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ENZYME entry: EC 3.4.22.55

Accepted Name
Caspase-2.
Alternative Name(s)
CASP-2.
ICH-1.
NEDD-2.
NEDD2 protein.
Neural precursor cell expressed developmentally down-regulated protein 2.
Reaction catalysed
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-|-
Comment(s)
  • 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 programed 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.
Cross-references
PROSITEPDOC00864
BRENDA3.4.22.55
EC2PDB3.4.22.55
ExplorEnz3.4.22.55
PRIAM enzyme-specific profiles3.4.22.55
KEGG Ligand Database for Enzyme Nomenclature3.4.22.55
IUBMB Enzyme Nomenclature3.4.22.55
IntEnz3.4.22.55
MEDLINEFind literature relating to 3.4.22.55
MetaCyc3.4.22.55
UniProtKB/Swiss-Prot
Q98943, CASP2_CHICK;  P42575, CASP2_HUMAN;  P29594, CASP2_MOUSE;  
P55215, CASP2_RAT;  

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