Aliases for CAPN9 Gene
External Ids for CAPN9 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 protein encoded by this gene is expressed predominantly in stomach and small intestine and may have specialized functions in the digestive tract. This gene is thought to be associated with gastric cancer. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
GeneCards Summary for CAPN9 Gene
CAPN9 (Calpain 9) is a Protein Coding gene. Among its related pathways are ERK Signaling and Apoptosis Pathway. GO annotations related to this gene include calcium ion binding and calcium-dependent cysteine-type endopeptidase activity. An important paralog of this gene is CAPNS2.
UniProtKB/Swiss-Prot for CAPN9 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), Alzheimers disease (calpain 1), gastric cancer (calpain 9) and muscular dystrophy (calpain 3).