KEGG   ENZYME: 3.4.22.57Help
Entry
EC 3.4.22.57                Enzyme                                 

Name
caspase-4;
ICErelII;
ICErel-II;
Ich-2;
transcript X;
TX;
TX protease;
caspase 4;
CASP-4
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp! but also cleaves at Asp-Glu-Val-Asp!
Comment
This enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36) 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 [3,5,6]. The enzyme is able to cleave itself and the p30 caspase-1 precursor, but, unlike caspase-1, it is very inefficient at generating mature interleukin-1beta (IL-1beta) from pro-IL-1beta [1,4]. Both this enzyme and caspase-5 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17) [3]. The caspase-1 inhibitor Ac-Tyr-Val-Ala-Asp-CHO can also inhibit this enzyme, but more slowly [4]. Belongs in peptidase family C14.
History
EC 3.4.22.57 created 2007
Orthology
K04394  
caspase 4
Genes
HSA: 
837(CASP4)
PTR: 
451518(CASP4)
PPS: 
100991353(CASP4)
GGO: 
101139012(CASP4)
PON: 
100436933(CASP4)
NLE: 
100587427(CASP4)
MCC: 
704864(CASP4)
MCF: 
102116921(CASP4)
CSAB: 
103248367(CASP4)
RRO: 
CJC: 
100385257(CASP4)
SBQ: 
RNO: 
114555(Casp4)
NGI: 
HGL: 
101700797(Casp4)
OCU: 
100359184(CASP4)
TUP: 
102489894(CASP4)
CFA: 
403724(CASP4)
AML: 
100464921(CASP4)
UMR: 
BTA: 
338039(CASP4)
BOM: 
102272500(CASP1)
OAS: 
SSC: 
100522887(CASP4)
LVE: 
ECB: 
100069303(CASP4)
MYD: 
102774240(CARD16)
PALE: 
LAV: 
MDO: 
SHR: 
 » show all
Taxonomy
Reference
1  [PMID:7743998]
  Authors
Faucheu C, Diu A, Chan AW, Blanchet AM, Miossec C, Herve F, Collard-Dutilleul V, Gu Y, Aldape RA, Lippke JA, et al.
  Title
A novel human protease similar to the interleukin-1 beta converting enzyme induces apoptosis in transfected cells.
  Journal
EMBO. J. 14 (1995) 1914-22.
  Sequence
[hsa:837]
Reference
2  [PMID:7797510]
  Authors
Kamens J, Paskind M, Hugunin M, Talanian RV, Allen H, Banach D, Bump N, Hackett M, Johnston CG, Li P, et al.
  Title
Identification and characterization of ICH-2, a novel member of the interleukin-1 beta-converting enzyme family of cysteine proteases.
  Journal
J. Biol. Chem. 270 (1995) 15250-6.
  Sequence
[hsa:837]
Reference
3  [PMID:16465268]
  Authors
Kamada S, Funahashi Y, Tsujimoto Y.
  Title
Caspase-4 and caspase-5, members of the ICE/CED-3 family of cysteine proteases, are CrmA-inhibitable proteases.
  Journal
Cell. Death. Differ. 4 (1997) 473-8.
Reference
4  [PMID:9578463]
  Authors
Fassy F, Krebs O, Rey H, Komara B, Gillard C, Capdevila C, Yea C, Faucheu C, Blanchet AM, Miossec C, Diu-Hercend A.
  Title
Enzymatic activity of two caspases related to interleukin-1beta-converting enzyme.
  Journal
Eur. J. Biochem. 253 (1998) 76-83.
Reference
5  [PMID:15163405]
  Authors
Martinon F, Tschopp J.
  Title
Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases.
  Journal
Cell. 117 (2004) 561-74.
Reference
6  [PMID:11104820]
  Authors
Chang HY, Yang X.
  Title
Proteases for cell suicide: functions and regulation of caspases.
  Journal
Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
182762-08-9

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