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.
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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   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.
DR   Genevisible; P07942; HS.
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
//