Calpain-2
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.53 calpain-2
Calpain-2 is the type example of peptidase family C2, a cytosolic Ca2+-dependent cysteine protease requiring millimolar Ca2+ for activity. The active enzyme is a heterodimer whose large subunit carries the peptidase unit and whose small subunit is shared with calpain-1 (EC 3.4.22.52). It has broad endopeptidase specificity and performs regulatory cleavage of cytoskeletal and focal-adhesion proteins. In animal cells it is activated at the plasma membrane during motility and adhesion. It features a cysteine-protease core with Ca2+-binding EF-hand domains.
Calpain-2 is the type example of peptidase family C2, a cytosolic Ca2+-dependent cysteine protease requiring millimolar Ca2+ for activity. The active enzyme is a heterodimer whose large subunit carries the peptidase unit and whose small subunit is shared with calpain-1 (EC 3.4.22.52). It has broad endopeptidase specificity and performs regulatory cleavage of cytoskeletal and focal-adhesion proteins. In animal cells it is activated at the plasma membrane during motility and adhesion. It features a cysteine-protease core with Ca2+-binding EF-hand domains.
References:
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