVNPGTEAVS GHITIYPSWG AAQSKEIIFL PSKEPAFVTV PGNGFADPFS
     ITPGIWVACI KAEGVLLDYL VLLPRDYYEA SVLQLPVTEP CAYAGPPQEN CLLYQHLPVT
     RFPCTLACEA RHFLLDGEPR PVAVRQPTPA HPVMVDLSGR EVELHLRLRI PQVGHYVVVV
     EYSTEAAQLF VVDVNVKSSG SVLAGQVNIY SCNYSVLCRS AVIDHMSRIA MYELLADADI
     QLKGHMARFL LHQVCIIPIE EFSAEYVRPQ VHCIASYGRF VNQSATCVSL AHETPPTALI
     LDVLSGRPFP HLPQQSSPSV DVLPGVTLKA PQNQVTLRGR VPHLGRYVFV IHFYQAAHPT
     FPAQVSVDGG WPRAGSFHAS FCPHVLGCRD QVIAEGQIEF DISEPEVAAT VKVPEGKSLV
     LVRVLVVPAE NYDYQILHKK SMDKSLEFIT NCGKNSFYLD PQTASRFCKN SARSLVAFYH
     KGALPCECHP TGATGPHCSP EGGQCPCQPN VIGRQCTRCA TGHYGFPRCK PCSCGRRLCE
     EMTGQCRCPP RTVRPQCEVC ETHSFSFHPM AGCEGCNCSR RGTIEAAMPE CDRDSGQCRC
     KPRITGRQCD RCASGFYRFP ECVPCNCNRD GTEPGVCDPG TGACLCKENV EGTECNVCRE
     GSFHLDPANL KGCTSCFCFG VNNQCHSSHK RRTKFVDMLG WHLETADRVD IPVSFNPGSN
     SMVADLQELP ATIHSASWVA PTSYLGDKVS SYGGYLTYQA KSFGLPGDMV LLEKKPDVQL
     TGQHMSIIYE ETNTPRPDRL HHGRVHVVEG NFRHASSRAP VSREELMTVL SRLADVRIQG
     LYFTETQRLT LSEVGLEEAS DTGSGRIALA VEICACPPAY AGDSCQGCSP GYYRDHKGLY
     TGRCVPCNCN GHSNQCQDGS GICVNCQHNT AGEHCERCQE GYYGNAVHGS CRACPCPHTN
     SFATGCVVNG GDVRCSCKAG YTGTQCERCA PGYFGNPQKF GGSCQPCSCN SNGQLGSCHP
     LTGDCINQEP KDSSPAEECD DCDSCVMTLL NDLATMGEQL RLVKSQLQGL SASAGLLEQM
     RHMETQAKDL RNQLLNYRSA ISNHGSKIEG LERELTDLNQ EFETLQEKAQ VNSRKAQTLN
     NNVNRATQSA KELDVKIKNV IRNVHILLKQ ISGTDGEGNN VPSGDFSREW AEAQRMMREL
     RNRNFGKHLR EAEADKRESQ LLLNRIRTWQ KTHQGENNGL ANSIRDSLNE YEAKLSDLRA
     RLQEAAAQAK QANGLNQENE RALGAIQRQV KEINSLQSDF TKYLTTADSS LLQTNIALQL
     MEKSQKEYEK LAASLNEARQ ELSDKVRELS RSAGKTSLVE EAEKHARSLQ ELAKQLEEIK
     RNASGDELVR CAVDAATAYE NILNAIKAAE DAANRAASAS ESALQTVIKE DLPRKAKTLS
     SNSDKLLNEA KMTQKKLKQE VSPALNNLQQ TLNIVTVQKE VIDTNLTTLR DGLHGIQRGD
     IDAMISSAKS MVRKANDITD EVLDGLNPIQ TDVERIKDTY GRTQNEDFKK ALTDADNSVN
     KLTNKLPDLW RKIESINQQL LPLGNISDNM DRIRELIQQA RDAASKVAVP MRFNGKSGVE
     VRLPNDLEDL KGYTSLSLFL QRPNSRENGG TENMFVMYLG NKDASRDYIG MAVVDGQLTC
     VYNLGDREAE LQVDQILTKS ETKEAVMDRV KFQRIYQFAR LNYTKGATSS KPETPGVYDM
     DGRNSNTLLN LDPENVVFYV GGYPPDFKLP SRLSFPPYKG CIELDDLNEN VLSLYNFKKT
     FNLNTTEVEP CRRRKEESDK NYFEGTGYAR VPTQPHAPIP TFGQTIQTTV DRGLLFFAEN
     GDRFISLNIE DGKLMVRYKL NSELPKERGV GDAINNGRDH SIQIKIGKLQ KRMWINVDVQ
     NTIIDGEVFD FSTYYLGGIP IAIRERFNIS TPAFRGCMKN LKKTSGVVRL NDTVGVTKKC
     SEDWKLVRSA SFSRGGQLSF TDLGLPPTDH LQASFGFQTF QPSGILLDHQ TWTRNLQVTL
     EDGYIELSTS DSGSPIFKSP QTYMDGLLHY VSVISDNSGL RLLIDDQLLR NSKRLKHISS
     SRQSLRLGGS NFEGCISNVF VQRLSLSPEV LDLTSNSLKR DVSLGGCSLN KPPFLMLLKG
     STRFNKTKTF RINQLLQDTP VASPRSVKVW QDACSPLPKT QANHGALQFG DIPTSHLLFK
     LPQELLKPRS QFAVDMQTTS SRGLVFHTGT KNSFMALYLS KGRLVFALGT DGKKLRIKSK
     EKCNDGKWHT VVFGHDGEKG RLVVDGLRAR EGSLPGNSTI SIRAPVYLGS PPSGKPKSLP
     TNSFVGCLKN FQLDSKPLYT PSSSFGVSSC LGGPLEKGIY FSEEGGHVVL AHSVLLGPEF
     KLVFSIRPRS LTGILIHIGS QPGKHLCVYL EAGKVTASMD SGAGGTSTSV TPKQSLCDGQ
     WHSVAVTIKQ HILHLELDTD SSYTAGQIPF PPASTQEPLH LGGAPANLTT LRIPVWKSFF
     GCLRNIHVNH IPVPVTEALE VQGPVSLNGC PDQ
//
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