KEGG   ENZYME: 3.4.22.57
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
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
HSA837(CASP4)
PTR451518(CASP4)
PPS100991353
GGO101139012 101139367
PON100436933
NLE100587427(CASP4)
HMH116476873
MCC704864(CASP4)
MCF102116921(CASP4)
MTHB126936246
MNI105493691
CSAB103248367(CASP4)
CATY105588758(CASP4)
PANU101005674
TGE112605779
MLEU105534144
RRO104665269(CASP4)
RBB108513171
TFN117080360
PTEH111540081
CANG105500954(CASP4)
CJC100385257
SBQ101048389
CIMI108315451
CSYR103267241 103267244
MMUR105862461 105862471
LCAT123641867 123641987
PCOQ105822166 105822168(CASP5)
OGA100953733 105888133(CASP4)
MMU12363(Casp4)
MCAL110301962
MPAH110328019(Casp4)
RNO114555(Casp4)
MCOC116072580(Casp4)
ANU117699797(Casp4)
NGI103743234(Casp4)
HGL101700797(Casp4)
CPOC100731032
CCAN109694936
DORD105980799(Casp5)
PLOP125349534
NCAR124960571 124960664
MMMA107145708 107145896
OCU100359184
OPI101530447 101530693
TUP102468460 102489894(CASP4)
GVR103595948
CFA403724(CASP4)
CLUD112671423(CASP4)
VVP112925945
VLG121501029
NPO129496568
AML100464921
UMR103662442
UAH113260124
UAR123792513
ELK111153907
LLV125078537
MPUF101686692
MNP132029007
MLK131834822
NVS122912246
ORO101382016
EJU114211414
ZCA113913479
MLX118013165
NSU110586195
LWW102743984(CASP4)
FCA493961(CASP4)
PYU121020795(CASP4)
PCOO112866024
PBG122482901
PVIV125177253
LRUF124505860
PTG102967742
PPAD109258467
PUC125910505
AJU106976501
HHV120246763
BTA338039(CASP4)
BOM102272500(CASP1)
BIU109569831
BBUB102394992
BBIS104983676
CHX102191717
OAS101117272
BTAX128060611
ODA120876144
CCAD122449950
MBEZ129554237
SSC100522887
CFR116656626
CBAI105067588
CDK105100419
VPC102540860
BACU103012084
BMUS118899368
LVE103078575
OOR101290090
DLE111167555
PCAD102987795
PSIU116757817(CASP4)
NASI112415742
ECB100069303(CASP4) 100069322
EPZ103559837 103559840
EAI106837655(CASP4) 106837665
MYB102257847 102260720 106726136 106726185
MYD102769995
MMYO118664119 118664385 118664387
MLF102423287 102430359 102430672 102430997
PKL118712751 118713780
EFUS103299257 103303785 114227918
MNA107532382
DRO112314268 112314306 112314322
SHON118988282
AJM119060734 119060770 119060787
PDIC114498810 114499617(CASP4) 114499889
PHAS123818755 123819792 123819902
MMF118627675 118628466 118628467
PPAM129086065 129086111
HAI109377696 109377700
RFQ117029841 117030503
PALE102887403 102895641
PGIG120599660 120599679
PVP105297443 105297474
RAY107504289 107504294
MJV108385984(CASP1) 118966797
TOD119242137 119242138 119242139
SARA105942813
LAV100661933
TMU101352905 101353422 101353932
ETF101653056
DNM101418845(CASP4) 101425305
MDO100032600
GAS123239006
SHR100914126 100914382
AFZ127554936 127554937 127554939 127554940
PCW110215002 110215005
PRET103474727
LCF108900839
ARUT117413658 117962789
CCRN123294631
 » show all
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)
DOI:10.1002/j.1460-2075.1995.tb07183.x
  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)
DOI:10.1128/mmbr.64.4.821-846.2000
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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