Bos taurus Gene: LAMC1 | |||||||||||||||
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Summary | |||||||||||||||
InnateDB Gene | IDBG-637115.3 | ||||||||||||||
Last Modified | 2014-10-13 [Report errors or provide feedback] | ||||||||||||||
Gene Symbol | LAMC1 | ||||||||||||||
Gene Name | laminin subunit gamma-1 precursor | ||||||||||||||
Synonyms | |||||||||||||||
Species | Bos taurus | ||||||||||||||
Ensembl Gene | ENSBTAG00000011966 | ||||||||||||||
Encoded Proteins |
laminin, gamma 1 (formerly LAMB2)
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Protein Structure | |||||||||||||||
Useful resources | Stemformatics EHFPI ImmGen | ||||||||||||||
Entrez Gene | |||||||||||||||
Summary |
This gene does not have any Entrez summary - the following is the summary from its human ortholog ENSG00000135862:
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, composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively), have 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 gamma chain isoform laminin, gamma 1. The gamma 1 chain, formerly thought to be a beta chain, contains structural domains similar to beta chains, however, lacks the short alpha region separating domains I and II. The structural organization of this gene also suggested that it had diverged considerably from the beta chain genes. Embryos of transgenic mice in which both alleles of the gamma 1 chain gene were inactivated by homologous recombination, lacked basement membranes, indicating that laminin, gamma 1 chain is necessary for laminin heterotrimer assembly. It has been inferred by analogy with the strikingly similar 3' UTR sequence in mouse laminin gamma 1 cDNA, that multiple polyadenylation sites are utilized in human to generate the 2 different sized mRNAs (5.5 and 7.5 kb) seen on Northern analysis. [provided by RefSeq, Aug 2011] 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, composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively), have 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 gamma chain isoform laminin, gamma 1. The gamma 1 chain, formerly thought to be a beta chain, contains structural domains similar to beta chains, however, lacks the short alpha region separating domains I and II. The structural organization of this gene also suggested that it had diverged considerably from the beta chain genes. Embryos of transgenic mice in which both alleles of the gamma 1 chain gene were inactivated by homologous recombination, lacked basement membranes, indicating that laminin, gamma 1 chain is necessary for laminin heterotrimer assembly. It has been inferred by analogy with the strikingly similar 3\' UTR sequence in mouse laminin gamma 1 cDNA, that multiple polyadenylation sites are utilized in human to generate the 2 different sized mRNAs (5.5 and 7.5 kb) seen on Northern analysis. [provided by RefSeq, Aug 2011] |
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Gene Information | |||||||||||||||
Type | Protein coding | ||||||||||||||
Genomic Location | Chromosome 16:65545497-65662819 | ||||||||||||||
Strand | Forward strand | ||||||||||||||
Band | |||||||||||||||
Transcripts |
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Interactions | |||||||||||||||
Number of Interactions |
This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 17 interaction(s) predicted by orthology.
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Gene Ontology | |||||||||||||||
Molecular Function |
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Biological Process |
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Cellular Component |
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Orthologs | |||||||||||||||
Species
Homo sapiens
Mus musculus
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Gene ID
Gene Order
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Pathway Predictions based on Human Orthology Data | |||||||||||||||
NETPATH |
Alpha6Beta4Integrin pathway
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REACTOME |
L1CAM interactions pathway
Developmental Biology pathway
Extracellular matrix organization pathway
Degradation of the extracellular matrix pathway
Axon guidance pathway
ECM proteoglycans pathway
Non-integrin membrane-ECM interactions pathway
Laminin interactions pathway
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KEGG |
ECM-receptor interaction pathway
Small cell lung cancer pathway
Focal adhesion pathway
Prion diseases pathway
Pathways in cancer pathway
Amoebiasis pathway
Toxoplasmosis pathway
ECM-receptor interaction pathway
Small cell lung cancer pathway
Focal adhesion pathway
Prion diseases pathway
Pathways in cancer pathway
Amoebiasis pathway
Toxoplasmosis pathway
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INOH | |||||||||||||||
PID NCI |
Beta1 integrin cell surface interactions
Regulation of nuclear SMAD2/3 signaling
Alpha6 beta4 integrin-ligand interactions
Beta3 integrin cell surface interactions
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Cross-References | |||||||||||||||
SwissProt | |||||||||||||||
TrEMBL | F1MD77 | ||||||||||||||
UniProt Splice Variant | |||||||||||||||
Entrez Gene | 532572 | ||||||||||||||
UniGene | Bt.19081 | ||||||||||||||
RefSeq | NM_001206817 | ||||||||||||||
HUGO | |||||||||||||||
OMIM | |||||||||||||||
CCDS | |||||||||||||||
HPRD | |||||||||||||||
IMGT | |||||||||||||||
EMBL | DAAA02043567 DAAA02043568 DAAA02043569 DAAA02043570 DAAA02043571 | ||||||||||||||
GenPept | |||||||||||||||
RNA Seq Atlas | 101909965 532572 | ||||||||||||||