Reaction: Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp
Other name(s): CASP-7; ICE-like apoptotic protease 3; ICE-LAP3; apoptotic protease Mch-3; Mch3; CMH-1
Comments: Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC 188.8.131.52) and caspase-6 (EC 184.108.40.206) . These caspases are responsible for the proteolysis of the majority of cellular polypeptides [e.g. poly(ADP-ribose) polymerase (PARP)], which leads to the apoptotic phenotype . Although a hydrophobic residue at P5 of caspase-2 (EC 220.127.116.11) and caspase-3 leads to more efficient hydrolysis, the amino-acid residue at this location in caspase-7 has no effect . Caspase-7 is activated by the initiator caspases [caspase-8 (EC 18.104.22.168), caspase-9 (EC 22.214.171.124) and caspase-10 (EC 126.96.36.199)]. Removal of the N-terminal prodomain occurs before cleavage in the linker region between the large and small subunits . Belongs in peptidase family C14.
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 189258-14-8
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