LAMC2_HUMAN
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 03-AUG-2022, entry version 210.
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).
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 -!- 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; 21.
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; 4.
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 GlyGen; Q13753; 4 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q13753; -.
DR MetOSite; Q13753; -.
DR PhosphoSitePlus; Q13753; -.
DR BioMuta; LAMC2; -.
DR DMDM; 90185107; -.
DR EPD; Q13753; -.
DR jPOST; Q13753; -.
DR MassIVE; Q13753; -.
DR MaxQB; Q13753; -.
DR PaxDb; Q13753; -.
DR PeptideAtlas; Q13753; -.
DR PRIDE; Q13753; -.
DR ProteomicsDB; 59675; -. [Q13753-1]
DR ProteomicsDB; 59676; -. [Q13753-2]
DR Antibodypedia; 3791; 286 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 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; GRQKSDQ; -.
DR OrthoDB; 156553at2759; -.
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; 9 hits in 1066 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 142 other tissues.
DR Genevisible; Q13753; HS.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
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:0016020; C:membrane; 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:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
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 GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 6.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 7.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00180; EGF_Lam; 7.
DR SMART; SM00281; LamB; 1.
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.
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; Reference proteome; Repeat; 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 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
