Calpain 11 (CAPN11)

Calcium-activated neutral proteinase 11

SPN	R544
HGNC	1478
MGI	1352490
PubMed	10559499
RGD	1302946
UniProt	Q9UMQ6

Calpains constitute a family of intracellular calcium-dependent cysteine proteases. There are eight members in this superfamily. They consist of a variable 80 kDa subunit and an invariant 30 kDa subunit. This calpain protein appears to have protease activity and calcium-binding ability.

The complete CAPN11 coding sequence encodes a deduced 702-amino acid protein with similarity to the large subunits of calpains. CAPN11 can be subdivided into the 4 domains typical of calpains. Domain II shows the characteristics of a protease domain and contains the cysteine, histidine, and asparagine residues that are part of the active site of cysteine proteases. Domain IV contains 5 putative calcium-binding EF-hand motifs.

Reference

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and analysis of human chromosome 6."
Nature 425:805-811(2003) [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]

"CAPN11: a calpain with high mRNA levels in testis and located on chromosome 6."
Genomics 59:243-247(1999) [PubMed] [Europe PMC] [Abstract]