Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Forms a heterodimer with a small (regulatory) subunit (CAPNS1). Ubiquitous. Activated by 200-1000 micromolar concentrations of calcium and inhibited by calpastatin. Belongs to the peptidase C2 family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Protease; EC 184.108.40.206; Motility/polarity/chemotaxis
Molecular Function: calcium ion binding; calcium-dependent cysteine-type endopeptidase activity; cysteine-type peptidase activity; cytoskeletal protein binding; protein binding; protein heterodimerization activity
Biological Process: blastocyst development; myoblast fusion; proteolysis; proteolysis involved in cellular protein catabolic process; regulation of cytoskeleton organization and biogenesis; response to hypoxia
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.