Laminin, beta 1

Laminin subunit beta-1 is a protein that in humans is encoded by the LAMB1 gene.[5][6][7][8]

LAMB1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4AQS
Identifiers
Aliases	LAMB1, CLM, LIS5, Laminin, beta 1, laminin subunit beta 1
External IDs	OMIM: 150240 MGI: 96743 HomoloGene: 1722 GeneCards: LAMB1
Gene location (Human) Chr. Chromosome 7 (human)[1] Band 7q31.1 Start 107,923,799 bp[1] End 108,003,213 bp[1]
Gene location (Mouse) Chr. Chromosome 12 (mouse)[2] Band 12 A2|12 13.39 cM Start 31,315,233 bp[2] End 31,379,643 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tibial nerve right lung stromal cell of endometrium upper lobe of left lung parietal pleura sural nerve left uterine tube trigeminal ganglion gastric mucosa pericardium Top expressed in external carotid artery internal carotid artery iris secondary oocyte left lung lobe medullary collecting duct vas deferens sciatic nerve ciliary body primitive streak More reference expression data BioGPS More reference expression data
Gene ontology Molecular function extracellular matrix structural constituent structural molecule activity protein binding integrin binding Cellular component laminin-8 complex extracellular matrix laminin-2 complex extracellular region basement membrane laminin-10 complex perinuclear region of cytoplasm laminin-1 complex extracellular exosome extracellular space endoplasmic reticulum lumen collagen-containing extracellular matrix laminin complex Biological process endodermal cell differentiation positive regulation of epithelial cell proliferation positive regulation of cell migration neuronal-glial interaction involved in cerebral cortex radial glia guided migration extracellular matrix organization odontogenesis cell adhesion substrate adhesion-dependent cell spreading neuron projection development post-translational protein modification animal organ morphogenesis tissue development cell migration basement membrane assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3912 16777 Ensembl ENSG00000091136 ENSMUSG00000002900 UniProt P07942 P02469 RefSeq (mRNA) NM_002291 NM_008482 RefSeq (protein) NP_002282 NP_032508 Location (UCSC) Chr 7: 107.92 – 108 Mb Chr 12: 31.32 – 31.38 Mb PubMed search [3] [4]
Wikidata
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Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms, which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the beta chain isoform laminin, beta 1. The beta 1 chain has 7 structurally distinct domains, which it shares with other beta chain isomers. The C-terminal helical region containing domains I and II are separated by domain alpha, domains III and V contain several EGF-like repeats, and domains IV and VI have a globular conformation. Laminin, beta 1 is expressed in most tissues that produce basement membranes, and is one of the 3 chains constituting laminin 1, the first laminin isolated from Engelbreth-Holm-Swarm (EHS) tumor. A sequence in the beta 1 chain that is involved in cell attachment, chemotaxis, and binding to the laminin receptor was identified and shown to have the capacity to inhibit metastasis.[8]

5′-UTR of Laminin-B1 harbors IRES (internal ribosome entry site) between −293 and −1 upstream of the start codon. IRES are involved in cancer malignancy.[9]