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ENZYME entry: EC 184.108.40.206
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|Neural precursor cell expressed developmentally down-regulated protein 2.|
|Strict requirement for an Asp residue at P1, with 316-asp being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-|
- Caspase-2 is an initiator caspase, as are caspases-8 (EC 220.127.116.11),
caspase-9 (EC 18.104.22.168) and caspase-10 (EC 22.214.171.124).
- 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 126.96.36.199), or by a caspase-
- 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
- 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.
|PRIAM enzyme-specific profiles||188.8.131.52|
|KEGG Ligand Database for Enzyme Nomenclature||184.108.40.206|
|IUBMB Enzyme Nomenclature||220.127.116.11|
|MEDLINE||Find literature relating to 18.104.22.168|
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