CATH Domain 5k20C00
based on mapping to UniProt P55210
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.
-!- 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 lead 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 to peptidase family C14.
UniProtKB Entries (1)
PAK2 Phosphorylation Inhibits Caspase-7 by Two Divergent Mechanisms: Slowing Activation and Blocking Substrate Binding
To Be Published