ID 3.4.22.60 DE caspase-7. AN apoptotic protease Mch-3. AN CASP-7. AN CMH-1. AN ICE-LAP3. AN ICE-like apoptotic protease 3. AN Mch3. CA Strict requirement for an Asp residue at position P1 and has a preferred CA cleavage sequence of Asp-Glu-Val-Asp-|-. CC -!- Caspase-7 is an effector/executioner caspase, as are caspase-3 CC (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59). CC -!- These caspases are responsible for the proteolysis of the majority of CC cellular polypeptides, [e.g. poly(ADP-ribose) polymerase (PARP)], CC which lead to the apoptotic phenotype. CC -!- Although a hydrophobic residue at P5 of caspase-2 (EC 3.4.22.55) and CC caspase-3 leads to more efficient hydrolysis, the amino-acid residue CC at this location in caspase-7 has no effect. CC -!- Caspase-7 is activated by the initiator caspases [caspase-8 CC (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 CC (EC 3.4.22.63)]. CC -!- Removal of the N-terminal prodomain occurs before cleavage in the CC linker region between the large and small subunits. CC -!- Belongs to peptidase family C14. DR F1NV61, CASP7_CHICK; P55210, CASP7_HUMAN; P55214, CASP7_MESAU; DR P97864, CASP7_MOUSE; P42573, CED3_CAEEL ; P45436, CED3_CAERE ; //