MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Laminin subunit gamma-2; AltName: Full=Cell-scattering factor 140 kDa subunit; Short=CSF 140 kDa subunit; AltName: Full=Epiligrin subunit gamma; AltName: Full=Kalinin subunit gamma; AltName: Full=Kalinin/nicein/epiligrin 100 kDa subunit; AltName: Full=Ladsin 140 kDa subunit; AltName: Full=Laminin B2t chain; AltName: Full=Laminin-5 subunit gamma; AltName: Full=Large adhesive scatter factor 140 kDa subunit; AltName: Full=Nicein subunit gamma; Flags: Precursor; |
 |
|
| MyHits synonyms | LAMC2_HUMAN , Q13753 , Q02536 , Q02537 , Q13752 , Q14941 , Q14DF7 , Q2M1N2 , Q5VYE8 , 0BBE1A56516C5C9A |
 Legends: 1, N-linked (GlcNAc...). {ECO:0000255}; 2, DISULFID Interchain. {ECO:0000305}; 3, VARIANT A -> P (in dbSNP:rs12065473); 4, VARIANT R -> Q (in dbSNP:rs17481405); 5, VARIANT T -> M (in dbSNP:rs11586699); 6, VARIANT D -> V (in dbSNP:rs12037099); 7, VARIANT D -> E (in dbSNP:rs2296306); 8, VARIANT S -> I (in dbSNP:rs4373715); 9, VARIANT S -> T (in dbSNP:rs2296303); 10, CONFLICT F -> L (in Ref. 2; CAA52108). {ECO:0000305}; 11, CONFLICT M -> I (in Ref. 1; CAA78728/CAA78729). {ECO:0000305}; 12, CONFLICT N -> S (in Ref. 1; CAA78728/CAA78729). {ECO:0000305}; 13, CONFLICT R -> P (in Ref. 1; CAA78728/CAA78729). {ECO:0000305}; 14, CONFLICT S -> T (in Ref. 3; AAC50457/AAC50456). {ECO:0000305}; 15, SIGNAL {ECO:0000255}; 16, Laminin EGF-like 1. {ECO:0000255|PROSITE- ProRule:PRU00460}; 17, Laminin EGF-like 2. {ECO:0000255|PROSITE- ProRule:PRU00460}; 18, Laminin EGF-like 3. {ECO:0000255|PROSITE- ProRule:PRU00460}; 19, Laminin EGF-like 4; first part. {ECO:0000255|PROSITE-ProRule:PRU00460}; 20, Laminin IV type A. {ECO:0000255|PROSITE- ProRule:PRU00458}; 21, Laminin EGF-like 4; second part. {ECO:0000255|PROSITE-ProRule:PRU00460}; 22, Laminin EGF-like 5. {ECO:0000255|PROSITE- ProRule:PRU00460}; 23, Laminin EGF-like 6. {ECO:0000255|PROSITE- ProRule:PRU00460}; 24, Laminin EGF-like 7. {ECO:0000255|PROSITE- ProRule:PRU00460}; 25, Laminin EGF-like 8; truncated. {ECO:0000255|PROSITE-ProRule:PRU00460}; 26, COILED {ECO:0000255}; 27, VAR_SEQ DQPLSVDEEGLVLLEQKLSRAKTQINSQLRPMMSELEERAR QQRGHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALE QQ -> GM (in isoform Short). {ECO:0000303|PubMed:15489334}; 28, ismart:EGF_Lam [T]; 29, ismart:EGF [T]; 30, ipat:EGF_LAM_1 [T]; 31, iprf:EGF_LAM_2 [T]; 32, ismart:LamB [T]; 33, ipfam:Laminin_EGF [T]; 34, iprf:LAMININ_IVA [T]; 35, ipfam:Laminin_B [T].
| |
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 30-NOV-2016, entry version 174.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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,
RT spatial 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.,
RA Sariola H., Tryggvason K.;
RT "Structure of the human laminin gamma 2 chain gene (LAMC2):
RT alternative splicing with different tissue distribution of two
RT 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT carcinoma cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11767-11771(1993).
RN [8]
RP INVOLVEMENT IN H-JEB.
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
RT the junctional forms of epidermolysis bullosa.";
RL Nat. Genet. 6:293-297(1994).
RN [9]
RP INVOLVEMENT IN H-JEB.
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
RT basis 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin
CC is thought to mediate the attachment, migration and organization
CC of cells into tissues during embryonic development by interacting
CC with other extracellular matrix components. Ladsin exerts cell-
CC scattering activity toward a wide variety of cells, including
CC epithelial, endothelial, and fibroblastic cells.
CC {ECO:0000269|PubMed:8265624}.
CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC different polypeptide chains (alpha, beta, gamma), which are bound
CC to each other by disulfide bonds into a cross-shaped molecule
CC comprising one long and three short arms with globules at each
CC end. Gamma-2 is a subunit of laminin-5 (laminin-332 or
CC 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
CC specific epithelial cells of embryonic and neonatal tissues. In
CC 17-week old embryo the small variant is found in cerebral cortex,
CC lung, and distal tubes of kidney, but not in epithelia except for
CC distal tubuli.
CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact
CC with other laminin chains to form a coiled coil structure.
CC -!- DOMAIN: Domain IV is globular.
CC -!- DISEASE: Epidermolysis bullosa, junctional, Herlitz type (H-JEB)
CC [MIM:226700]: An infantile and lethal form of junctional
CC epidermolysis bullosa, a group of blistering skin diseases
CC characterized by tissue separation which occurs within the dermo-
CC epidermal basement In the Herlitz type, death occurs usually
CC within the first six months of life. Occasionally, children
CC survive to teens. It is marked by bullous lesions at birth and
CC extensive denudation of skin and mucous membranes that may be
CC hemorrhagic. {ECO:0000269|PubMed:11810295,
CC ECO:0000269|PubMed:8012393}. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Binds heparin. {ECO:0000250}.
CC -!- SIMILARITY: Contains 8 laminin EGF-like domains.
CC {ECO:0000255|PROSITE-ProRule:PRU00460}.
CC -!- SIMILARITY: Contains 1 laminin IV type A domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00458}.
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; CAH70980.1; -; 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 UniGene; Hs.591484; -.
DR ProteinModelPortal; Q13753; -.
DR SMR; Q13753; -.
DR BioGrid; 110112; 5.
DR IntAct; Q13753; 1.
DR MINT; MINT-4053464; -.
DR STRING; 9606.ENSP00000264144; -.
DR ChEMBL; CHEMBL2364187; -.
DR Allergome; 8331; Hom s Laminin gamma_2.
DR iPTMnet; Q13753; -.
DR PhosphoSitePlus; Q13753; -.
DR BioMuta; LAMC2; -.
DR DMDM; 90185107; -.
DR EPD; Q13753; -.
DR MaxQB; Q13753; -.
DR PaxDb; Q13753; -.
DR PeptideAtlas; Q13753; -.
DR PRIDE; Q13753; -.
DR Ensembl; ENST00000264144; ENSP00000264144; ENSG00000058085. [Q13753-1]
DR Ensembl; ENST00000493293; ENSP00000432063; ENSG00000058085. [Q13753-2]
DR GeneID; 3918; -.
DR KEGG; hsa:3918; -.
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; CAB004257; -.
DR HPA; HPA024638; -.
DR MalaCards; LAMC2; -.
DR MIM; 150292; gene.
DR MIM; 226700; phenotype.
DR neXtProt; NX_Q13753; -.
DR OpenTargets; ENSG00000058085; -.
DR Orphanet; 79402; Generalized junctional epidermolysis bullosa, non-Herlitz type.
DR Orphanet; 79405; Junctional epidermolysis bullosa inversa.
DR Orphanet; 79404; Junctional epidermolysis bullosa, Herlitz type.
DR PharmGKB; PA30281; -.
DR eggNOG; ENOG410IP6C; Eukaryota.
DR eggNOG; ENOG4110QI9; LUCA.
DR GeneTree; ENSGT00780000121851; -.
DR HOGENOM; HOG000019301; -.
DR HOVERGEN; HBG062127; -.
DR InParanoid; Q13753; -.
DR KO; K06246; -.
DR OMA; TEEVVCN; -.
DR OrthoDB; EOG091G005L; -.
DR PhylomeDB; Q13753; -.
DR BioCyc; ZFISH:ENSG00000058085-MONOMER; -.
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 SIGNOR; Q13753; -.
DR ChiTaRS; LAMC2; human.
DR GeneWiki; Laminin,_gamma_2; -.
DR GenomeRNAi; 3918; -.
DR PMAP-CutDB; Q13753; -.
DR PRO; PR:Q13753; -.
DR Proteomes; UP000005640; Chromosome 1.
DR Bgee; ENSG00000058085; -.
DR CleanEx; HS_LAMC2; -.
DR Genevisible; Q13753; HS.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR GO; GO:0031581; P:hemidesmosome assembly; TAS:Reactome.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002049; Laminin_EGF.
DR InterPro; IPR000034; Laminin_IV.
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 Complete proteome; Direct protein sequencing; Disulfide bond;
KW Epidermolysis bullosa; Extracellular matrix; Glycoprotein;
KW Heparin-binding; Laminin EGF-like domain; Polymorphism;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1 21 {ECO:0000255}.
FT CHAIN 22 1193 Laminin subunit gamma-2.
FT /FTId=PRO_0000017077.
FT DOMAIN 28 83 Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00460}.
FT DOMAIN 84 130 Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00460}.
FT DOMAIN 139 186 Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00460}.
FT DOMAIN 187 196 Laminin EGF-like 4; first part.
FT {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DOMAIN 213 381 Laminin IV type A. {ECO:0000255|PROSITE-
FT ProRule:PRU00458}.
FT DOMAIN 382 415 Laminin EGF-like 4; second part.
FT {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DOMAIN 416 461 Laminin EGF-like 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00460}.
FT DOMAIN 462 516 Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT ProRule:PRU00460}.
FT DOMAIN 517 572 Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT ProRule:PRU00460}.
FT DOMAIN 573 602 Laminin EGF-like 8; truncated.
FT {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT REGION 603 1193 Domain II and I.
FT COILED 611 718 {ECO:0000255}.
FT COILED 811 1076 {ECO:0000255}.
FT COILED 1117 1193 {ECO:0000255}.
FT CARBOHYD 342 342 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 362 362 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 942 942 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 1033 1033 N-linked (GlcNAc...). {ECO:0000255}.
FT DISULFID 28 37 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 30 53 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 56 65 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 68 81 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 84 96 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 86 102 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 104 113 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 116 128 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 139 150 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 141 155 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 157 166 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 169 184 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 462 470 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 464 481 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 484 493 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 496 514 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 517 531 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 519 538 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 541 550 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 553 570 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 573 585 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 575 591 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 593 602 {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT DISULFID 609 609 Interchain. {ECO:0000305}.
FT DISULFID 612 612 Interchain. {ECO:0000305}.
FT DISULFID 1184 1184 Interchain. {ECO:0000305}.
FT VAR_SEQ 1110 1193 DQPLSVDEEGLVLLEQKLSRAKTQINSQLRPMMSELEERAR
FT QQRGHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALE
FT QQ -> GM (in isoform Short).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_003040.
FT VARIANT 111 111 A -> P (in dbSNP:rs12065473).
FT /FTId=VAR_050081.
FT VARIANT 115 115 R -> Q (in dbSNP:rs17481405).
FT /FTId=VAR_050082.
FT VARIANT 124 124 T -> M (in dbSNP:rs11586699).
FT /FTId=VAR_050083.
FT VARIANT 136 136 D -> V (in dbSNP:rs12037099).
FT /FTId=VAR_050084.
FT VARIANT 247 247 D -> E (in dbSNP:rs2296306).
FT /FTId=VAR_022017.
FT VARIANT 608 608 S -> I (in dbSNP:rs4373715).
FT /FTId=VAR_050085.
FT VARIANT 733 733 S -> T (in dbSNP:rs2296303).
FT /FTId=VAR_020304.
FT CONFLICT 12 12 F -> L (in Ref. 2; CAA52108).
FT {ECO:0000305}.
FT CONFLICT 473 473 M -> I (in Ref. 1; CAA78728/CAA78729).
FT {ECO:0000305}.
FT CONFLICT 521 521 N -> S (in Ref. 1; CAA78728/CAA78729).
FT {ECO:0000305}.
FT CONFLICT 857 857 R -> P (in Ref. 1; CAA78728/CAA78729).
FT {ECO:0000305}.
FT CONFLICT 883 883 S -> T (in Ref. 3; AAC50457/AAC50456).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 573 612 ismart:EGF_Lam [T]
FT MYHIT 461 494 ismart:EGF [T]
FT MYHIT 417 460 ismart:EGF [T]
FT MYHIT 538 573 ipat:EGF_LAM_1 [T]
FT MYHIT 84 130 iprf:EGF_LAM_2 [T]
FT MYHIT 530 571 ismart:EGF [T]
FT MYHIT 462 514 ismart:EGF_Lam [T]
FT MYHIT 245 370 ismart:LamB [T]
FT MYHIT 155 189 ipat:EGF_LAM_1 [T]
FT MYHIT 517 570 ipfam:Laminin_EGF [T]
FT MYHIT 213 381 iprf:LAMININ_IVA [T]
FT MYHIT 370 413 ismart:EGF_Lam [T]
FT MYHIT 140 185 ismart:EGF [T]
FT MYHIT 139 184 ismart:EGF_Lam [T]
FT MYHIT 381 405 ipfam:Laminin_EGF [T]
FT MYHIT 28 81 ismart:EGF_Lam [T]
FT MYHIT 28 83 iprf:EGF_LAM_2 [T]
FT MYHIT 84 128 ipfam:Laminin_EGF [T]
FT MYHIT 28 81 ipfam:Laminin_EGF [T]
FT MYHIT 250 380 ipfam:Laminin_B [T]
FT MYHIT 139 186 iprf:EGF_LAM_2 [T]
FT MYHIT 573 614 iprf:EGF_LAM_2 [T]
FT MYHIT 84 128 ismart:EGF_Lam [T]
FT MYHIT 139 184 ipfam:Laminin_EGF [T]
FT MYHIT 517 570 ismart:EGF_Lam [T]
FT MYHIT 83 129 ismart:EGF [T]
FT MYHIT 517 572 iprf:EGF_LAM_2 [T]
FT MYHIT 574 603 ismart:EGF [T]
FT MYHIT 462 516 iprf:EGF_LAM_2 [T]
FT MYHIT 462 505 ipfam:Laminin_EGF [T]
FT MYHIT 573 604 ipfam:Laminin_EGF [T]
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
//
| |