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) 101139367
PON: 100436933
NLE: 100587427(CASP4)
MCC: 704864(CASP4)
MCF: 102116921(CASP4)
CSAB: 103248367(CASP4)
RRO: 104665269
RBB: 108513171
CJC: 100385257(CASP4)
SBQ: 101048389
MMU: 12363(Casp4)
RNO: 114555(Casp4)
NGI: 103743234(Casp4)
HGL: 101700797(Casp4)
CCAN: 109694936
OCU: 100358658 100359184(CASP4)
TUP: 102468460 102489894(CASP4)
CFA: 403724(CASP4)
AML: 100464921(CASP4)
UMR: 103662442
ORO: 101382016
FCA: 493961(CASP4)
PTG: 102967742
AJU: 106976501
BTA: 338039(CASP4)
BOM: 102272500(CASP1)
BIU: 109569831
PHD: 102340851
CHX: 102191717(CASP1)
OAS: 101117272
SSC: 100522887
CDK: 105100419
BACU: 103012084
LVE: 103078575
OOR: 101290090
ECB: 100069303(CASP4) 100069322
MYD: 102769995
LAV: 100661933
MDO: 100032600
 » 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 14:1914-22 (1995)
  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 270:15250-6 (1995)
DOI:10.1074/jbc.270.25.15250
  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 4:473-8 (1997)
DOI:10.1038/sj.cdd.4400268
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 253:76-83 (1998)
DOI:10.1046/j.1432-1327.1998.2530076.x
Reference
5  [PMID:15163405]
  Authors
Martinon F, Tschopp J.
  Title
Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases.
  Journal
Cell 117:561-74 (2004)
DOI:10.1016/j.cell.2004.05.004
Reference
6  [PMID:11104820]
  Authors
Chang HY, Yang X.
  Title
Proteases for cell suicide: functions and regulation of caspases.
  Journal
Microbiol Mol Biol Rev 64:821-46 (2000)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.22.57
IUBMB Enzyme Nomenclature: 3.4.22.57
ExPASy - ENZYME nomenclature database: 3.4.22.57
BRENDA, the Enzyme Database: 3.4.22.57
CAS: 182762-08-9

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