KEGG   ENZYME: 3.4.21.108Help
Entry
EC 3.4.21.108               Enzyme                                 

Name
HtrA2 peptidase;
high temperature requirement protein A2;
HtrA2;
Omi stress-regulated endoprotease;
serine proteinase OMI;
HtrA2 protease;
OMI/HtrA2 protease;
HtrA2/Omi;
Omi/HtrA2
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues
Comment
This enzyme is upregulated in mammalian cells in response to stress induced by both heat shock and tunicamycin treatment [4]. It can induce apoptosis in a caspase-independent manner through its peptidase activity and in a caspase-dependent manner by disrupting the interaction between caspase and the inhibitor of apoptosis (IAP) [3]. Belongs in peptidase family S1C.
History
EC 3.4.21.108 created 2006
Orthology
K08669  HtrA serine peptidase 2
Genes
HSA: 27429(HTRA2)
PTR: 459339(HTRA2)
PPS: 100985283(HTRA2)
GGO: 101153780(HTRA2)
PON: 100461940(HTRA2)
NLE: 100591213(HTRA2)
MCC: 709938(HTRA2)
MCF: 102126403(HTRA2)
CSAB: 103220019(HTRA2)
RRO: 104674825(HTRA2)
RBB: 108531686(HTRA2)
CJC: 100385512(HTRA2)
SBQ: 101046884(HTRA2)
MMU: 64704(Htra2)
RNO: 297376(Htra2)
CGE: 100760629(Htra2)
NGI: 103726986(Htra2)
HGL: 101725239(Htra2)
CCAN: 109692441(Htra2)
OCU: 100338967(HTRA2)
TUP: 102501824(HTRA2)
CFA: 475782(HTRA2)
AML: 100471770(HTRA2)
UMR: 103671421(HTRA2)
ORO: 101375505 101382419(HTRA2)
FCA: 768259(HTRA2)
PTG: 102968855(HTRA2)
AJU: 106988577(HTRA2)
BTA: 523039(HTRA2)
BOM: 102273081
BIU: 109565903(HTRA2)
PHD: 102334875(HTRA2)
CHX: 102181963(HTRA2)
OAS: 101120228(HTRA2)
SSC: 100512831(HTRA2)
CFR: 102522927(HTRA2)
CDK: 105105950(HTRA2)
BACU: 103003966(HTRA2)
LVE: 103086746(HTRA2)
OOR: 101276862(HTRA2)
ECB: 100053688(HTRA2)
EPZ: 103557683(HTRA2)
EAI: 106823864(HTRA2)
MYB: 102242360(HTRA2)
MYD: 102772576(HTRA2)
HAI: 109371208(HTRA2)
RSS: 109457409(HTRA2)
PALE: 102890616(HTRA2)
LAV: 100659066(HTRA2)
TMU: 101344176
MDO: 100025882(HTRA2)
SHR: 100923981(HTRA2)
GGA: 395990(HTRA2)
MGP: 100538527(HTRA2)
CJO: 107306835(HTRA2)
APLA: 101802615(HTRA2)
ACYG: 106043211(HTRA2)
TGU: 100220514(HTRA2)
GFR: 102042326(HTRA2)
FAB: 101806812(HTRA2)
PHI: 102107154(HTRA2)
PMAJ: 107203523(HTRA2)
CCAE: 111929153(HTRA2)
CCW: 104690945(HTRA2)
FPG: 101914636(HTRA2)
FCH: 102050387(HTRA2)
CLV: 102085893(HTRA2)
EGZ: 104130002(HTRA2)
AAM: 106487415(HTRA2)
ASN: 102378167(HTRA2)
AMJ: 102573820(HTRA2)
PSS: 102456624(HTRA2)
CMY: 102937290(HTRA2)
CPIC: 101936375(HTRA2)
ACS: 100565079(htra2)
PVT: 110079828(HTRA2)
PBI: 103059726(HTRA2)
GJA: 107110467(HTRA2)
XLA: 108706463(htra2.S)
XTR: 100492982(htra2)
NPR: 108804097
DRE: 100137109(zgc:174193) 560917 797799 799791(si:dkey-33c12.10)
CCAR: 109054998
IPU: 108263241
AMEX: 103043568
TRU: 101079124
LCO: 104921575
NCC: 104960364
MZE: 101482753
OLA: 101174474
XMA: 102226566(htra2)
PRET: 103458895(htra2)
NFU: 107392303
KMR: 108235278(htra2)
CSEM: 103376892
LCF: 108892481
SDU: 111225343
HCQ: 109522905(htra2)
BPEC: 110155255(htra2)
MALB: 109955094
SASA: 106589831
OTW: 112224672
ELS: 105015851
SFM: 108918851(htra2)
LCM: 102356234(HTRA2)
SPU: 756975
APLC: 110973949
SKO: 102807217
DME: Dmel_CG8464(HtrA2)
DSI: Dsimw501_GD20417(Dsim_GD20417)
MDE: 101893592
AAG: 5567933
AME: 551969
BIM: 100747622
BTER: 100651265
SOC: 105199767
AEC: 105152625
ACEP: 105624355
PBAR: 105432441
HST: 105188006
DQU: 106750279
CFO: 105256231
LHU: 105672452
PGC: 109861450
PCF: 106791733
NVI: 100122950
MDL: 103578876
DPA: 109538837
BMOR: 100533207(htra2)
PMAC: 106713982
PRAP: 110994139
HAW: 110379176
PXY: 105386447
CLEC: 106670287
ZNE: 110835296
FCD: 110858213
CRG: 105347711
OBI: 106876978
SHX: MS3_03139
EGL: EGR_02598
EPA: 110232501
ADF: 107348404
HMG: 101239153
CRB: 17883659
BRP: 103874520
BOE: 106306356
THJ: 104802800
LJA: Lj1g3v4921060.1(Lj1g3v4921060.1) Lj1g3v4921060.3(Lj1g3v4921060.3)
MDM: 103414110
RCU: 8287072
JCU: 105647513
OBR: 102706235
ZMA: 100277723(cl62390_1)
SITA: 101768487
APRO: F751_2338
SPAR: SPRG_10340
 » show all
Taxonomy
Reference
1  [PMID:12835328]
  Authors
Srinivasula SM, Gupta S, Datta P, Zhang Z, Hegde R, Cheong N, Fernandes-Alnemri T, Alnemri ES.
  Title
Inhibitor of apoptosis proteins are substrates for the mitochondrial serine protease Omi/HtrA2.
  Journal
J Biol Chem 278:31469-72 (2003)
DOI:10.1074/jbc.C300240200
Reference
2  [PMID:10873535]
  Authors
Savopoulos JW, Carter PS, Turconi S, Pettman GR, Karran EH, Gray CW, Ward RV, Jenkins O, Creasy CL.
  Title
Expression, purification, and functional analysis of the human serine protease HtrA2.
  Journal
Protein Expr Purif 19:227-34 (2000)
DOI:10.1006/prep.2000.1240
  Sequence
[hsa:27429]
Reference
3  [PMID:14512424]
  Authors
Martins LM, Turk BE, Cowling V, Borg A, Jarrell ET, Cantley LC, Downward J.
  Title
Binding specificity and regulation of the serine protease and PDZ domains of HtrA2/Omi.
  Journal
J Biol Chem 278:49417-27 (2003)
DOI:10.1074/jbc.M308659200
  Sequence
[hsa:27429]
Reference
4  [PMID:10971580]
  Authors
Gray CW, Ward RV, Karran E, Turconi S, Rowles A, Viglienghi D, Southan C, Barton A, Fantom KG, West A, Savopoulos J, Hassan NJ, Clinkenbeard H, Hanning C, Amegadzie B, Davis JB, Dingwall C, Livi GP, Creasy CL.
  Title
Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response.
  Journal
Eur J Biochem 267:5699-710 (2000)
DOI:10.1046/j.1432-1327.2000.01589.x
  Sequence
[hsa:27429] [mmu:64704]
Reference
5  [PMID:11967569]
  Authors
Li W, Srinivasula SM, Chai J, Li P, Wu JW, Zhang Z, Alnemri ES, Shi Y.
  Title
Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi.
  Journal
Nat Struct Biol 9:436-41 (2002)
DOI:10.1038/nsb795
  Sequence
[hsa:27429]
Other DBs
ExplorEnz - The Enzyme Database: 3.4.21.108
IUBMB Enzyme Nomenclature: 3.4.21.108
ExPASy - ENZYME nomenclature database: 3.4.21.108
BRENDA, the Enzyme Database: 3.4.21.108

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