Aliases for CAPN6 Gene
External Ids for CAPN6 Gene
Previous GeneCards Identifiers for CAPN6 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 highly expressed in the placenta. Its C-terminal region lacks any homology to the calmodulin-like domain of other calpains. The protein lacks critical active site residues and thus is suggested to be proteolytically inactive. The protein may play a role in tumor formation by inhibiting apoptosis and promoting angiogenesis. [provided by RefSeq, Nov 2009]
GeneCards Summary for CAPN6 Gene
CAPN6 (Calpain 6) is a Protein Coding gene. Diseases associated with CAPN6 include Leiomyosarcoma and Corneal Dystrophy, Posterior Polymorphous, 1. Among its related pathways are Arrhythmogenic right ventricular cardiomyopathy (ARVC) and DREAM Repression and Dynorphin Expression. GO annotations related to this gene include microtubule binding and calcium-dependent cysteine-type endopeptidase activity. An important paralog of this gene is CAPN5.
UniProtKB/Swiss-Prot for CAPN6 Gene
Microtubule-stabilizing protein that may be involved in the regulation of microtubule dynamics and cytoskeletal organization. May act as a regulator of RAC1 activity through interaction with ARHGEF2 to control lamellipodial formation and cell mobility. Does not seem to have protease activity as it has lost the active site residues (By similarity).
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.