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-MAR-2024, entry version 217.
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.
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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; 55.
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; 17.
DR   MINT; Q16787; -.
DR   STRING; 9606.ENSP00000324532; -.
DR   ChEMBL; CHEMBL2364187; -.
DR   DrugBank; DB06245; Lanoteplase.
DR   GlyCosmos; Q16787; 6 sites, 1 glycan.
DR   GlyGen; Q16787; 11 sites, 3 O-linked glycans (6 sites).
DR   iPTMnet; Q16787; -.
DR   PhosphoSitePlus; Q16787; -.
DR   SwissPalm; Q16787; -.
DR   BioMuta; LAMA3; -.
DR   DMDM; 215274012; -.
DR   EPD; Q16787; -.
DR   jPOST; Q16787; -.
DR   MassIVE; Q16787; -.
DR   MaxQB; 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; 258 antibodies from 30 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   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; 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.
DR   Genevisible; Q16787; HS.
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   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
//