ID LAMB1_HUMAN Reviewed; 1786 AA.
AC P07942; Q14D91;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 27-MAR-2024, entry version 227.
DE RecName: Full=Laminin subunit beta-1;
DE AltName: Full=Laminin B1 chain;
DE AltName: Full=Laminin-1 subunit beta;
DE AltName: Full=Laminin-10 subunit beta;
DE AltName: Full=Laminin-12 subunit beta;
DE AltName: Full=Laminin-2 subunit beta;
DE AltName: Full=Laminin-6 subunit beta;
DE AltName: Full=Laminin-8 subunit beta;
DE Flags: Precursor;
GN Name=LAMB1;
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 [GENOMIC DNA], AND VARIANT ARG-1022.
RX PubMed=1975589; DOI=10.1016/s0021-9258(18)55441-7;
RA Vuolteenaho R., Chow L.T., Tryggvason K.;
RT "Structure of the human laminin B1 chain gene.";
RL J. Biol. Chem. 265:15611-15616(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-1022.
RX PubMed=3611077; DOI=10.1016/s0021-9258(18)60982-2;
RA Pikkarainen T., Eddy R., Fukushima Y., Byers M., Shows T., Pihlajaniemi T.,
RA Saraste M., Tryggvason K.;
RT "Human laminin B1 chain. A multidomain protein with gene (LAMB1) locus in
RT the q22 region of chromosome 7.";
RL J. Biol. Chem. 262:10454-10462(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1276-1709.
RX PubMed=3661559;
RA Jaye M., Modi W.S., Ricca G.A., Mudd R., Chiu I.M., O'Brien S.J.,
RA Drohan W.N.;
RT "Isolation of a cDNA clone for the human laminin-B1 chain and its gene
RT localization.";
RL Am. J. Hum. Genet. 41:605-615(1987).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1279.
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 [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1279.
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 [8]
RP INVOLVEMENT IN LIS5, AND FUNCTION.
RX PubMed=23472759; DOI=10.1016/j.ajhg.2013.02.005;
RA Radmanesh F., Caglayan A.O., Silhavy J.L., Yilmaz C., Cantagrel V.,
RA Omar T., Rosti B., Kaymakcalan H., Gabriel S., Li M., Sestan N.,
RA Bilguvar K., Dobyns W.B., Zaki M.S., Gunel M., Gleeson J.G.;
RT "Mutations in LAMB1 cause cobblestone brain malformation without muscular
RT or ocular abnormalities.";
RL Am. J. Hum. Genet. 92:468-474(2013).
RN [9]
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 [10]
RP PHOSPHORYLATION AT SER-1478; SER-1496; SER-1666 AND SER-1682.
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 [11]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-1022, AND IDENTIFICATION BY MASS
RP 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. Involved in the organization of the
CC laminar architecture of cerebral cortex. It is probably required for
CC the integrity of the basement membrane/glia limitans that serves as an
CC anchor point for the endfeet of radial glial cells and as a physical
CC barrier to migrating neurons. Radial glial cells play a central role in
CC cerebral cortical development, where they act both as the proliferative
CC unit of the cerebral cortex and a scaffold for neurons migrating toward
CC the pial surface. {ECO:0000269|PubMed:23472759}.
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. Beta-1 is a
CC subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-
CC 211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8
CC (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213).
CC Interacts with ITGB1 (By similarity). {ECO:0000250|UniProtKB:Q01635}.
CC -!- INTERACTION:
CC P07942; P11912: CD79A; NbExp=3; IntAct=EBI-949174, EBI-7797864;
CC P07942; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-949174, EBI-13345167;
CC P07942; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-949174, EBI-741480;
CC P07942; C5MBE7: CTRG_03389; Xeno; NbExp=2; IntAct=EBI-949174, EBI-16225951;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Note=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 -!- DISEASE: Lissencephaly 5 (LIS5) [MIM:615191]: An autosomal recessive
CC brain malformation characterized by cobblestone changes in the cortex,
CC more severe in the posterior region, and subcortical band heterotopia.
CC Affected individuals have hydrocephalus, seizures, and severely delayed
CC psychomotor development. {ECO:0000269|PubMed:23472759}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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; M61951; AAA59486.1; -; Genomic_DNA.
DR EMBL; M58147; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61917; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61918; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61921; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61922; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61923; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61924; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61925; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61926; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61927; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61928; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61929; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61930; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61931; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61932; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61933; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61934; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61935; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61936; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61938; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61939; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61940; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61941; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61942; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61943; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61944; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61945; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61946; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61947; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61948; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61949; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M61950; AAA59486.1; JOINED; Genomic_DNA.
DR EMBL; M55370; AAA59485.1; -; Genomic_DNA.
DR EMBL; M55378; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55365; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55371; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55372; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55373; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55374; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55375; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55376; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55344; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55345; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55346; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55347; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55348; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55349; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55350; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55351; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55352; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55353; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55355; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55356; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55357; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55358; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55359; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55360; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55361; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55362; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55363; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55364; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55366; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55367; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55368; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M55369; AAA59485.1; JOINED; Genomic_DNA.
DR EMBL; M61916; AAA59482.1; -; mRNA.
DR EMBL; CH236947; EAL24388.1; -; Genomic_DNA.
DR EMBL; BC113455; AAI13456.1; -; mRNA.
DR EMBL; M20206; AAA59487.1; -; mRNA.
DR CCDS; CCDS5750.1; -.
DR PIR; S13547; MMHUB1.
DR RefSeq; NP_002282.2; NM_002291.2.
DR PDB; 5XAU; X-ray; 1.80 A; B/E=1714-1786.
DR PDB; 7CEC; EM; 3.90 A; D=1714-1786.
DR PDB; 8DMK; EM; 3.70 A; B=29-335.
DR PDBsum; 5XAU; -.
DR PDBsum; 7CEC; -.
DR PDBsum; 8DMK; -.
DR AlphaFoldDB; P07942; -.
DR EMDB; EMD-27542; -.
DR EMDB; EMD-30342; -.
DR SMR; P07942; -.
DR BioGRID; 110106; 149.
DR ComplexPortal; CPX-1770; Laminin-111 complex.
DR ComplexPortal; CPX-1771; Laminin-211 complex.
DR ComplexPortal; CPX-1775; Laminin-311 complex variant A.
DR ComplexPortal; CPX-1777; Laminin-411 complex.
DR ComplexPortal; CPX-1779; Laminin-511 complex.
DR ComplexPortal; CPX-1781; Laminin-213 complex.
DR ComplexPortal; CPX-3166; Laminin-311 complex variant B.
DR CORUM; P07942; -.
DR IntAct; P07942; 53.
DR MINT; P07942; -.
DR STRING; 9606.ENSP00000222399; -.
DR ChEMBL; CHEMBL2364187; -.
DR DrugBank; DB06245; Lanoteplase.
DR GlyConnect; 1442; 33 N-Linked glycans (6 sites).
DR GlyCosmos; P07942; 13 sites, 34 glycans.
DR GlyGen; P07942; 16 sites, 33 N-linked glycans (6 sites), 2 O-linked glycans (4 sites).
DR iPTMnet; P07942; -.
DR MetOSite; P07942; -.
DR PhosphoSitePlus; P07942; -.
DR SwissPalm; P07942; -.
DR BioMuta; LAMB1; -.
DR DMDM; 317373377; -.
DR EPD; P07942; -.
DR jPOST; P07942; -.
DR MassIVE; P07942; -.
DR MaxQB; P07942; -.
DR PaxDb; 9606-ENSP00000222399; -.
DR PeptideAtlas; P07942; -.
DR ProteomicsDB; 52043; -.
DR Pumba; P07942; -.
DR Antibodypedia; 1361; 483 antibodies from 42 providers.
DR DNASU; 3912; -.
DR Ensembl; ENST00000222399.11; ENSP00000222399.6; ENSG00000091136.15.
DR GeneID; 3912; -.
DR KEGG; hsa:3912; -.
DR MANE-Select; ENST00000222399.11; ENSP00000222399.6; NM_002291.3; NP_002282.2.
DR UCSC; uc003vew.3; human.
DR AGR; HGNC:6486; -.
DR CTD; 3912; -.
DR DisGeNET; 3912; -.
DR GeneCards; LAMB1; -.
DR HGNC; HGNC:6486; LAMB1.
DR HPA; ENSG00000091136; Low tissue specificity.
DR MalaCards; LAMB1; -.
DR MIM; 150240; gene.
DR MIM; 615191; phenotype.
DR neXtProt; NX_P07942; -.
DR OpenTargets; ENSG00000091136; -.
DR Orphanet; 352682; Cobblestone lissencephaly without muscular or ocular involvement.
DR PharmGKB; PA30275; -.
DR VEuPathDB; HostDB:ENSG00000091136; -.
DR eggNOG; KOG0994; Eukaryota.
DR GeneTree; ENSGT00940000156003; -.
DR HOGENOM; CLU_001560_1_0_1; -.
DR InParanoid; P07942; -.
DR OMA; AMDFDQD; -.
DR OrthoDB; 90222at2759; -.
DR PhylomeDB; P07942; -.
DR TreeFam; TF312903; -.
DR PathwayCommons; P07942; -.
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; P07942; -.
DR SIGNOR; P07942; -.
DR BioGRID-ORCS; 3912; 14 hits in 1161 CRISPR screens.
DR ChiTaRS; LAMB1; human.
DR GeneWiki; Laminin,_beta_1; -.
DR GenomeRNAi; 3912; -.
DR Pharos; P07942; Tbio.
DR PRO; PR:P07942; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P07942; Protein.
DR Bgee; ENSG00000091136; Expressed in tibial nerve and 198 other cell types or tissues.
DR ExpressionAtlas; P07942; baseline and differential.
DR Genevisible; P07942; 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; IDA:UniProtKB.
DR GO; GO:0005606; C:laminin-1 complex; IDA:UniProtKB.
DR GO; GO:0043259; C:laminin-10 complex; IDA:UniProtKB.
DR GO; GO:0005607; C:laminin-2 complex; IDA:UniProtKB.
DR GO; GO:0043257; C:laminin-8 complex; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; NAS:ComplexPortal.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IDA:HGNC-UCL.
DR GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; TAS:HGNC-UCL.
DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
DR GO; GO:0021812; P:neuronal-glial interaction involved in cerebral cortex radial glia guided migration; IMP:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; IDA:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; NAS:ComplexPortal.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
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; NAS:ComplexPortal.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; NAS:ComplexPortal.
DR GO; GO:0110011; P:regulation of basement membrane organization; NAS:ComplexPortal.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:BHF-UCL.
DR CDD; cd22300; cc_LAMB1_C; 1.
DR CDD; cd00055; EGF_Lam; 13.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF233; LAMININ SUBUNIT BETA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF21199; LAMININ_IV_B; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR SUPFAM; SSF46579; Prefoldin; 1.
DR PROSITE; PS00022; EGF_1; 9.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01248; EGF_LAM_1; 11.
DR PROSITE; PS50027; EGF_LAM_2; 13.
DR PROSITE; PS51116; LAMININ_IVB; 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; Lissencephaly; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT CHAIN 22..1786
FT /note="Laminin subunit beta-1"
FT /id="PRO_0000017065"
FT DOMAIN 31..270
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 271..334
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 335..397
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 398..457
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 458..509
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 510..540
FT /note="Laminin EGF-like 5; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 549..767
FT /note="Laminin IV type B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00462"
FT DOMAIN 773..820
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 821..866
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 867..916
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 917..975
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 976..1027
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1028..1083
FT /note="Laminin EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1084..1131
FT /note="Laminin EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1132..1178
FT /note="Laminin EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 1179..1397
FT /note="Domain II"
FT REGION 1398..1430
FT /note="Domain alpha"
FT REGION 1431..1786
FT /note="Domain I"
FT COILED 1216..1315
FT /evidence="ECO:0000255"
FT COILED 1353..1388
FT /evidence="ECO:0000255"
FT COILED 1442..1781
FT /evidence="ECO:0000255"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02469"
FT MOD_RES 1478
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 1496
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 1666
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 1682
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1041
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 1336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 271..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 273..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 300..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 312..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 335..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 337..362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 365..374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 377..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 398..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 400..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 428..437
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 440..455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 458..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 460..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 481..490
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 493..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 510..522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 512..529
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 531..540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 773..785
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 775..792
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 794..803
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 806..818
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 821..833
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 823..840
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 842..851
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 854..864
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 867..876
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 869..883
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 886..895
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 898..914
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 917..933
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 919..944
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 946..955
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 958..973
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 976..990
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 978..997
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1000..1009
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1012..1025
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1028..1040
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1030..1054
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1056..1065
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1068..1081
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1084..1096
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1086..1103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1105..1114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1117..1129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1132..1144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1134..1151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1153..1162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1165..1176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1179
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1182
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1785
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT VARIANT 379
FT /note="P -> S (in dbSNP:rs28750165)"
FT /id="VAR_061349"
FT VARIANT 670
FT /note="V -> A (in dbSNP:rs20555)"
FT /id="VAR_014698"
FT VARIANT 860
FT /note="G -> S (in dbSNP:rs35710474)"
FT /id="VAR_032774"
FT VARIANT 1022
FT /note="Q -> R (in dbSNP:rs20556)"
FT /evidence="ECO:0000269|PubMed:1975589,
FT ECO:0000269|PubMed:3611077, ECO:0007744|PubMed:21269460"
FT /id="VAR_014699"
FT CONFLICT 1470
FT /note="L -> V (in Ref. 5; AAA59487)"
FT /evidence="ECO:0000305"
FT CONFLICT 1696
FT /note="E -> G (in Ref. 5; AAA59487)"
FT /evidence="ECO:0000305"
FT HELIX 1717..1784
FT /evidence="ECO:0007829|PDB:5XAU"
SQ SEQUENCE 1786 AA; 198038 MW; 8F8EF96E765B9A0D CRC64;
MGLLQLLAFS FLALCRARVR AQEPEFSYGC AEGSCYPATG DLLIGRAQKL SVTSTCGLHK
PEPYCIVSHL QEDKKCFICN SQDPYHETLN PDSHLIENVV TTFAPNRLKI WWQSENGVEN
VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI ERSSDFGKTW GVYRYFAYDC EASFPGISTG
PMKKVDDIIC DSRYSDIEPS TEGEVIFRAL DPAFKIEDPY SPRIQNLLKI TNLRIKFVKL
HTLGDNLLDS RMEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGFNEEV EGMVHGHCMC
RHNTKGLNCE LCMDFYHDLP WRPAEGRNSN ACKKCNCNEH SISCHFDMAV YLATGNVSGG
VCDDCQHNTM GRNCEQCKPF YYQHPERDIR DPNFCERCTC DPAGSQNEGI CDSYTDFSTG
LIAGQCRCKL NVEGEHCDVC KEGFYDLSSE DPFGCKSCAC NPLGTIPGGN PCDSETGHCY
CKRLVTGQHC DQCLPEHWGL SNDLDGCRPC DCDLGGALNN SCFAESGQCS CRPHMIGRQC
NEVEPGYYFA TLDHYLYEAE EANLGPGVSI VERQYIQDRI PSWTGAGFVR VPEGAYLEFF
IDNIPYSMEY DILIRYEPQL PDHWEKAVIT VQRPGRIPTS SRCGNTIPDD DNQVVSLSPG
SRYVVLPRPV CFEKGTNYTV RLELPQYTSS DSDVESPYTL IDSLVLMPYC KSLDIFTVGG
SGDGVVTNSA WETFQRYRCL ENSRSVVKTP MTDVCRNIIF SISALLHQTG LACECDPQGS
LSSVCDPNGG QCQCRPNVVG RTCNRCAPGT FGFGPSGCKP CECHLQGSVN AFCNPVTGQC
HCFQGVYARQ CDRCLPGHWG FPSCQPCQCN GHADDCDPVT GECLNCQDYT MGHNCERCLA
GYYGDPIIGS GDHCRPCPCP DGPDSGRQFA RSCYQDPVTL QLACVCDPGY IGSRCDDCAS
GYFGNPSEVG GSCQPCQCHN NIDTTDPEAC DKETGRCLKC LYHTEGEHCQ FCRFGYYGDA
LQQDCRKCVC NYLGTVQEHC NGSDCQCDKA TGQCLCLPNV IGQNCDRCAP NTWQLASGTG
CDPCNCNAAH SFGPSCNEFT GQCQCMPGFG GRTCSECQEL FWGDPDVECR ACDCDPRGIE
TPQCDQSTGQ CVCVEGVEGP RCDKCTRGYS GVFPDCTPCH QCFALWDVII AELTNRTHRF
LEKAKALKIS GVIGPYRETV DSVERKVSEI KDILAQSPAA EPLKNIGNLF EEAEKLIKDV
TEMMAQVEVK LSDTTSQSNS TAKELDSLQT EAESLDNTVK ELAEQLEFIK NSDIRGALDS
ITKYFQMSLE AEERVNASTT EPNSTVEQSA LMRDRVEDVM MERESQFKEK QEEQARLLDE
LAGKLQSLDL SAAAEMTCGT PPGASCSETE CGGPNCRTDE GERKCGGPGC GGLVTVAHNA
WQKAMDLDQD VLSALAEVEQ LSKMVSEAKL RADEAKQSAE DILLKTNATK EKMDKSNEEL
RNLIKQIRNF LTQDSADLDS IEAVANEVLK MEMPSTPQQL QNLTEDIRER VESLSQVEVI
LQHSAADIAR AEMLLEEAKR ASKSATDVKV TADMVKEALE EAEKAQVAAE KAIKQADEDI
QGTQNLLTSI ESETAASEET LFNASQRISE LERNVEELKR KAAQNSGEAE YIEKVVYTVK
QSAEDVKKTL DGELDEKYKK VENLIAKKTE ESADARRKAE MLQNEAKTLL AQANSKLQLL
KDLERKYEDN QRYLEDKAQE LARLEGEVRS LLKDISQKVA VYSTCL
//
