ID   3.4.22.56
DE   caspase-3.
AN   apopain.
AN   CASP-3.
AN   CPP32.
AN   yama protein.
CA   Strict requirement for an Asp residue at positions P1 and P4. It has a
CA   preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic
CA   amino-acid residue at P2 and a hydrophilic amino-acid residue at P3,
CA   although Val or Ala are also accepted at this position.
CC   -!- Caspase-3 is an effector/executioner caspase, as are caspase-6
CC       (EC 3.4.22.59) and caspase-7 (EC 3.4.22.60).
CC   -!- These caspases are responsible for the proteolysis of the majority of
CC       cellular polypeptides, [e.g. poly(ADP-ribose) polymerase (PARP)],
CC       which leads to the apoptotic phenotype.
CC   -!- Procaspase-3 can be activated by caspase-1 (EC 3.4.22.36), caspase-8
CC       (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10
CC       (EC 3.4.22.63) as well as by the serine protease granzyme B.
CC   -!- Caspase-3 can activate procaspase-2 (EC 3.4.22.55).
CC   -!- Activation occurs by inter-domain cleavage followed by removal of the
CC       N-terminal prodomain.
CC   -!- While Asp-Glu-(Val/Ile)-Asp is thought to be the preferred cleavage
CC       sequence, the enzyme can accommodate different residues at P2 and P3
CC       of the substrate.
CC   -!- Like caspase-2, a hydrophobic residue at P5 of caspase-3 leads to
CC       more efficient hydrolysis, e.g. (Val/Leu)-Asp-Val-Ala-Asp-|- is a
CC       better substrate than Asp-Val-Ala-Asp-|-.
CC   -!- This is not the case for caspase-7.
CC   -!- Belongs to peptidase family C14.
DR   Q08DY9, CASP3_BOVIN;  Q8MKI5, CASP3_CANLF;  Q8MJU1, CASP3_FELCA;
DR   P42574, CASP3_HUMAN;  Q2PFV2, CASP3_MACFA;  Q60431, CASP3_MESAU;
DR   P70677, CASP3_MOUSE;  Q5IS54, CASP3_PANTR;  Q95ND5, CASP3_PIG  ;
DR   Q8MJC3, CASP3_RABIT;  P55213, CASP3_RAT  ;  Q5IS99, CASP3_SAIBB;
DR   P55866, CASP3_XENLA;
//