GenomeNet

Database: UniProt
Entry: Q13753
LinkDB: Q13753
Original site: Q13753 
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   13-FEB-2019, entry version 190.
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}.
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   UniGene; Hs.591484; -.
DR   ProteinModelPortal; Q13753; -.
DR   SMR; Q13753; -.
DR   BioGrid; 110112; 6.
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; 1.
DR   MINT; Q13753; -.
DR   STRING; 9606.ENSP00000264144; -.
DR   ChEMBL; CHEMBL2364187; -.
DR   Allergome; 8331; Hom s Laminin gamma_2.
DR   GlyConnect; 1445; -.
DR   iPTMnet; Q13753; -.
DR   PhosphoSitePlus; Q13753; -.
DR   BioMuta; LAMC2; -.
DR   DMDM; 90185107; -.
DR   EPD; Q13753; -.
DR   jPOST; Q13753; -.
DR   MaxQB; Q13753; -.
DR   PaxDb; Q13753; -.
DR   PeptideAtlas; Q13753; -.
DR   PRIDE; Q13753; -.
DR   ProteomicsDB; 59675; -.
DR   ProteomicsDB; 59676; -. [Q13753-2]
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   EuPathDB; HostDB:ENSG00000058085.14; -.
DR   GeneCards; LAMC2; -.
DR   GeneReviews; LAMC2; -.
DR   HGNC; HGNC:6493; LAMC2.
DR   HPA; CAB004257; -.
DR   HPA; CAB078165; -.
DR   HPA; HPA024638; -.
DR   MalaCards; LAMC2; -.
DR   MIM; 150292; gene.
DR   MIM; 226700; phenotype.
DR   neXtProt; NX_Q13753; -.
DR   OpenTargets; ENSG00000058085; -.
DR   Orphanet; 79405; Junctional epidermolysis bullosa inversa.
DR   Orphanet; 79402; Junctional epidermolysis bullosa, generalized intermediate.
DR   Orphanet; 79404; Junctional epidermolysis bullosa, generalized severe.
DR   PharmGKB; PA30281; -.
DR   eggNOG; ENOG410IP6C; Eukaryota.
DR   eggNOG; ENOG4110QI9; LUCA.
DR   GeneTree; ENSGT00940000160470; -.
DR   HOGENOM; HOG000019301; -.
DR   HOVERGEN; HBG062127; -.
DR   InParanoid; Q13753; -.
DR   KO; K06246; -.
DR   OMA; TEEVVCN; -.
DR   OrthoDB; 1504122at2759; -.
DR   PhylomeDB; 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   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; Expressed in 163 organ(s), highest expression level in islet of Langerhans.
DR   Genevisible; Q13753; HS.
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:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0070831; P:basement membrane assembly; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0008544; P:epidermis development; TAS:ProtInc.
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 population proliferation; IMP:BHF-UCL.
DR   GO; GO:0048731; P:system development; IEA:InterPro.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR031082; Laminin_gamma-2.
DR   InterPro; IPR000034; Laminin_IV.
DR   PANTHER; PTHR10574:SF313; PTHR10574:SF313; 1.
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...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    362    362       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    942    942       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1033   1033       N-linked (GlcNAc...) asparagine.
FT                                {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}.
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
//
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