LAMC1_HUMAN
ID LAMC1_HUMAN Reviewed; 1609 AA.
AC P11047; Q5VYE7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Laminin subunit gamma-1;
DE AltName: Full=Laminin B2 chain;
DE AltName: Full=Laminin-1 subunit gamma;
DE AltName: Full=Laminin-10 subunit gamma;
DE AltName: Full=Laminin-11 subunit gamma;
DE AltName: Full=Laminin-2 subunit gamma;
DE AltName: Full=Laminin-3 subunit gamma;
DE AltName: Full=Laminin-4 subunit gamma;
DE AltName: Full=Laminin-6 subunit gamma;
DE AltName: Full=Laminin-7 subunit gamma;
DE AltName: Full=Laminin-8 subunit gamma;
DE AltName: Full=Laminin-9 subunit gamma;
DE AltName: Full=S-laminin subunit gamma;
DE Short=S-LAM gamma;
DE Flags: Precursor;
GN Name=LAMC1 {ECO:0000303|PubMed:28397838, ECO:0000312|HGNC:HGNC:6492};
GN Synonyms=LAMB2;
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 VARIANTS VAL-458 AND PRO-888.
RX PubMed=3360804; DOI=10.1016/s0021-9258(18)68707-1;
RA Pikkarainen T., Kallunki T., Tryggvason K.;
RT "Human laminin B2 chain. Comparison of the complete amino acid sequence
RT with the B1 chain reveals variability in sequence homology between
RT different structural domains.";
RL J. Biol. Chem. 263:6751-6758(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-458 AND PRO-888.
RX PubMed=1985895; DOI=10.1016/s0021-9258(18)52424-8;
RA Kallunki T., Ikonen J., Chow L.T., Kallunki P., Tryggvason K.;
RT "Structure of the human laminin B2 chain gene reveals extensive divergence
RT from the laminin B1 chain gene.";
RL J. Biol. Chem. 266:221-228(1991).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1282-1609.
RC TISSUE=Endothelial cell;
RX PubMed=1806043; DOI=10.3109/10425179109020782;
RA Santos C.L.S., Sabbaga J., Brentani R.;
RT "Differences in human laminin B2 sequences.";
RL DNA Seq. 1:275-277(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1393-1609.
RX PubMed=3234037; DOI=10.1159/000132610;
RA Fukushima Y., Pikkarainen T., Kallunki T., Eddy R.L., Byers M.G.,
RA Haley L.L., Henry W.M., Tryggvason K., Shows T.B.;
RT "Isolation of a human laminin B2 (LAMB2) cDNA clone and assignment of the
RT gene to chromosome region 1q25-->q31.";
RL Cytogenet. Cell Genet. 48:137-141(1988).
RN [6]
RP GLYCOSYLATION AT ASN-650.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1107; ASN-1161; ASN-1175;
RP ASN-1223 AND ASN-1395.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-650; ASN-1107; ASN-1241 AND
RP ASN-1395.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1493, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP PHOSPHORYLATION AT SER-1149.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-1116.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [15]
RP VARIANT LEU-363.
RX PubMed=28397838; DOI=10.1038/mp.2017.60;
RA Harripaul R., Vasli N., Mikhailov A., Rafiq M.A., Mittal K.,
RA Windpassinger C., Sheikh T.I., Noor A., Mahmood H., Downey S., Johnson M.,
RA Vleuten K., Bell L., Ilyas M., Khan F.S., Khan V., Moradi M., Ayaz M.,
RA Naeem F., Heidari A., Ahmed I., Ghadami S., Agha Z., Zeinali S., Qamar R.,
RA Mozhdehipanah H., John P., Mir A., Ansar M., French L., Ayub M.,
RA Vincent J.B.;
RT "Mapping autosomal recessive intellectual disability: combined microarray
RT and exome sequencing identifies 26 novel candidate genes in 192
RT consanguineous families.";
RL Mol. Psychiatry 23:973-984(2018).
CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC thought to mediate the attachment, migration and organization of cells
CC into tissues during embryonic development by interacting with other
CC extracellular matrix components.
CC -!- 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-1 is a
CC subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-
CC 211 or merosin), laminin-3 (laminin-121 or S-laminin), laminin-4
CC (laminin-221 or S-merosin), laminin-6 (laminin-311 or K-laminin),
CC laminin-7 (laminin-321 or KS-laminin), laminin-8 (laminin-411),
CC laminin-9 (laminin-421), laminin-10 (laminin-511) and laminin-11
CC (laminin-521).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- TISSUE SPECIFICITY: Found in the basement membranes (major component).
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: Domains VI and IV are globular.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J03202; AAA59488.1; -; mRNA.
DR EMBL; M55210; AAA59492.1; -; Genomic_DNA.
DR EMBL; M55217; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55201; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55211; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55212; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55213; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55214; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55215; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55216; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55192; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55193; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55194; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55195; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55196; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55197; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55198; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55199; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55200; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55202; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55203; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55204; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55205; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55206; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55207; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55208; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; M55209; AAA59492.1; JOINED; Genomic_DNA.
DR EMBL; AL354953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X13939; CAA32122.1; -; mRNA.
DR EMBL; M27654; AAA59489.1; -; mRNA.
DR CCDS; CCDS1351.1; -.
DR PIR; S13548; MMHUB2.
DR RefSeq; NP_002284.3; NM_002293.3.
DR PDB; 5XAU; X-ray; 1.80 A; C/F=1528-1609.
DR PDB; 7CEC; EM; 3.90 A; E=1528-1609.
DR PDBsum; 5XAU; -.
DR PDBsum; 7CEC; -.
DR AlphaFoldDB; P11047; -.
DR SMR; P11047; -.
DR BioGRID; 110109; 132.
DR ComplexPortal; CPX-1770; Laminin-111 complex.
DR ComplexPortal; CPX-1771; Laminin-211 complex.
DR ComplexPortal; CPX-1772; Laminin-121 complex.
DR ComplexPortal; CPX-1773; Laminin-221 complex.
DR ComplexPortal; CPX-1775; Laminin-311 complex variant A.
DR ComplexPortal; CPX-1776; Laminin-321 complex.
DR ComplexPortal; CPX-1777; Laminin-411 complex.
DR ComplexPortal; CPX-1778; Laminin-421 complex.
DR ComplexPortal; CPX-1779; Laminin-511 complex.
DR ComplexPortal; CPX-1780; Laminin-521 complex.
DR ComplexPortal; CPX-3166; Laminin-311 complex variant B.
DR CORUM; P11047; -.
DR IntAct; P11047; 27.
DR MINT; P11047; -.
DR STRING; 9606.ENSP00000258341; -.
DR ChEMBL; CHEMBL2364187; -.
DR DrugBank; DB06245; Lanoteplase.
DR CarbonylDB; P11047; -.
DR GlyConnect; 1444; 60 N-Linked glycans (9 sites).
DR GlyGen; P11047; 19 sites, 63 N-linked glycans (9 sites), 4 O-linked glycans (5 sites).
DR iPTMnet; P11047; -.
DR PhosphoSitePlus; P11047; -.
DR SwissPalm; P11047; -.
DR BioMuta; LAMC1; -.
DR DMDM; 224471885; -.
DR EPD; P11047; -.
DR jPOST; P11047; -.
DR MassIVE; P11047; -.
DR MaxQB; P11047; -.
DR PaxDb; P11047; -.
DR PeptideAtlas; P11047; -.
DR PRIDE; P11047; -.
DR ProteomicsDB; 52689; -.
DR Antibodypedia; 1055; 527 antibodies from 34 providers.
DR DNASU; 3915; -.
DR Ensembl; ENST00000258341.5; ENSP00000258341.3; ENSG00000135862.6.
DR GeneID; 3915; -.
DR KEGG; hsa:3915; -.
DR MANE-Select; ENST00000258341.5; ENSP00000258341.3; NM_002293.4; NP_002284.3.
DR UCSC; uc001gpy.4; human.
DR CTD; 3915; -.
DR DisGeNET; 3915; -.
DR GeneCards; LAMC1; -.
DR HGNC; HGNC:6492; LAMC1.
DR HPA; ENSG00000135862; Tissue enhanced (placenta).
DR MIM; 150290; gene.
DR neXtProt; NX_P11047; -.
DR OpenTargets; ENSG00000135862; -.
DR PharmGKB; PA30280; -.
DR VEuPathDB; HostDB:ENSG00000135862; -.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000158069; -.
DR HOGENOM; CLU_002471_1_0_1; -.
DR InParanoid; P11047; -.
DR OMA; NGQCDIH; -.
DR OrthoDB; 156553at2759; -.
DR PhylomeDB; P11047; -.
DR TreeFam; TF352481; -.
DR PathwayCommons; P11047; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-3000157; Laminin interactions.
DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-373760; L1CAM interactions.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR SignaLink; P11047; -.
DR SIGNOR; P11047; -.
DR BioGRID-ORCS; 3915; 10 hits in 1072 CRISPR screens.
DR ChiTaRS; LAMC1; human.
DR GeneWiki; Laminin,_gamma_1; -.
DR GenomeRNAi; 3915; -.
DR Pharos; P11047; Tbio.
DR PRO; PR:P11047; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P11047; protein.
DR Bgee; ENSG00000135862; Expressed in stromal cell of endometrium and 207 other tissues.
DR ExpressionAtlas; P11047; baseline and differential.
DR Genevisible; P11047; HS.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
DR GO; GO:0005606; C:laminin-1 complex; TAS:HGNC-UCL.
DR GO; GO:0043259; C:laminin-10 complex; TAS:BHF-UCL.
DR GO; GO:0043260; C:laminin-11 complex; TAS:BHF-UCL.
DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; IC:ComplexPortal.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IMP:HGNC-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IDA:HGNC-UCL.
DR GO; GO:0016477; P:cell migration; IMP:HGNC-UCL.
DR GO; GO:0007492; P:endoderm development; TAS:ProtInc.
DR GO; GO:0022617; P:extracellular matrix disassembly; IMP:HGNC-UCL.
DR GO; GO:0031581; P:hemidesmosome assembly; IMP:HGNC-UCL.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IC:ComplexPortal.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; TAS:HGNC-UCL.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IC:ComplexPortal.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IC:ComplexPortal.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:HGNC-UCL.
DR GO; GO:0110011; P:regulation of basement membrane organization; IC:ComplexPortal.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:BHF-UCL.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 10.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 10.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 10.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00136; LamNT; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01248; EGF_LAM_1; 11.
DR PROSITE; PS50027; EGF_LAM_2; 10.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Basement membrane; Cell adhesion; Coiled coil;
KW Disulfide bond; Extracellular matrix; Glycoprotein;
KW Laminin EGF-like domain; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..33
FT CHAIN 34..1609
FT /note="Laminin subunit gamma-1"
FT /id="PRO_0000017074"
FT DOMAIN 46..285
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 286..341
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 342..397
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 398..444
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 445..494
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 495..504
FT /note="Laminin EGF-like 5; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 514..689
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 690..723
FT /note="Laminin EGF-like 5; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 724..772
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 773..827
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 828..883
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 884..934
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 935..982
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 983..1030
FT /note="Laminin EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 1030..1609
FT /note="Domain II and I"
FT COILED 1038..1609
FT /evidence="ECO:0000255"
FT MOD_RES 1149
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 1493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 650
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 1022
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 1161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 1175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 1205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 1241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 1380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 1439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 286..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 288..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 307..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 319..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 342..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 344..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 370..379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 382..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 398..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 400..416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 418..427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 430..442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 445..456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 447..463
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 465..474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 477..492
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 724..733
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 726..740
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 742..751
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 754..770
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 773..781
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 775..792
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 795..804
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 807..825
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 828..842
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 830..849
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 852..861
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 864..881
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 884..898
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 886..905
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 907..916
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 919..932
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 935..947
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 937..954
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 956..965
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 968..980
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 983..995
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 985..1001
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1003..1012
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1015..1028
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1031
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1034
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1600
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT VARIANT 363
FT /note="H -> L (found in a consanguineous family with
FT intellectual disability; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28397838"
FT /id="VAR_080757"
FT VARIANT 458
FT /note="I -> V (in dbSNP:rs20563)"
FT /evidence="ECO:0000269|PubMed:1985895,
FT ECO:0000269|PubMed:3360804"
FT /id="VAR_014700"
FT VARIANT 731
FT /note="E -> K (in dbSNP:rs2230157)"
FT /id="VAR_054488"
FT VARIANT 888
FT /note="L -> P (in dbSNP:rs20558)"
FT /evidence="ECO:0000269|PubMed:1985895,
FT ECO:0000269|PubMed:3360804"
FT /id="VAR_014701"
FT VARIANT 1116
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs548688323)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035821"
FT VARIANT 1121
FT /note="R -> Q (in dbSNP:rs20559)"
FT /id="VAR_014702"
FT CONFLICT 212
FT /note="I -> F (in Ref. 2; AAA59492)"
FT /evidence="ECO:0000305"
FT HELIX 1536..1552
FT /evidence="ECO:0007829|PDB:5XAU"
FT HELIX 1554..1595
FT /evidence="ECO:0007829|PDB:5XAU"
SQ SEQUENCE 1609 AA; 177603 MW; 42D9A9958EEBBB01 CRC64;
MRGSHRAAPA LRPRGRLWPV LAVLAAAAAA GCAQAAMDEC TDEGGRPQRC MPEFVNAAFN
VTVVATNTCG TPPEEYCVQT GVTGVTKSCH LCDAGQPHLQ HGAAFLTDYN NQADTTWWQS
QTMLAGVQYP SSINLTLHLG KAFDITYVRL KFHTSRPESF AIYKRTREDG PWIPYQYYSG
SCENTYSKAN RGFIRTGGDE QQALCTDEFS DISPLTGGNV AFSTLEGRPS AYNFDNSPVL
QEWVTATDIR VTLNRLNTFG DEVFNDPKVL KSYYYAISDF AVGGRCKCNG HASECMKNEF
DKLVCNCKHN TYGVDCEKCL PFFNDRPWRR ATAESASECL PCDCNGRSQE CYFDPELYRS
TGHGGHCTNC QDNTDGAHCE RCRENFFRLG NNEACSSCHC SPVGSLSTQC DSYGRCSCKP
GVMGDKCDRC QPGFHSLTEA GCRPCSCDPS GSIDECNIET GRCVCKDNVE GFNCERCKPG
FFNLESSNPR GCTPCFCFGH SSVCTNAVGY SVYSISSTFQ IDEDGWRAEQ RDGSEASLEW
SSERQDIAVI SDSYFPRYFI APAKFLGKQV LSYGQNLSFS FRVDRRDTRL SAEDLVLEGA
GLRVSVPLIA QGNSYPSETT VKYVFRLHEA TDYPWRPALT PFEFQKLLNN LTSIKIRGTY
SERSAGYLDD VTLASARPGP GVPATWVESC TCPVGYGGQF CEMCLSGYRR ETPNLGPYSP
CVLCACNGHS ETCDPETGVC NCRDNTAGPH CEKCSDGYYG DSTAGTSSDC QPCPCPGGSS
CAVVPKTKEV VCTNCPTGTT GKRCELCDDG YFGDPLGRNG PVRLCRLCQC SDNIDPNAVG
NCNRLTGECL KCIYNTAGFY CDRCKDGFFG NPLAPNPADK CKACNCNLYG TMKQQSSCNP
VTGQCECLPH VTGQDCGACD PGFYNLQSGQ GCERCDCHAL GSTNGQCDIR TGQCECQPGI
TGQHCERCEV NHFGFGPEGC KPCDCHPEGS LSLQCKDDGR CECREGFVGN RCDQCEENYF
YNRSWPGCQE CPACYRLVKD KVADHRVKLQ ELESLIANLG TGDEMVTDQA FEDRLKEAER
EVMDLLREAQ DVKDVDQNLM DRLQRVNNTL SSQISRLQNI RNTIEETGNL AEQARAHVEN
TERLIEIASR ELEKAKVAAA NVSVTQPEST GDPNNMTLLA EEARKLAERH KQEADDIVRV
AKTANDTSTE AYNLLLRTLA GENQTAFEIE ELNRKYEQAK NISQDLEKQA ARVHEEAKRA
GDKAVEIYAS VAQLSPLDSE TLENEANNIK MEAENLEQLI DQKLKDYEDL REDMRGKELE
VKNLLEKGKT EQQTADQLLA RADAAKALAE EAAKKGRDTL QEANDILNNL KDFDRRVNDN
KTAAEEALRK IPAINQTITE ANEKTREAQQ ALGSAAADAT EAKNKAHEAE RIASAVQKNA
TSTKAEAERT FAEVTDLDNE VNNMLKQLQE AEKELKRKQD DADQDMMMAG MASQAAQEAE
INARKAKNSV TSLLSIINDL LEQLGQLDTV DLNKLNEIEG TLNKAKDEMK VSDLDRKVSD
LENEAKKQEA AIMDYNRDIE EIMKDIRNLE DIRKTLPSGC FNTPSIEKP
