CATH Classification

Domain Context

CATH Clusters

Superfamily Caspase-like
Functional Family Putative caspase-2

Enzyme Information
based on mapping to UniProt P42575
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, caspase-9 (EC and caspase-10 (EC -!- 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, 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.

UniProtKB Entries (1)

Homo sapiens

PDB Structure

External Links
Primary Citation
Structural and enzymatic insights into caspase-2 protein substrate recognition and catalysis.
Tang, Y., Wells, J.A., Arkin, M.R.