| 简介 | 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]
Diseases associated with CAPN6 include Leiomyosarcoma and Leiomyoma. Among its related pathways are DREAM Repression and Dynorphin Expression and Extracellular matrix organization. Gene Ontology (GO) annotations related to this gene include microtubule binding and calcium-dependent cysteine-type endopeptidase activity. An important paralog of this gene is CAPN5.
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).
calpain,class C,large polypeptide,likely lacking a protease activity,papain superfamily,nCL-3 type,expressed only in placenta,homolog to C elegans sex determination gene tra3
Cytoplasm, perinuclear region {ECO:0000269 PubMed:17210638}
Cytoplasm, cytoskeleton, spindle {ECO:0000269 PubMed:17210638}5
Note: During mitose associated with the mitotic spindle. At telophase colocalized to the midbody spindle.
Quaternary structure:
Interacts (via domain III) with microtubules.
Interacts (via domain II) with ARHGEF2 (via the N-terminal zinc finger). |
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