-!- Caspase-2 is an initiator caspase, as are caspases-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63). -!- Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. -!- Two forms of caspase-2 exist that have antagonistic effects: caspase- 2L induces programd cell death and caspase-2S suppresses cell death. -!- Caspase-2 is activated by caspase-3 (EC 3.4.22.56), or by a caspase- 3-like protease. -!- Activation involves cleavage of the N-terminal prodomain, followed by self-proteolysis between the large and small subunits of pro-caspase- 2 and further proteolysis into smaller fragments. -!- Proteolysis occurs at Asp residues and the preferred substrate for this enzyme is a pentapeptide rather than a tetrapeptide. -!- Apart from itself, the enzyme can cleave golgin-16, which is present in the Golgi complex and has a cleavage site that is unique for caspase-2. -!- Alpha-II-spectrin, a component of the membrane cytoskeleton, is a substrate of the large isoform of pro-caspase-2 (caspase-2L) but not of the short isoform (caspase-2S). -!- Belongs to peptidase family C14.