CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.50.1460
Functional Family

Enzyme Information

3.4.22.36
Caspase-1.
based on mapping to UniProt P29466
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.

UniProtKB Entries (1)

P29466
CASP1_HUMAN
Homo sapiens
Caspase-1

PDB Structure

PDB 1SC1
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structures of a ligand-free and malonate-bound human caspase-1: implications for the mechanism of substrate binding.
Romanowski, M.J., Scheer, J.M., O'Brien, T., McDowell, R.S.
Structure