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 02-OCT-2024, entry version 230. 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; Q8IW75: SERPINA12; NbExp=3; IntAct=EBI-949174, EBI-6152746; 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; 156. 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; 99. 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 jPOST; P07942; -. DR MassIVE; P07942; -. DR PaxDb; 9606-ENSP00000222399; -. DR PeptideAtlas; P07942; -. DR ProteomicsDB; 52043; -. DR Pumba; P07942; -. DR Antibodypedia; 1361; 471 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; IPR050440; Laminin/Netrin_ECM. 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; KW Proteomics identification; Reference proteome; 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 //