Calpain 6 (CAPN6)

CAPNX; CalpM; CANPX; Calpamodulin; Calpain-like protease X-linked

SPN	R546
HGNC	1483
MGI	1100850
PubMed	20814968
RGD	70960
UniProt	Q9Y6Q1

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.

CAPN6 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.

Reference

"A new subfamily of vertebrate calpains lacking a calmodulin-like domain: implications for calpain regulation and evolution."
Genomics 45:175-184(1997) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence of the human X chromosome."
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Calpain 6 is involved in microtubule stabilization and cytoskeletal organization."
Mol. Cell. Biol. 27:2548-2561(2007) [PubMed] [Europe PMC] [Abstract]

"The consensus coding sequences of human breast and colorectal cancers."
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]