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 |
PROSITE | PDOC00864 |
BRENDA | 3.4.22.55 |
EC2PDB | 3.4.22.55 |
ExplorEnz | 3.4.22.55 |
PRIAM enzyme-specific profiles | 3.4.22.55 |
KEGG Ligand Database for Enzyme Nomenclature | 3.4.22.55 |
IUBMB Enzyme Nomenclature | 3.4.22.55 |
IntEnz | 3.4.22.55 |
MEDLINE | Find literature relating to 3.4.22.55 |
MetaCyc | 3.4.22.55 |
Rhea expert-curated reactions | 3.4.22.55 |
UniProtKB/Swiss-Prot |
|
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