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Serine protease HTRA2, mitochondrial (EC 3.4.21.108) (High temperature requirement protein A2) (HtrA2) (Omi stress-regulated endoprotease) (Serine protease 25) (Serine proteinase OMI)

 HTRA2_MOUSE             Reviewed;         458 AA.
Q9JIY5; Q9R108;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
27-MAR-2002, sequence version 2.
25-OCT-2017, entry version 153.
RecName: Full=Serine protease HTRA2, mitochondrial;
EC=3.4.21.108;
AltName: Full=High temperature requirement protein A2;
Short=HtrA2;
AltName: Full=Omi stress-regulated endoprotease;
AltName: Full=Serine protease 25;
AltName: Full=Serine proteinase OMI;
Flags: Precursor;
Name=Htra2; Synonyms=Omi, Prss25;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=10971580; DOI=10.1046/j.1432-1327.2000.01589.x;
Gray C.W., Ward R.V., Karran E.H., Turconi S., Rowles A.,
Viglienghi D., Southan C., Barton A., Fantom K.G., West A.,
Savopoulos J.W., Hassan N.J., Clinkenbeard H., Hanning C.,
Amegadzie B., Davis J.B., Dingwall C., Livi G.P., Creasy C.L.;
"Characterization of human HtrA2, a novel serine protease involved in
the mammalian cellular stress response.";
Eur. J. Biochem. 267:5699-5710(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
Faccio L., Fusco C., Zervos A.S.;
"Characterization of the mouse homolog of Omi serine protease.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION IN APOPTOSIS, AND MUTAGENESIS OF ALA-134; ALA-137 AND
SER-306.
PubMed=11604410; DOI=10.1074/jbc.M109891200;
Verhagen A.M., Silke J., Ekert P.G., Pakusch M., Kaufmann H.,
Connolly L.M., Day C.L., Tikoo A., Burke R., Wrobel C., Moritz R.L.,
Simpson R.J., Vaux D.L.;
"HtrA2 promotes cell death through its serine protease activity and
its ability to antagonize inhibitor of apoptosis proteins.";
J. Biol. Chem. 277:445-454(2002).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Serine protease that shows proteolytic activity against
a non-specific substrate beta-casein. Promotes or induces cell
death either by direct binding to and inhibition of BIRC proteins
(also called inhibitor of apoptosis proteins, IAPs), leading to an
increase in caspase activity, or by a BIRC inhibition-independent,
caspase-independent and serine protease activity-dependent
mechanism. Cleaves THAP5 and promotes its degradation during
apoptosis (By similarity). {ECO:0000250,
ECO:0000269|PubMed:11604410}.
-!- CATALYTIC ACTIVITY: 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.
-!- SUBUNIT: Homotrimer. Interacts with MXI2. Interacts with THAP5
under apoptotic conditions (By similarity). The mature protein,
but not the precursor, binds to BIRC2/c-IAP1, BIRC3/c-IAP2 and
XIAP/BIRC4 (By similarity). Interacts with BIRC6/bruce (By
similarity). {ECO:0000250}.
-!- INTERACTION:
O35387:Hax1; NbExp=3; IntAct=EBI-2365838, EBI-642449;
Q99MS3:Mpv17l; NbExp=2; IntAct=EBI-2365838, EBI-15727135;
Q99MS3-1:Mpv17l; NbExp=3; IntAct=EBI-2365838, EBI-15727082;
Q99MS3-3:Mpv17l; NbExp=2; IntAct=EBI-2365838, EBI-15727109;
P98170:XIAP (xeno); NbExp=4; IntAct=EBI-2365838, EBI-517127;
Q60989:Xiap; NbExp=2; IntAct=EBI-2365838, EBI-517478;
-!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein
{ECO:0000305}. Note=Predominantly present in the intermembrane
space. Released into the cytosol following apoptotic stimuli, such
as UV treatment, and stimulation of mitochondria with BID.
-!- DOMAIN: The mature N-terminus is involved in the interaction with
XIAP.
-!- DOMAIN: The PDZ domain mediates interaction with MXI2.
-!- PTM: Autoproteolytically activated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF164513; AAF89534.1; -; mRNA.
EMBL; AF175324; AAD50499.1; -; mRNA.
CCDS; CCDS20267.1; -.
RefSeq; NP_062726.3; NM_019752.3.
UniGene; Mm.21880; -.
ProteinModelPortal; Q9JIY5; -.
SMR; Q9JIY5; -.
BioGrid; 211100; 8.
DIP; DIP-41272N; -.
IntAct; Q9JIY5; 7.
MINT; MINT-219738; -.
STRING; 10090.ENSMUSP00000087073; -.
ChEMBL; CHEMBL3259508; -.
MEROPS; S01.278; -.
iPTMnet; Q9JIY5; -.
PhosphoSitePlus; Q9JIY5; -.
REPRODUCTION-2DPAGE; Q9JIY5; -.
EPD; Q9JIY5; -.
MaxQB; Q9JIY5; -.
PaxDb; Q9JIY5; -.
PeptideAtlas; Q9JIY5; -.
PRIDE; Q9JIY5; -.
Ensembl; ENSMUST00000089645; ENSMUSP00000087073; ENSMUSG00000068329.
GeneID; 64704; -.
KEGG; mmu:64704; -.
UCSC; uc009clu.3; mouse.
CTD; 27429; -.
MGI; MGI:1928676; Htra2.
eggNOG; KOG1320; Eukaryota.
eggNOG; COG0265; LUCA.
GeneTree; ENSGT00510000046315; -.
HOGENOM; HOG000223641; -.
HOVERGEN; HBG052044; -.
InParanoid; Q9JIY5; -.
KO; K08669; -.
OMA; AHVVINK; -.
OrthoDB; EOG091G0LXR; -.
PhylomeDB; Q9JIY5; -.
TreeFam; TF323480; -.
BRENDA; 3.4.21.108; 3474.
PRO; PR:Q9JIY5; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000068329; -.
CleanEx; MM_HTRA2; -.
ExpressionAtlas; Q9JIY5; baseline and differential.
Genevisible; Q9JIY5; MM.
GO; GO:0035631; C:CD40 receptor complex; IDA:BHF-UCL.
GO; GO:0000785; C:chromatin; ISO:MGI.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005856; C:cytoskeleton; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:1905370; C:serine-type endopeptidase complex; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0008233; F:peptidase activity; IMP:ParkinsonsUK-UCL.
GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
GO; GO:0008236; F:serine-type peptidase activity; ISO:MGI.
GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
GO; GO:0007628; P:adult walking behavior; IMP:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0044257; P:cellular protein catabolic process; ISO:MGI.
GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:MGI.
GO; GO:0034605; P:cellular response to heat; ISO:MGI.
GO; GO:0035458; P:cellular response to interferon-beta; ISO:MGI.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:ParkinsonsUK-UCL.
GO; GO:0071300; P:cellular response to retinoic acid; ISO:MGI.
GO; GO:0006672; P:ceramide metabolic process; IEA:Ensembl.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
GO; GO:1904924; P:negative regulation of mitophagy in response to mitochondrial depolarization; IMP:ParkinsonsUK-UCL.
GO; GO:0048666; P:neuron development; IMP:MGI.
GO; GO:0019742; P:pentacyclic triterpenoid metabolic process; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:MGI.
GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
GO; GO:0010822; P:positive regulation of mitochondrion organization; ISO:MGI.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; ISO:MGI.
GO; GO:0070207; P:protein homotrimerization; ISO:MGI.
GO; GO:0006508; P:proteolysis; IMP:ParkinsonsUK-UCL.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
GO; GO:0009635; P:response to herbicide; IEA:Ensembl.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001940; Peptidase_S1C.
Pfam; PF13180; PDZ_2; 1.
PRINTS; PR00834; PROTEASES2C.
SMART; SM00228; PDZ; 1.
SUPFAM; SSF50156; SSF50156; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
Apoptosis; Complete proteome; Hydrolase; Membrane; Mitochondrion;
Protease; Reference proteome; Serine protease; Transit peptide;
Transmembrane; Transmembrane helix; Zymogen.
TRANSIT 1 31 Mitochondrion.
PROPEP 32 133 {ECO:0000255}.
/FTId=PRO_0000026947.
CHAIN 134 458 Serine protease HTRA2, mitochondrial.
/FTId=PRO_0000026948.
TRANSMEM 105 125 Helical. {ECO:0000255}.
DOMAIN 364 446 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
REGION 166 342 Serine protease.
MOTIF 134 137 IAP-binding motif. {ECO:0000250}.
ACT_SITE 198 198 Charge relay system.
{ECO:0000250|UniProtKB:O43464}.
ACT_SITE 228 228 Charge relay system.
{ECO:0000250|UniProtKB:O43464}.
ACT_SITE 306 306 Charge relay system.
{ECO:0000250|UniProtKB:O43464}.
MUTAGEN 134 134 A->G: Loss of interaction with XIAP.
{ECO:0000269|PubMed:11604410}.
MUTAGEN 137 137 A->I: Stronger interaction with XIAP
third BIR domain.
{ECO:0000269|PubMed:11604410}.
MUTAGEN 306 306 S->A: Loss of protease activity.
{ECO:0000269|PubMed:11604410}.
CONFLICT 449 449 T -> I (in Ref. 1; AAF89534).
{ECO:0000305}.
SEQUENCE 458 AA; 49348 MW; C1E77346FB8D75BD CRC64;
MAALKAGRGA NWSLRAWRAL GGIFWRKPPL LAPDLRALLT SGTPDSQIWM TYGTPSLPAQ
VPEGFLASRA DLTSRTPDLW ARLNVGTSGS SDQEARRSPG SRRREWLAVA VGAGGAVVLL
LWGWGRGLST VLAAVPAPPP TSPRSQYNFI ADVVEKTAPA VVYIEILDRH PFSGREVPIS
NGSGFVVASD GLIVTNAHVV ADRRRVRVRL PSGDTYEAMV TAVDPVADIA TLRIQTKEPL
PTLPLGRSAD VRQGEFVVAM GSPFALQNTI TSGIVSSAQR PARDLGLPQN NVEYIQTDAA
IDFGNSGGPL VNLDGEVIGV NTMKVTAGIS FAIPSDRLRE FLHRGEKKNS WFGTSGSQRR
YIGVMMLTLT PSILIELQLR EPSFPDVQHG VLIHKVILGS PAHRAGLRPG DVILAIGEKL
AQNAEDVYEA VRTQSQLAVR IRRGSETLTL YVTPEVTE


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