Aliases for CAPN10 Gene
External Ids for CAPN10 Gene
Previous GeneCards Identifiers for CAPN10 Gene
Calpains represent a 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 catalytic subunit has four domains: domain I, the N-terminal regulatory domain that is processed upon calpain activation; domain II, the protease domain; domain III, a linker domain of unknown function; and domain IV, the calmodulin-like calcium-binding domain. This gene encodes a large subunit. It is an atypical calpain in that it lacks the calmodulin-like calcium-binding domain and instead has a divergent C-terminal domain. It is similar in organization to calpains 5 and 6. This gene is associated with type 2 or non-insulin-dependent diabetes mellitus (NIDDM), and is located within the NIDDM1 region. Multiple alternative transcript variants have been described for this gene. [provided by RefSeq, Sep 2010]
GeneCards Summary for CAPN10 Gene
CAPN10 (Calpain 10) is a Protein Coding gene. Diseases associated with CAPN10 include Diabetes Mellitus, Noninsulin-Dependent 1 and Polycystic Ovary Syndrome. Among its related pathways are Degradation of the extracellular matrix and Arrhythmogenic right ventricular cardiomyopathy (ARVC). GO annotations related to this gene include cytoskeletal protein binding and calcium-dependent cysteine-type endopeptidase activity. An important paralog of this gene is CAPN12.
UniProtKB/Swiss-Prot for CAPN10 Gene
Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. May play a role in insulin-stimulated glucose uptake.
Calpains are a group of calcium-sensitive cysteine proteases that are ubiquitously expressed in mammals. 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.