ID   LAMC2_HUMAN             Reviewed;        1193 AA.
AC   Q13753; Q02536; Q02537; Q13752; Q14941; Q14DF7; Q2M1N2; Q5VYE8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   27-MAR-2024, entry version 219.
DE   RecName: Full=Laminin subunit gamma-2;
DE   AltName: Full=Cell-scattering factor 140 kDa subunit;
DE            Short=CSF 140 kDa subunit;
DE   AltName: Full=Epiligrin subunit gamma;
DE   AltName: Full=Kalinin subunit gamma;
DE   AltName: Full=Kalinin/nicein/epiligrin 100 kDa subunit;
DE   AltName: Full=Ladsin 140 kDa subunit;
DE   AltName: Full=Laminin B2t chain;
DE   AltName: Full=Laminin-5 subunit gamma;
DE   AltName: Full=Large adhesive scatter factor 140 kDa subunit;
DE   AltName: Full=Nicein subunit gamma;
DE   Flags: Precursor;
GN   Name=LAMC2; Synonyms=LAMB2T, LAMNB2;
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], AND ALTERNATIVE SPLICING.
RC   TISSUE=Fibrosarcoma;
RX   PubMed=1383240; DOI=10.1083/jcb.119.3.679;
RA   Kallunki P., Sainio K., Eddy R., Byers M., Kallunki T., Sariola H.,
RA   Beck K., Hirvonen H., Shows T.B., Tryggvason K.;
RT   "A truncated laminin chain homologous to the B2 chain: structure, spatial
RT   expression, and chromosomal assignment.";
RL   J. Cell Biol. 119:679-693(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1090-1114.
RC   TISSUE=Epidermis, and Keratinocyte;
RX   PubMed=8306988; DOI=10.1111/j.1432-1033.1994.tb19932.x;
RA   Vailly J., Verrando P., Champliaud M.-F., Gerecke D., Wagman D.W.,
RA   Baudoin C., Aberdam D., Burgeson R., Bauer E., Ortonne J.-P.;
RT   "The 100-kDa chain of nicein/kalinin is a laminin B2 chain variant.";
RL   Eur. J. Biochem. 219:209-218(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Placenta;
RX   PubMed=8786121; DOI=10.1006/geno.1996.0076;
RA   Airenne T., Haakana H., Sainio K., Kallunki T., Kallunki P., Sariola H.,
RA   Tryggvason K.;
RT   "Structure of the human laminin gamma 2 chain gene (LAMC2): alternative
RT   splicing with different tissue distribution of two transcripts.";
RL   Genomics 32:54-64(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC   TISSUE=Cerebellum;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE OF 435-449, FUNCTION, AND HEPARIN-BINDING.
RX   PubMed=8265624; DOI=10.1073/pnas.90.24.11767;
RA   Miyazaki K., Kikkawa Y., Nakamura A., Yasumitsu H., Umeda M.;
RT   "A large cell-adhesive scatter factor secreted by human gastric carcinoma
RT   cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:11767-11771(1993).
RN   [8]
RP   INVOLVEMENT IN JEB3B.
RX   PubMed=8012393; DOI=10.1038/ng0394-293;
RA   Pulkkinen L., Christiano A.M., Airenne T., Haakana H., Tryggvason K.,
RA   Uitto J.;
RT   "Mutations in the gamma 2 chain gene (LAMC2) of kalinin/laminin 5 in the
RT   junctional forms of epidermolysis bullosa.";
RL   Nat. Genet. 6:293-297(1994).
RN   [9]
RP   INVOLVEMENT IN JEB3A, AND INVOLVEMENT IN JEB3B.
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   [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., 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).
RN   [11]
RP   GLYCOSYLATION.
RX   PubMed=32337544; DOI=10.1093/glycob/cwaa039;
RA   Toledo A.G., Pihl J., Spliid C.B., Persson A., Nilsson J., Pereira M.A.,
RA   Gustavsson T., Choudhary S., Oo H.Z., Black P.C., Daugaard M., Esko J.D.,
RA   Larson G., Salanti A., Clausen T.M.;
RT   "An affinity chromatography and glycoproteomics workflow to profile the
RT   chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in
RT   the placenta and in cancer.";
RL   Glycobiology 30:989-1002(2020).
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. Ladsin exerts cell-scattering activity
CC       toward a wide variety of cells, including epithelial, endothelial, and
CC       fibroblastic cells. {ECO:0000269|PubMed:8265624}.
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. Gamma-2 is a
CC       subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane. Note=Major component.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q13753-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q13753-2; Sequence=VSP_003040;
CC   -!- TISSUE SPECIFICITY: The large variant is expressed only in specific
CC       epithelial cells of embryonic and neonatal tissues. In 17-week old
CC       embryo the small variant is found in cerebral cortex, lung, and distal
CC       tubes of kidney, but not in epithelia except for distal tubuli.
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 IV is globular.
CC   -!- PTM: O-glycosylated; contains chondroitin sulfate (CS). CS attachment
CC       is on either Ser-803 or Ser-805. {ECO:0000269|PubMed:32337544}.
CC   -!- DISEASE: Epidermolysis bullosa, junctional 3A, intermediate (JEB3A)
CC       [MIM:619785]: 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       JEB3A 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 3B, severe (JEB3B)
CC       [MIM:619786]: 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       JEB3B 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:11810295,
CC       ECO:0000269|PubMed:8012393}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: Binds heparin. {ECO:0000250}.
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DR   EMBL; Z15008; CAA78728.1; -; mRNA.
DR   EMBL; Z15009; CAA78729.1; -; mRNA.
DR   EMBL; X73902; CAA52108.1; -; mRNA.
DR   EMBL; U31201; AAC50457.1; -; Genomic_DNA.
DR   EMBL; U31178; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31179; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31180; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31181; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31182; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31183; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31184; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31186; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31187; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31188; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31189; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31190; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31191; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31192; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31193; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31194; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31195; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31196; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31197; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31198; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31199; AAC50457.1; JOINED; Genomic_DNA.
DR   EMBL; U31200; AAC50456.1; -; Genomic_DNA.
DR   EMBL; U31178; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31179; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31180; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31181; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31182; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31183; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31184; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31186; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31187; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31188; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31189; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31190; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31191; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31192; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31193; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31194; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31195; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31196; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31197; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; U31198; AAC50456.1; JOINED; Genomic_DNA.
DR   EMBL; AL354953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471067; EAW91146.1; -; Genomic_DNA.
DR   EMBL; BC112286; AAI12287.1; -; mRNA.
DR   EMBL; BC113378; AAI13379.1; -; mRNA.
DR   CCDS; CCDS1352.1; -. [Q13753-1]
DR   CCDS; CCDS44285.1; -. [Q13753-2]
DR   PIR; A44018; A44018.
DR   RefSeq; NP_005553.2; NM_005562.2. [Q13753-1]
DR   RefSeq; NP_061486.2; NM_018891.2. [Q13753-2]
DR   AlphaFoldDB; Q13753; -.
DR   SMR; Q13753; -.
DR   BioGRID; 110112; 27.
DR   ComplexPortal; CPX-1774; Laminin-332 complex variant A.
DR   ComplexPortal; CPX-1783; Laminin-522 complex.
DR   ComplexPortal; CPX-3165; Laminin-332 complex variant B.
DR   IntAct; Q13753; 6.
DR   MINT; Q13753; -.
DR   STRING; 9606.ENSP00000264144; -.
DR   ChEMBL; CHEMBL2364187; -.
DR   Allergome; 8331; Hom s Laminin gamma_2.
DR   GlyConnect; 1445; 2 N-Linked glycans (2 sites).
DR   GlyCosmos; Q13753; 4 sites, 2 glycans.
DR   GlyGen; Q13753; 12 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (6 sites).
DR   iPTMnet; Q13753; -.
DR   MetOSite; Q13753; -.
DR   PhosphoSitePlus; Q13753; -.
DR   SwissPalm; Q13753; -.
DR   BioMuta; LAMC2; -.
DR   DMDM; 90185107; -.
DR   EPD; Q13753; -.
DR   jPOST; Q13753; -.
DR   MassIVE; Q13753; -.
DR   MaxQB; Q13753; -.
DR   PaxDb; 9606-ENSP00000264144; -.
DR   PeptideAtlas; Q13753; -.
DR   ProteomicsDB; 59675; -. [Q13753-1]
DR   ProteomicsDB; 59676; -. [Q13753-2]
DR   Pumba; Q13753; -.
DR   Antibodypedia; 3791; 320 antibodies from 32 providers.
DR   DNASU; 3918; -.
DR   Ensembl; ENST00000264144.5; ENSP00000264144.4; ENSG00000058085.15. [Q13753-1]
DR   Ensembl; ENST00000493293.5; ENSP00000432063.1; ENSG00000058085.15. [Q13753-2]
DR   GeneID; 3918; -.
DR   KEGG; hsa:3918; -.
DR   MANE-Select; ENST00000264144.5; ENSP00000264144.4; NM_005562.3; NP_005553.2.
DR   UCSC; uc001gpz.5; human. [Q13753-1]
DR   AGR; HGNC:6493; -.
DR   CTD; 3918; -.
DR   DisGeNET; 3918; -.
DR   GeneCards; LAMC2; -.
DR   GeneReviews; LAMC2; -.
DR   HGNC; HGNC:6493; LAMC2.
DR   HPA; ENSG00000058085; Tissue enhanced (urinary).
DR   MalaCards; LAMC2; -.
DR   MIM; 150292; gene.
DR   MIM; 619785; phenotype.
DR   MIM; 619786; phenotype.
DR   neXtProt; NX_Q13753; -.
DR   OpenTargets; ENSG00000058085; -.
DR   Orphanet; 79402; Intermediate generalized junctional epidermolysis bullosa.
DR   Orphanet; 79404; Severe generalized junctional epidermolysis bullosa.
DR   PharmGKB; PA30281; -.
DR   VEuPathDB; HostDB:ENSG00000058085; -.
DR   eggNOG; KOG1836; Eukaryota.
DR   GeneTree; ENSGT00940000160470; -.
DR   HOGENOM; CLU_002471_0_0_1; -.
DR   InParanoid; Q13753; -.
DR   OMA; ARWVQTC; -.
DR   OrthoDB; 90222at2759; -.
DR   PhylomeDB; Q13753; -.
DR   PathwayCommons; Q13753; -.
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-446107; Type I hemidesmosome assembly.
DR   Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR   SignaLink; Q13753; -.
DR   SIGNOR; Q13753; -.
DR   BioGRID-ORCS; 3918; 11 hits in 1146 CRISPR screens.
DR   ChiTaRS; LAMC2; human.
DR   GeneWiki; Laminin,_gamma_2; -.
DR   GenomeRNAi; 3918; -.
DR   Pharos; Q13753; Tbio.
DR   PRO; PR:Q13753; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q13753; Protein.
DR   Bgee; ENSG00000058085; Expressed in islet of Langerhans and 143 other cell types or tissues.
DR   GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005607; C:laminin-2 complex; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:BHF-UCL.
DR   CDD; cd00055; EGF_Lam; 6.
DR   Gene3D; 2.10.25.10; Laminin; 5.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10574:SF313; LAMININ SUBUNIT GAMMA-2; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 7.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00180; EGF_Lam; 7.
DR   SMART; SM00281; LamB; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 5.
DR   PROSITE; PS00022; EGF_1; 4.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 6.
DR   PROSITE; PS50027; EGF_LAM_2; 6.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   Genevisible; Q13753; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Basement membrane; Cell adhesion; Coiled coil;
KW   Direct protein sequencing; Disulfide bond; Epidermolysis bullosa;
KW   Extracellular matrix; Glycoprotein; Heparin-binding;
KW   Laminin EGF-like domain; Proteoglycan; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..1193
FT                   /note="Laminin subunit gamma-2"
FT                   /id="PRO_0000017077"
FT   DOMAIN          28..83
FT                   /note="Laminin EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          84..130
FT                   /note="Laminin EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          139..186
FT                   /note="Laminin EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          187..196
FT                   /note="Laminin EGF-like 4; first part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          213..381
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT   DOMAIN          382..415
FT                   /note="Laminin EGF-like 4; second part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          416..461
FT                   /note="Laminin EGF-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          462..516
FT                   /note="Laminin EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          517..572
FT                   /note="Laminin EGF-like 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          573..602
FT                   /note="Laminin EGF-like 8; truncated"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   REGION          603..1193
FT                   /note="Domain II and I"
FT   COILED          611..718
FT                   /evidence="ECO:0000255"
FT   COILED          811..1076
FT                   /evidence="ECO:0000255"
FT   COILED          1117..1193
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        803
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        805
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        942
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1033
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        30..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        56..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        68..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        84..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        86..102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        104..113
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        116..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        139..150
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        141..155
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        157..166
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        169..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        462..470
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        464..481
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        484..493
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        496..514
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        517..531
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        519..538
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        541..550
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        553..570
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        573..585
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        575..591
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        593..602
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        609
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        612
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        1184
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   VAR_SEQ         1110..1193
FT                   /note="DQPLSVDEEGLVLLEQKLSRAKTQINSQLRPMMSELEERARQQRGHLHLLET
FT                   SIDGILADVKNLENIRDNLPPGCYNTQALEQQ -> GM (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_003040"
FT   VARIANT         111
FT                   /note="A -> P (in dbSNP:rs12065473)"
FT                   /id="VAR_050081"
FT   VARIANT         115
FT                   /note="R -> Q (in dbSNP:rs17481405)"
FT                   /id="VAR_050082"
FT   VARIANT         124
FT                   /note="T -> M (in dbSNP:rs11586699)"
FT                   /id="VAR_050083"
FT   VARIANT         136
FT                   /note="D -> V (in dbSNP:rs12037099)"
FT                   /id="VAR_050084"
FT   VARIANT         247
FT                   /note="D -> E (in dbSNP:rs2296306)"
FT                   /id="VAR_022017"
FT   VARIANT         608
FT                   /note="S -> I (in dbSNP:rs4373715)"
FT                   /id="VAR_050085"
FT   VARIANT         733
FT                   /note="S -> T (in dbSNP:rs2296303)"
FT                   /id="VAR_020304"
FT   CONFLICT        12
FT                   /note="F -> L (in Ref. 2; CAA52108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        473
FT                   /note="M -> I (in Ref. 1; CAA78728/CAA78729)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        521
FT                   /note="N -> S (in Ref. 1; CAA78728/CAA78729)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        857
FT                   /note="R -> P (in Ref. 1; CAA78728/CAA78729)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        883
FT                   /note="S -> T (in Ref. 3; AAC50457/AAC50456)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1193 AA;  130976 MW;  0BBE1A56516C5C9A CRC64;
     MPALWLGCCL CFSLLLPAAR ATSRREVCDC NGKSRQCIFD RELHRQTGNG FRCLNCNDNT
     DGIHCEKCKN GFYRHRERDR CLPCNCNSKG SLSARCDNSG RCSCKPGVTG ARCDRCLPGF
     HMLTDAGCTQ DQRLLDSKCD CDPAGIAGPC DAGRCVCKPA VTGERCDRCR SGYYNLDGGN
     PEGCTQCFCY GHSASCRSSA EYSVHKITST FHQDVDGWKA VQRNGSPAKL QWSQRHQDVF
     SSAQRLDPVY FVAPAKFLGN QQVSYGQSLS FDYRVDRGGR HPSAHDVILE GAGLRITAPL
     MPLGKTLPCG LTKTYTFRLN EHPSNNWSPQ LSYFEYRRLL RNLTALRIRA TYGEYSTGYI
     DNVTLISARP VSGAPAPWVE QCICPVGYKG QFCQDCASGY KRDSARLGPF GTCIPCNCQG
     GGACDPDTGD CYSGDENPDI ECADCPIGFY NDPHDPRSCK PCPCHNGFSC SVMPETEEVV
     CNNCPPGVTG ARCELCADGY FGDPFGEHGP VRPCQPCQCN NNVDPSASGN CDRLTGRCLK
     CIHNTAGIYC DQCKAGYFGD PLAPNPADKC RACNCNPMGS EPVGCRSDGT CVCKPGFGGP
     NCEHGAFSCP ACYNQVKIQM DQFMQQLQRM EALISKAQGG DGVVPDTELE GRMQQAEQAL
     QDILRDAQIS EGASRSLGLQ LAKVRSQENS YQSRLDDLKM TVERVRALGS QYQNRVRDTH
     RLITQMQLSL AESEASLGNT NIPASDHYVG PNGFKSLAQE ATRLAESHVE SASNMEQLTR
     ETEDYSKQAL SLVRKALHEG VGSGSGSPDG AVVQGLVEKL EKTKSLAQQL TREATQAEIE
     ADRSYQHSLR LLDSVSRLQG VSDQSFQVEE AKRIKQKADS LSSLVTRHMD EFKRTQKNLG
     NWKEEAQQLL QNGKSGREKS DQLLSRANLA KSRAQEALSM GNATFYEVES ILKNLREFDL
     QVDNRKAEAE EAMKRLSYIS QKVSDASDKT QQAERALGSA AADAQRAKNG AGEALEISSE
     IEQEIGSLNL EANVTADGAL AMEKGLASLK SEMREVEGEL ERKELEFDTN MDAVQMVITE
     AQKVDTRAKN AGVTIQDTLN TLDGLLHLMD QPLSVDEEGL VLLEQKLSRA KTQINSQLRP
     MMSELEERAR QQRGHLHLLE TSIDGILADV KNLENIRDNL PPGCYNTQAL EQQ
//