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CATH Superfamily 3.30.70.1470

Caspase-like

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Caspase-like
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 1: Putative caspase-2

There are 1 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Caspase-2. [EC: 3.4.22.55]
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 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.
 19 A0A0S2Z3H1 A0A0S2Z3H1 A0A0S2Z3H1 A0A0S2Z3H1 A0A2R9A1X3 A0A2R9A1X3 A0A2R9A1X3 A0A2R9A1X3 H2QVJ4 H2QVJ4
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