ID   3.4.22.55
DE   caspase-2.
AN   CASP-2.
AN   ICH-1.
AN   NEDD-2.
AN   NEDD2 protein.
AN   neural precursor cell expressed developmentally down-regulated protein 2.
CA   Strict requirement for an Asp residue at P1, with 316-Asp being essential
CA   for proteolytic activity and has a preferred cleavage sequence of Val-
CA   Asp-Val-Ala-Asp-|-.
CC   -!- Caspase-2 is an initiator caspase, as are caspases-8 (EC 3.4.22.61),
CC       caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63).
CC   -!- Contains a caspase-recruitment domain (CARD) in its N-terminal
CC       prodomain, which plays a role in procaspase activation.
CC   -!- Two forms of caspase-2 exist that have antagonistic effects: caspase-
CC       2L induces programed cell death and caspase-2S suppresses cell death.
CC   -!- Caspase-2 is activated by caspase-3 (EC 3.4.22.56), or by a caspase-
CC       3-like protease.
CC   -!- Activation involves cleavage of the N-terminal prodomain, followed by
CC       self-proteolysis between the large and small subunits of pro-caspase-
CC       2 and further proteolysis into smaller fragments.
CC   -!- Proteolysis occurs at Asp residues and the preferred substrate for
CC       this enzyme is a pentapeptide rather than a tetrapeptide.
CC   -!- Apart from itself, the enzyme can cleave golgin-16, which is present
CC       in the Golgi complex and has a cleavage site that is unique for
CC       caspase-2.
CC   -!- alphaII-spectrin, a component of the membrane cytoskeleton, is a
CC       substrate of the large isoform of pro-caspase-2 (caspase-2L) but not
CC       of the short isoform (caspase-2S).
CC   -!- Belongs to peptidase family C14.
DR   Q98943, CASP2_CHICK;  P42575, CASP2_HUMAN;  P29594, CASP2_MOUSE;
DR   P55215, CASP2_RAT  ;
//