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CATH Superfamily 3.40.50.1460

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: waiting to be named.

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 25: Cell death protein 3

There are 2 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-7. [EC: 3.4.22.60]
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.
  • Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59).
  • These caspases are responsible for the proteolysis of the majority of cellular polypeptides, (e.g. poly(ADP-ribose) polymerase (PARP)), which lead to the apoptotic phenotype.
  • Although a hydrophobic residue at P5 of caspase-2 (EC 3.4.22.55) and caspase-3 leads to more efficient hydrolysis, the amino-acid residue at this location in caspase-7 has no effect.
  • Caspase-7 is activated by the initiator caspases (caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63)).
  • Removal of the N-terminal prodomain occurs before cleavage in the linker region between the large and small subunits.
  • Belongs to peptidase family C14.
 5 A0A2P4W6K8 A0A2P4W6K8 P42573 P45436 P45436
Caspase-1. [EC: 3.4.22.36]
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.
  • Part of the family of inflammatory-caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice.
  • Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation.
  • Cleaves pro-interleukin-1-beta (pro-IL-1-beta) to form mature IL-1- beta, a potent mediator of inflammation.
  • Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-gamma-inducing factor.
  • Inhibited by Ac-Tyr-Val-Ala-Asp-CHO.
  • Caspase-11 plays a critical role in the activation of caspase-1 in mice whereas caspase-4 enhances its activation in humans.
  • Belongs to peptidase family C14.
 1 G5EBM1
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