Active Site

Peptidase family C14A, His active site (IPR016129)

Short name: Caspase_his_AS


Interleukin-1 beta converting enzyme (EC: (ICE) [PMID: 7773174, PMID: 7610484] is responsible for the cleavage of the IL-1 beta precursor at an Asp-Ala bond to generate the mature biologically active cytokine. ICE a thiol protease composed of two subunits of 10 (p10) and 20 Kd (p20), both derived by the autocleavage of a 45 Kd precursor (p45). Two residues are implicated in the catalytic mechanism: a cysteine and an histidine. They are located in the P20 subunit after cleavage of the precursor. ICE belongs to a family of peptidases [PMID: 9270303] which is implicated in programmed cell death (apoptosis) and which has been termed 'caspase' for cysteine aspase. ICE is known as Caspase-1 and the other members of this family [PMID: 8861900] include:

  • Caspase-2 (ICH-1, NEDD-2).
  • Caspase-3 (also known as apopain, CPP32, Yama), a protease which, at the onset of apoptosis, proteolytically cleaves poly(ADP-ribose) polymerase at an Asp-Gly bond.
  • Caspase-4 (ICH-2, TX, ICErel-II).
  • Caspase-5 (ICH-3, TY, ICErel-III).
  • Caspase-6 (MCH-2).
  • Caspase-7 (MCH-3, ICE-LAP3, CMH-1, SCA-2, LICE2).
  • Caspase-8 (MCH-5, MACH, FLICE).
  • Caspase-9 (MCH-6, ICE-LAP6).
  • Caspase-10 (MCH-4, FLICE2).
  • Caspase-11.
  • Caspase-12.
  • Caspase-13 (ERICE).
  • Caspase-14.
  • Caenorhabditis elegans ced-3 involved in the initiation of apoptosis.
  • Drosophila Ice.

This entry represents a conserved region containing the histidine active site.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns