Laminin, beta 1

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	MGI: 96743 HomoloGene: 1722 GeneCards: LAMB1
Gene location (Human) Chr. Chromosome 7 (human)[1] Band No data available Start 107,923,799 bp[1] End 108,003,255 bp[1]
Gene location (Mouse) Chr. Chromosome 12 (mouse)[2] Band No data available Start 31,265,234 bp[2] End 31,329,644 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • extracellular matrix structural constituent • structural molecule activity Cellular component • laminin-8 complex • extracellular matrix • proteinaceous 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 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 • cellular protein metabolic process 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 7: 31.27 – 31.33 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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

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. [Petz 2011

References

Further reading