Aliases for CAPN1 Gene
External Ids for CAPN1 Gene
Previous GeneCards Identifiers for CAPN1 Gene
The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 1. Several transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Nov 2010]
GeneCards Summary for CAPN1 Gene
CAPN1 (Calpain 1, (Mu/I) Large Subunit) is a Protein Coding gene. Diseases associated with CAPN1 include meningothelial meningioma. 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 CAPN9.
UniProtKB/Swiss-Prot for CAPN1 Gene
Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction
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).