ID LAMA3_HUMAN Reviewed; 3333 AA. AC Q16787; B0YJ33; Q13679; Q13680; Q6VU67; Q6VU68; Q6VU69; Q76E14; Q96TG0; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 3. DT 27-NOV-2024, entry version 221. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), INVOLVEMENT IN JEB2C, AND RP VARIANT SER-2834. 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., Darling J., RA Atherton D.J., Van Steensel M.A.M., Munro C.S., Smith F.J.D., McGrath J.A.; RT "An unusual N-terminal deletion of the laminin alpha3a isoform leads to the RT chronic granulation tissue disorder laryngo-onycho-cutaneous syndrome."; RL Hum. Mol. Genet. 12:2395-2409(2003). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2). RX PubMed=15044476; DOI=10.1074/jbc.m400670200; RA Kariya Y., Yasuda C., Nakashima Y., Ishida K., Tsubota Y., Miyazaki K.; RT "Characterization of laminin 5B and NH2-terminal proteolytic fragment of RT 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., Strausberg R.L., RA 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], AND VARIANT SER-2834. RX PubMed=16177791; DOI=10.1038/nature03983; RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J., RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.; RT "DNA sequence and analysis of human chromosome 18."; RL Nature 437:551-555(2005). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-2858 (ISOFORM 1), NUCLEOTIDE SEQUENCE RP [MRNA] OF 1528-2858 (ISOFORMS 1/2), AND INVOLVEMENT IN JEB2B. 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., Uitto J., RA Ortonne J.-P., Meneguzzi G.; RT "Cloning of the laminin alpha 3 chain gene (LAMA3) and identification of a RT homozygous deletion in a patient with Herlitz junctional epidermolysis RT bullosa."; RL Genomics 30:273-280(1995). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1528-3333 (ISOFORMS 1/2). RA Aberdam D., Vidal F., Baudoin C., Miquel C., Ortonne J.-P., 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). RC TISSUE=Keratinocyte; RX PubMed=8077230; DOI=10.1016/s0021-9258(17)31713-1; 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 JEB2B, AND VARIANT JEB2B 2270-ARG--GLN-3333 DEL. RX PubMed=8530087; DOI=10.1006/geno.1995.1246; RA McGrath J.A., Kivirikko S., Ciatti S., Moss C., Dunnill G.S., Eady R.A., RA 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 exclusion in RT a fetus at risk."; RL Genomics 29:282-284(1995). RN [9] RP INVOLVEMENT IN JEB2B, AND VARIANT JEB2B 2270-ARG--GLN-3333 DEL. 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 INVOLVEMENT IN JEB2A, AND INVOLVEMENT IN JEB2B. RX PubMed=11810295; DOI=10.1007/s00439-001-0630-1; RA Nakano A., Chao S.C., Pulkkinen L., Murrell D., Bruckner-Tuderman L., RA Pfendner E., Uitto J.; RT "Laminin 5 mutations in junctional epidermolysis bullosa: molecular basis RT of Herlitz vs. non-Herlitz phenotypes."; RL Hum. Genet. 110:41-51(2002). RN [11] 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., Buerckstuemmer T., RA 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 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 -!- 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=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 epithelia CC and in other specialized tissues with prominent secretory or protective CC functions. Epithelial basement membrane, and epithelial cell tongue CC that migrates into a wound bed. A differential and focal expression of CC the subunit alpha-3 is 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 with CC other laminin chains to form a coiled coil structure. CC -!- DOMAIN: Domain G is globular. CC -!- DISEASE: Epidermolysis bullosa, junctional 2A, intermediate (JEB2A) CC [MIM:619783]: A form of epidermolysis bullosa, a genodermatosis CC characterized by recurrent blistering, fragility of the skin and CC mucosal epithelia, and erosions caused by minor mechanical trauma. CC JEB2A is an autosomal recessive, intermediate form in which blistering CC lesions occur between the epidermis and the dermis at the lamina lucida CC level of the basement membrane zone. In intermediate forms of CC junctional epidermolysis bullosa, blistering does not lead to the CC formation of chronic granulation tissue and does not affect the CC lifespan of affected individuals. Nail dystrophy and dental enamel CC defects are present. Scarring or non-scarring alopecia and diffuse hair CC loss may occur. {ECO:0000269|PubMed:11810295}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Epidermolysis bullosa, junctional 2B, severe (JEB2B) CC [MIM:619784]: A form of epidermolysis bullosa, a genodermatosis CC characterized by recurrent blistering, fragility of the skin and CC mucosal epithelia, and erosions caused by minor mechanical trauma. CC JEB2B is an autosomal recessive form in which blistering lesions occur CC between the epidermis and the dermis at the lamina lucida level of the CC basement membrane zone. It belongs to the severe spectrum of junctional CC epidermolysis bullosa (previously known as generalized severe or CC Herlitz type), characterized by onset of blistering over large regions CC of the body at birth or in early infancy. Blistering also affects the CC mucous membranes, such as the moist lining of the mouth and digestive CC tract, which can make it difficult to eat and digest food. The CC extensive blistering leads to scarring and the formation of red, bumpy CC patches called granulation tissue. Other complications can include CC fusion of the fingers and toes, abnormalities of the fingernails and CC toenails, joint deformities, dental enamel defects, and alopecia. CC Severe, junctional forms are associated with death in the first 6 to 24 CC months of life. {ECO:0000269|PubMed:7633458, CC ECO:0000269|PubMed:8530087, ECO:0000269|PubMed:8586427}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Epidermolysis bullosa, junctional 2C, laryngoonychocutaneous CC (JEB2C) [MIM:245660]: A form of epidermolysis bullosa, a genodermatosis CC characterized by recurrent blistering, fragility of the skin and CC mucosal epithelia, and erosions caused by minor mechanical trauma. CC JEB2C is an autosomal recessive, severe form in which blistering CC lesions occur between the epidermis and the dermis at the lamina lucida CC level of the basement membrane zone. JEB2C manifestations appear in CC early infancy and include hoarse cry, skin ulceration, nail dystrophy CC with recurrent loss of toenails and fingernails, and conjunctival CC scarring. Some patients have amelogenesis imperfecta. Death in CC childhood is common. {ECO:0000269|PubMed:12915477}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. [Q16787-1] DR RefSeq; NP_001121189.2; NM_001127717.2. [Q16787-3] DR RefSeq; NP_001121190.2; NM_001127718.2. [Q16787-4] DR RefSeq; NP_001289925.1; NM_001302996.1. DR RefSeq; NP_937762.2; NM_198129.2. [Q16787-2] DR SMR; Q16787; -. DR BioGRID; 110103; 57. 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; 38. DR MINT; Q16787; -. DR STRING; 9606.ENSP00000324532; -. DR ChEMBL; CHEMBL2364187; -. DR DrugBank; DB06245; Lanoteplase. DR GlyCosmos; Q16787; 6 sites, 1 glycan. DR GlyGen; Q16787; 13 sites, 8 N-linked glycans (4 sites), 3 O-linked glycans (6 sites). DR iPTMnet; Q16787; -. DR PhosphoSitePlus; Q16787; -. DR SwissPalm; Q16787; -. DR BioMuta; LAMA3; -. DR DMDM; 215274012; -. DR jPOST; Q16787; -. DR MassIVE; Q16787; -. DR PaxDb; 9606-ENSP00000324532; -. DR PeptideAtlas; Q16787; -. DR ProteomicsDB; 2880; -. DR ProteomicsDB; 61068; -. [Q16787-2] DR ProteomicsDB; 61069; -. [Q16787-1] DR ProteomicsDB; 61070; -. [Q16787-3] DR Pumba; Q16787; -. DR Antibodypedia; 1948; 193 antibodies from 29 providers. DR DNASU; 3909; -. DR Ensembl; ENST00000269217.11; ENSP00000269217.5; ENSG00000053747.17. [Q16787-1] DR Ensembl; ENST00000313654.14; ENSP00000324532.8; ENSG00000053747.17. [Q16787-2] DR Ensembl; ENST00000399516.7; ENSP00000382432.2; ENSG00000053747.17. [Q16787-3] DR Ensembl; ENST00000587184.5; ENSP00000466557.1; ENSG00000053747.17. [Q16787-4] DR GeneID; 3909; -. DR KEGG; hsa:3909; -. DR MANE-Select; ENST00000313654.14; ENSP00000324532.8; NM_198129.4; NP_937762.2. DR UCSC; uc002kuq.4; human. [Q16787-2] DR AGR; HGNC:6483; -. DR CTD; 3909; -. DR DisGeNET; 3909; -. DR GeneCards; LAMA3; -. DR GeneReviews; LAMA3; -. DR HGNC; HGNC:6483; LAMA3. DR HPA; ENSG00000053747; Low tissue specificity. DR MalaCards; LAMA3; -. DR MIM; 245660; phenotype. DR MIM; 600805; gene. DR MIM; 619783; phenotype. DR MIM; 619784; phenotype. DR neXtProt; NX_Q16787; -. DR OpenTargets; ENSG00000053747; -. DR Orphanet; 79402; Intermediate generalized junctional epidermolysis bullosa. DR Orphanet; 2407; Laryngo-onycho-cutaneous syndrome. DR Orphanet; 79404; Severe generalized junctional epidermolysis bullosa. DR PharmGKB; PA30272; -. DR VEuPathDB; HostDB:ENSG00000053747; -. DR eggNOG; KOG1836; Eukaryota. DR GeneTree; ENSGT00940000155638; -. DR InParanoid; Q16787; -. DR OrthoDB; 90222at2759; -. DR PhylomeDB; Q16787; -. DR TreeFam; TF335359; -. DR PathwayCommons; Q16787; -. 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 SignaLink; Q16787; -. DR SIGNOR; Q16787; -. DR BioGRID-ORCS; 3909; 22 hits in 1152 CRISPR screens. DR ChiTaRS; LAMA3; human. DR GeneWiki; Laminin,_alpha_3; -. DR GenomeRNAi; 3909; -. DR Pharos; Q16787; Tbio. DR PRO; PR:Q16787; -. DR Proteomes; UP000005640; Chromosome 18. DR RNAct; Q16787; protein. DR Bgee; ENSG00000053747; Expressed in right lung and 157 other cell types or tissues. DR ExpressionAtlas; Q16787; baseline and differential. DR GO; GO:0005912; C:adherens junction; IEA:Ensembl. 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:0030056; C:hemidesmosome; IEA:Ensembl. DR GO; GO:0005608; C:laminin-3 complex; IEA:Ensembl. DR GO; GO:0005610; C:laminin-5 complex; IEA:Ensembl. DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc. DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl. DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB. DR GO; GO:0008544; P:epidermis development; TAS:ProtInc. DR GO; GO:0031581; P:hemidesmosome assembly; IEA:Ensembl. 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; 14. DR CDD; cd00110; LamG; 5. DR FunFam; 2.10.25.10:FF:000011; Cadherin EGF LAG seven-pass G-type receptor; 1. DR FunFam; 2.10.25.10:FF:000106; Heparan sulfate proteoglycan 2; 1. DR FunFam; 2.10.25.10:FF:000083; Laminin subunit alpha; 2. DR FunFam; 2.10.25.10:FF:000090; laminin subunit alpha; 1. DR FunFam; 2.10.25.10:FF:000069; Laminin subunit alpha 1; 1. DR FunFam; 2.10.25.10:FF:000033; Laminin subunit alpha 2; 1. DR FunFam; 2.10.25.10:FF:000034; Laminin subunit alpha 3; 1. DR FunFam; 2.10.25.10:FF:000084; Laminin subunit alpha 3; 1. DR FunFam; 2.10.25.10:FF:000390; Laminin subunit alpha 3; 1. DR FunFam; 2.10.25.10:FF:000460; Laminin subunit alpha 3; 1. DR FunFam; 2.60.120.200:FF:000056; Laminin subunit alpha 3; 1. DR FunFam; 2.60.120.200:FF:000092; Laminin subunit alpha 3; 1. DR FunFam; 2.60.120.200:FF:000093; Laminin subunit alpha 3; 1. DR FunFam; 2.60.120.200:FF:000102; Laminin subunit alpha 3; 1. DR FunFam; 2.60.120.200:FF:000109; Laminin subunit alpha 3; 1. DR FunFam; 2.10.25.10:FF:000209; Laminin subunit alpha 5; 1. DR FunFam; 2.60.120.260:FF:000022; Laminin subunit alpha 5; 1. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 2.60.120.200; -; 5. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 2.10.25.10; Laminin; 12. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR050440; Laminin/Netrin_ECM. 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 PANTHER; PTHR10574:SF365; NETRIN-A-RELATED; 1. DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1. 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 PRINTS; PR00011; EGFLAMININ. 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; Concanavalin A-like lectins/glucanases; 5. DR SUPFAM; SSF57196; EGF/Laminin; 12. 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 Disease variant; Disulfide bond; Epidermolysis bullosa; KW Extracellular matrix; Glycoprotein; Laminin EGF-like domain; KW Proteomics identification; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..35 FT /evidence="ECO:0000255" FT CHAIN 36..3333 FT /note="Laminin subunit alpha-3" FT /id="PRO_0000017058" FT DOMAIN 43..298 FT /note="Laminin N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466" FT DOMAIN 299..355 FT /note="Laminin EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 356..425 FT /note="Laminin EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 426..469 FT /note="Laminin EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 491..535 FT /note="Laminin EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 536..588 FT /note="Laminin EGF-like 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 590..630 FT /note="Laminin EGF-like 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 631..683 FT /note="Laminin EGF-like 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 684..728 FT /note="Laminin EGF-like 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1266..1311 FT /note="Laminin EGF-like 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1312..1355 FT /note="Laminin EGF-like 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1356..1404 FT /note="Laminin EGF-like 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1405..1455 FT /note="Laminin EGF-like 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1476..1653 FT /note="Laminin IV type A" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458" FT DOMAIN 1687..1733 FT /note="Laminin EGF-like 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1734..1786 FT /note="Laminin EGF-like 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1787..1821 FT /note="Laminin EGF-like 15; truncated" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 2390..2591 FT /note="Laminin G-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 2598..2760 FT /note="Laminin G-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 2767..2927 FT /note="Laminin G-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 2986..3150 FT /note="Laminin G-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 3157..3330 FT /note="Laminin G-like 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT REGION 298..728 FT /note="Domain V" FT REGION 796..1265 FT /note="Domain IV 1 (domain IV B)" FT REGION 1266..1465 FT /note="Domain III B" FT REGION 1654..1821 FT /note="Domain III A" FT REGION 1822..2389 FT /note="Domain II and I" FT COILED 1852..1941 FT /evidence="ECO:0000255" FT COILED 1987..2169 FT /evidence="ECO:0000255" FT COILED 2322..2388 FT /evidence="ECO:0000255" FT MOTIF 2278..2280 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT CARBOHYD 142 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 242 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2365 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2502 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2584 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 299..308 FT /evidence="ECO:0000250" FT DISULFID 301..319 FT /evidence="ECO:0000250" FT DISULFID 321..330 FT /evidence="ECO:0000250" FT DISULFID 333..353 FT /evidence="ECO:0000250" FT DISULFID 356..365 FT /evidence="ECO:0000250" FT DISULFID 358..390 FT /evidence="ECO:0000250" FT DISULFID 393..402 FT /evidence="ECO:0000250" FT DISULFID 405..423 FT /evidence="ECO:0000250" FT DISULFID 426..436 FT /evidence="ECO:0000250" FT DISULFID 428..443 FT /evidence="ECO:0000250" FT DISULFID 445..454 FT /evidence="ECO:0000250" FT DISULFID 457..467 FT /evidence="ECO:0000250" FT DISULFID 491..503 FT /evidence="ECO:0000250" FT DISULFID 493..509 FT /evidence="ECO:0000250" FT DISULFID 511..520 FT /evidence="ECO:0000250" FT DISULFID 523..533 FT /evidence="ECO:0000250" FT DISULFID 536..548 FT /evidence="ECO:0000250" FT DISULFID 538..555 FT /evidence="ECO:0000250" FT DISULFID 557..566 FT /evidence="ECO:0000250" FT DISULFID 569..586 FT /evidence="ECO:0000250" FT DISULFID 601..610 FT /evidence="ECO:0000250" FT DISULFID 613..628 FT /evidence="ECO:0000250" FT DISULFID 631..645 FT /evidence="ECO:0000250" FT DISULFID 633..652 FT /evidence="ECO:0000250" FT DISULFID 654..663 FT /evidence="ECO:0000250" FT DISULFID 666..681 FT /evidence="ECO:0000250" FT DISULFID 684..696 FT /evidence="ECO:0000250" FT DISULFID 686..703 FT /evidence="ECO:0000250" FT DISULFID 705..714 FT /evidence="ECO:0000250" FT DISULFID 1266..1278 FT /evidence="ECO:0000250" FT DISULFID 1268..1285 FT /evidence="ECO:0000250" FT DISULFID 1287..1296 FT /evidence="ECO:0000250" FT DISULFID 1299..1309 FT /evidence="ECO:0000250" FT DISULFID 1312..1319 FT /evidence="ECO:0000250" FT DISULFID 1314..1326 FT /evidence="ECO:0000250" FT DISULFID 1328..1337 FT /evidence="ECO:0000250" FT DISULFID 1340..1353 FT /evidence="ECO:0000250" FT DISULFID 1356..1371 FT /evidence="ECO:0000250" FT DISULFID 1358..1378 FT /evidence="ECO:0000250" FT DISULFID 1380..1389 FT /evidence="ECO:0000250" FT DISULFID 1392..1402 FT /evidence="ECO:0000250" FT DISULFID 1405..1417 FT /evidence="ECO:0000250" FT DISULFID 1407..1424 FT /evidence="ECO:0000250" FT DISULFID 1426..1435 FT /evidence="ECO:0000250" FT DISULFID 1438..1453 FT /evidence="ECO:0000250" FT DISULFID 1687..1696 FT /evidence="ECO:0000250" FT DISULFID 1689..1703 FT /evidence="ECO:0000250" FT DISULFID 1706..1715 FT /evidence="ECO:0000250" FT DISULFID 1718..1731 FT /evidence="ECO:0000250" FT DISULFID 1734..1746 FT /evidence="ECO:0000250" FT DISULFID 1736..1755 FT /evidence="ECO:0000250" FT DISULFID 1757..1766 FT /evidence="ECO:0000250" FT DISULFID 1769..1784 FT /evidence="ECO:0000250" FT DISULFID 1822 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 1825 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 2561..2591 FT /evidence="ECO:0000250" FT DISULFID 2737..2760 FT /evidence="ECO:0000250" FT DISULFID 2895..2927 FT /evidence="ECO:0000250" FT DISULFID 3127..3150 FT /evidence="ECO:0000250" FT DISULFID 3302..3330 FT /evidence="ECO:0000250" FT VAR_SEQ 1..1620 FT /note="Missing (in isoform 1)" FT /evidence="ECO:0000303|PubMed:8586427" FT /id="VSP_035738" FT VAR_SEQ 1..1609 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:12915477" FT /id="VSP_047079" FT VAR_SEQ 1610..1665 FT /note="LSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVEICACPPAYA FT GDSC -> MPPAVRRSACSMGWLWIFGAALGQCLGYSSQQQRVPFLQPPGQSQLQASYV FT EFRPS (in isoform 4)" FT /evidence="ECO:0000303|PubMed:12915477" FT /id="VSP_047080" FT VAR_SEQ 1621..1665 FT /note="LYFTETQRLTLSEVGLEEASDTGSGRIALAVEICACPPAYAGDSC -> MPP FT AVRRSACSMGWLWIFGAALGQCLGYSSQQQRVPFLQPPGQSQLQASYVEFRPS (in FT isoform 1)" FT /evidence="ECO:0000303|PubMed:8586427" FT /id="VSP_035739" FT VAR_SEQ 1946..2002 FT /note="ILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKR FT ESQLL -> M (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:12915477" FT /id="VSP_043487" FT VARIANT 796 FT /note="T -> N (in dbSNP:rs17187262)" FT /id="VAR_050078" FT VARIANT 1206 FT /note="V -> A (in dbSNP:rs12457323)" FT /id="VAR_050079" FT VARIANT 1208 FT /note="P -> T (in dbSNP:rs17202961)" FT /id="VAR_050080" FT VARIANT 1774 FT /note="F -> L (in dbSNP:rs958631)" FT /id="VAR_059444" FT VARIANT 2270..3333 FT /note="Missing (in JEB2B)" FT /evidence="ECO:0000269|PubMed:7633458, FT ECO:0000269|PubMed:8530087" FT /id="VAR_086401" FT VARIANT 2702 FT /note="T -> A (in dbSNP:rs9952370)" FT /id="VAR_047374" FT VARIANT 2815 FT /note="N -> K (in dbSNP:rs1154232)" FT /id="VAR_047375" FT VARIANT 2834 FT /note="G -> S (in dbSNP:rs1154233)" FT /evidence="ECO:0000269|PubMed:12915477, FT ECO:0000269|PubMed:15044476, ECO:0000269|PubMed:16177791, FT ECO:0000269|PubMed:8077230, ECO:0000269|Ref.6" FT /id="VAR_059445" FT CONFLICT 1544 FT /note="G -> A (in Ref. 5; CAA59429 and 6; CAA59325)" FT /evidence="ECO:0000305" FT CONFLICT 1743..1745 FT /note="ATG -> GMC (in Ref. 5; CAA59428/CAA59429)" FT /evidence="ECO:0000305" FT CONFLICT 2101 FT /note="M -> K (in Ref. 5; CAA59428/CAA59429)" FT /evidence="ECO:0000305" FT CONFLICT 2374 FT /note="R -> L (in Ref. 5; CAA59428/CAA59429)" FT /evidence="ECO:0000305" FT CONFLICT 2589 FT /note="E -> Q (in Ref. 5; CAA59428/CAA59429)" FT /evidence="ECO:0000305" FT CONFLICT 2672 FT /note="D -> A (in Ref. 5; CAA59428/CAA59429)" FT /evidence="ECO:0000305" FT CONFLICT 2804 FT /note="G -> A (in Ref. 5; CAA59428/CAA59429)" FT /evidence="ECO:0000305" SQ SEQUENCE 3333 AA; 366619 MW; 6F99AF4D4B99FCB0 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 DSGGPIFKSP 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 //