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CATH Superfamily 1.10.533.10

Death Domain, Fas

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:

"
Death Domain, Fas
".

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 41: Caspase 9

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-9. [EC: 3.4.22.62]
Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa.
  • Caspase-9 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) 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.
  • An alternatively spliced version of caspase-9 also exists, caspase- 9S, that inhibits apoptosis, similar to the situation found with caspase-2.
  • Phosphorylation of caspase-9 from some species by Akt, a serine- threonine protein kinase, inhibits caspase activity in vitro and caspase activation in vivo.
  • The activity of caspase-9 is increased dramatically upon association with the apoptosome but the enzyme can be activated without proteolytic cleavage.
  • Procaspase-3 is the enzyme's physiological substrate.
  • Belongs to peptidase family C14.
 2 P55211 Q8C3Q9
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