EC               Enzyme                                 

HtrA2 peptidase;
high temperature requirement protein A2;
Omi stress-regulated endoprotease;
serine proteinase OMI;
HtrA2 protease;
OMI/HtrA2 protease;
Acting on peptide bonds (peptidases);
Serine endopeptidases
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
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.
EC created 2006
K08669  HtrA serine peptidase 2
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)
MCAL: 110295867(Htra2)
MPAH: 110317283(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)
VVP: 112916707(HTRA2)
AML: 100471770(HTRA2)
UMR: 103671421(HTRA2)
UAH: 113243611(HTRA2)
ORO: 101375505 101382419(HTRA2)
ELK: 111148182
FCA: 768259(HTRA2)
PTG: 102968855(HTRA2)
PPAD: 109263345(HTRA2)
AJU: 106988577(HTRA2)
BTA: 523039(HTRA2)
BOM: 102273081
BIU: 109565903(HTRA2)
BBUB: 102389817(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)
DLE: 111169079(HTRA2)
PCAD: 102995172(HTRA2)
ECB: 100053688(HTRA2)
EPZ: 103557683(HTRA2)
EAI: 106823864(HTRA2)
MYB: 102242360(HTRA2)
MYD: 102772576(HTRA2)
MNA: 107529250(HTRA2)
HAI: 109371208(HTRA2)
DRO: 112303094(HTRA2)
PALE: 102890616(HTRA2)
RAY: 107502930(HTRA2)
MJV: 108402276(HTRA2)
LAV: 100659066(HTRA2)
TMU: 101344176
MDO: 100025882(HTRA2)
SHR: 100923981(HTRA2)
PCW: 110221089(HTRA2)
OAA: 114811155(HTRA2)
GGA: 395990(HTRA2)
MGP: 100538527(HTRA2)
CJO: 107306835(HTRA2)
NMEL: 110390926(HTRA2)
ACYG: 106043211(HTRA2)
TGU: 115494796(HTRA2)
LSR: 110468691(HTRA2)
SCAN: 103823115(HTRA2)
GFR: 102042326(HTRA2)
FAB: 101806812(HTRA2)
PHI: 102107154(HTRA2)
PMAJ: 107203523(HTRA2)
CCAE: 111929153(HTRA2)
CCW: 104690945(HTRA2)
ETL: 114068870(HTRA2)
FPG: 101914636(HTRA2)
FCH: 102050387(HTRA2)
CLV: 102085893(HTRA2)
EGZ: 104130002(HTRA2)
NNI: 104013943(HTRA2)
ACUN: 113490506(HTRA2)
PADL: 103922175(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)
PMUR: 107292494(HTRA2)
TSR: 106538932(HTRA2)
PMUA: 114603783(HTRA2)
GJA: 107110467(HTRA2)
XLA: 108706463(htra2.S)
XTR: 100492982(htra2)
NPR: 108804097
DRE: 100137109(zgc:174193) 110438948 110438965 560917 797799 799791(si:dkey-33c12.10)
SGH: 107582530
IPU: 108263241
PHYP: 113539574(htra2)
AMEX: 103043568
EEE: 113585783(htra2)
TRU: 101079124(htra2)
LCO: 104921575
NCC: 104960364
MZE: 101482753
ONL: 100693638
OLA: 101174474
XMA: 102226566(htra2)
XCO: 114134420(htra2)
PRET: 103458895(htra2)
CVG: 107087576
NFU: 107392303
KMR: 108235278
ALIM: 106521377
AOCE: 111578923(htra2)
CSEM: 103376892
POV: 109628063
LCF: 108892481
SDU: 111225343
SLAL: 111651107(htra2)
HCQ: 109522905(htra2)
BPEC: 110155255(htra2)
MALB: 109955094
SASA: 106589831
OTW: 112224672
SALP: 111968136
ELS: 105015851
SFM: 108918851
PKI: 111845796
LCM: 102356234(HTRA2)
BFO: 118413391
APLC: 110973949
SKO: 102807217
DME: Dmel_CG8464(HtrA2)
DER: 6552632
DSE: 6606394
DSI: Dsimw501_GD20417(Dsim_GD20417)
DAN: 6500264
DSR: 110176513
DPE: 6588623
DMN: 108157255
DWI: 6647029
DAZ: 108620802
DNV: 108660102
DHE: 111601551
DVI: 6630732
MDE: 101893592
LCQ: 111675035
AAG: 5567933
AME: 551969
BIM: 100747622
BTER: 100651265
CCAL: 108623857
OBB: 114872063
SOC: 105199767
MPHA: 105830742
AEC: 105152625
ACEP: 105624355
PBAR: 105432441
VEM: 105564315
HST: 105188006
DQU: 106750279
CFO: 105256231
LHU: 105672452
PGC: 109861450
OBO: 105274742
PCF: 106791733
NVI: 100122950
CSOL: 105368312
MDL: 103578876
DPA: 109538837
BMOR: 100533207(htra2)
BMAN: 114248093
PMAC: 106713982
PRAP: 110994139
HAW: 110379176
PXY: 105386447
BTAB: 109042751
CLEC: 106670287
ZNE: 110835296
FCD: 110858213
PVM: 113804151
DPTE: 113798514
CSCU: 111623622
PTEP: 107446348
PCAN: 112565039
CRG: 105347711
OBI: 106876978
LAK: 106151169
SHX: MS3_03139
EGL: EGR_02598
NVE: 116617828
EPA: 110232501
ADF: 107348404
AMIL: 114963716
PDAM: 113671173
SPIS: 111326210
DGT: 114516112
HMG: 101239153
ATH: AT5G27660(DEG14)
CRB: 17883659
BRP: 103874520
BOE: 106306356
THJ: 104802800
CIT: 102608405
GRA: 105792510
GHI: 107894209
GAB: 108468039
DZI: 111293631
GSJ: 114398353
VRA: 106775158
VAR: 108342259
CAM: 101500419
LJA: Lj1g3v4921060.1(Lj1g3v4921060.1) Lj1g3v4921060.2(Lj1g3v4921060.2) Lj1g3v4921060.3(Lj1g3v4921060.3)
ADU: 107492133
AIP: 107645908
LANG: 109329681
PPER: 18772880
PMUM: 103344586
PAVI: 110759195
PXB: 103965318
CSV: 101212324
CMO: 103494739
MCHA: 111018849
CMAX: 111465556
CMOS: 111444435
CPEP: 111798791
RCU: 8287072
JCU: 105647513
HBR: 110659756
MESC: 110620825
POP: 7473270
PEU: 105125071
JRE: 109012743
VVI: 100264796
CANN: 107863029
NSY: 104247943
NTO: 104112327
NAU: 109242764
INI: 109181984
SIND: 105172372
OEU: 111386814
HAN: 110890458
LSV: 111884540
CCAV: 112505655
DCR: 108224612
BVG: 104890298
SOE: 110794681
CQI: 110736872
NNU: 104609043
OSA: 4350193
DOSA: Os11t0246600-00(Os11g0246600)
OBR: 102706235
BDI: 100822885
ATS: 109732288
SBI: 8057143
ZMA: 100277723(cl62390_1)
SITA: 101768487
PDA: 103715494
EGU: 105051535
DCT: 110101476
PEQ: 110033765
AOF: 109827286
ATR: 18448569
PPP: 112283886
APRO: F751_2338
SPAR: SPRG_10340
IDO: I598_0941(htrA_1)
 » show all
1  [PMID:12835328]
Srinivasula SM, Gupta S, Datta P, Zhang Z, Hegde R, Cheong N, Fernandes-Alnemri T, Alnemri ES.
Inhibitor of apoptosis proteins are substrates for the mitochondrial serine protease Omi/HtrA2.
J Biol Chem 278:31469-72 (2003)
2  [PMID:10873535]
Savopoulos JW, Carter PS, Turconi S, Pettman GR, Karran EH, Gray CW, Ward RV, Jenkins O, Creasy CL.
Expression, purification, and functional analysis of the human serine protease HtrA2.
Protein Expr Purif 19:227-34 (2000)
3  [PMID:14512424]
Martins LM, Turk BE, Cowling V, Borg A, Jarrell ET, Cantley LC, Downward J.
Binding specificity and regulation of the serine protease and PDZ domains of HtrA2/Omi.
J Biol Chem 278:49417-27 (2003)
4  [PMID:10971580]
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
Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response.
Eur J Biochem 267:5699-710 (2000)
[hsa:27429] [mmu:64704]
5  [PMID:11967569]
Li W, Srinivasula SM, Chai J, Li P, Wu JW, Zhang Z, Alnemri ES, Shi Y.
Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi.
Nat Struct Biol 9:436-41 (2002)
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