Aliases for CAPN7 Gene
External Ids for CAPN7 Gene
Previous GeneCards Identifiers for CAPN7 Gene
Calpains are ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. The calpain proteins are heterodimers consisting of an invariant small subunit and variable large subunits. The large subunit possesses a cysteine protease domain, and both subunits possess calcium-binding domains. Calpains have been implicated in neurodegenerative processes, as their activation can be triggered by calcium influx and oxidative stress. The function of the protein encoded by this gene is not known. An orthologue has been found in mouse but it seems to diverge from other family members. The mouse orthologue is thought to be calcium independent with protease activity. [provided by RefSeq, Jul 2008]
GeneCards Summary for CAPN7 Gene
CAPN7 (Calpain 7) is a Protein Coding gene. Among its related pathways are ERK Signaling and Apoptosis Pathway. GO annotations related to this gene include calcium-dependent cysteine-type endopeptidase activity and MIT domain binding. An important paralog of this gene is CAPN15.
UniProtKB/Swiss-Prot for CAPN7 Gene
Calcium-regulated non-lysosomal thiol-protease.
Calpains are a group of calcium-sensitive cysteine proteases that are ubiquitously expressed in mammals. This family contains 14 members with mu-calpain (calpain 1) and m-calpain (calpain 2) being the most well-characterized. Structurally, calpains contain two subunits; an 80 kDa catalytic subunit and a 28 kDa regulatory subunit that functions as a chaperone to stabilize the 80 kDa structure. Calpains are regulated by Ca2+ concentration, phosphorylation, calpastatin and probably by altering their subcellular localization (limiting access to substrate). These endopeptidases have numerous functions including, but not limited to, remodeling of cytoskeletal attachments to the plasma membrane during cell fusion and cell motility, proteolytic modification of molecules in signal transduction pathways, degradation of enzymes controlling progression through the cell cycle, regulation of gene expression, substrate degradation in some apoptotic pathways, and an involvement in long-term potentiation. Perturbations in calpain activity have been associated in pathophysiological processes contributing to type II diabetes (calpain 10), Alzheimer's disease (calpain 1), gastric cancer (calpain 9) and muscular dystrophy (calpain 3).