Calpain-1
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.52 calpain-1
Calpain-1 is a cytosolic Ca2+-dependent cysteine protease of peptidase family C2, requiring micromolar Ca2+ for activity. The active enzyme is a heterodimer in which the large subunit contains the peptidase unit and the small subunit is shared with calpain-2 (EC 3.4.22.53). It has broad endopeptidase specificity and performs limited, regulatory cleavage of cytoskeletal, membrane-associated and signaling proteins. In animal cells it transduces Ca2+ signals into reversible proteolytic modulation. It features a cysteine-protease core flanked by Ca2+-binding domains.
Calpain-1 is a cytosolic Ca2+-dependent cysteine protease of peptidase family C2, requiring micromolar Ca2+ for activity. The active enzyme is a heterodimer in which the large subunit contains the peptidase unit and the small subunit is shared with calpain-2 (EC 3.4.22.53). It has broad endopeptidase specificity and performs limited, regulatory cleavage of cytoskeletal, membrane-associated and signaling proteins. In animal cells it transduces Ca2+ signals into reversible proteolytic modulation. It features a cysteine-protease core flanked by Ca2+-binding domains.
References:
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