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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_HUMAN             Reviewed;         458 AA.
O43464; Q9HBZ4; Q9P0Y3; Q9P0Y4;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 2.
25-OCT-2017, entry version 190.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF SER-306.
PubMed=10644717; DOI=10.1074/jbc.275.4.2581;
Faccio L., Fusco C., Chen A., Martinotti S., Bonventre J.V.,
Zervos A.S.;
"Characterization of a novel human serine protease that has extensive
homology to bacterial heat shock endoprotease HtrA and is regulated by
kidney ischemia.";
J. Biol. Chem. 275:2581-2588(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), AND
CHARACTERIZATION.
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Kidney;
PubMed=10995577; DOI=10.1006/geno.2000.6263;
Faccio L., Fusco C., Viel A., Zervos A.S.;
"Tissue-specific splicing of Omi stress-regulated endoprotease leads
to an inactive protease with a modified PDZ motif.";
Genomics 68:343-347(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 134-458, INTERACTION WITH XIAP, AND MUTAGENESIS OF
ALA-134.
PubMed=11583623; DOI=10.1016/S1097-2765(01)00341-0;
Suzuki Y., Imai Y., Nakayama H., Takahashi K., Takio K., Takahashi R.;
"A serine protease, HtrA2, is released from the mitochondria and
interacts with XIAP, inducing cell death.";
Mol. Cell 8:613-621(2001).
[7]
CHARACTERIZATION.
PubMed=10873535; DOI=10.1006/prep.2000.1240;
Savopoulos J.W., Carter P.S., Turconi S., Pettman G.R., Karran E.H.,
Gray C.W., Ward R.V., Jenkins O., Creasy C.L.;
"Expression, purification, and functional analysis of the human serine
protease HtrA2.";
Protein Expr. Purif. 19:227-234(2000).
[8]
FUNCTION, AND INTERACTION WITH BIRC6/BRUCE.
PubMed=15200957; DOI=10.1016/j.molcel.2004.05.018;
Bartke T., Pohl C., Pyrowolakis G., Jentsch S.;
"Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3
ubiquitin ligase.";
Mol. Cell 14:801-811(2004).
[9]
FUNCTION, AND INTERACTION WITH THAP5.
PubMed=19502560; DOI=10.1152/ajpheart.00234.2009;
Balakrishnan M.P., Cilenti L., Mashak Z., Popat P., Alnemri E.S.,
Zervos A.S.;
"THAP5 is a human cardiac-specific inhibitor of cell cycle that is
cleaved by the proapoptotic Omi/HtrA2 protease during cell death.";
Am. J. Physiol. 297:H643-H653(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-458, SUBUNIT, AND ACTIVE
SITE.
PubMed=11967569; DOI=10.1038/nsb795;
Li W., Srinivasula S.M., Chai J., Li P., Wu J.W., Zhang Z.,
Alnemri E.S., Shi Y.;
"Structural insights into the pro-apoptotic function of mitochondrial
serine protease HtrA2/Omi.";
Nat. Struct. Biol. 9:436-441(2002).
[14]
INVOLVEMENT IN PARK13, VARIANTS SER-141 AND SER-399, AND
CHARACTERIZATION OF VARIANTS SER-141 AND SER-399.
PubMed=15961413; DOI=10.1093/hmg/ddi215;
Strauss K.M., Martins L.M., Plun-Favreau H., Marx F.P., Kautzmann S.,
Berg D., Gasser T., Wszolek Z., Mueller T., Bornemann A., Wolburg H.,
Downward J., Riess O., Schulz J.B., Krueger R.;
"Loss of function mutations in the gene encoding Omi/HtrA2 in
Parkinson's disease.";
Hum. Mol. Genet. 14:2099-2111(2005).
[15]
INVOLVEMENT IN PARK13, VARIANTS PRO-72 AND SER-141, AND VARIANT PARK13
TRP-404.
PubMed=18401856; DOI=10.1002/humu.20713;
Bogaerts V., Nuytemans K., Reumers J., Pals P., Engelborghs S.,
Pickut B., Corsmit E., Peeters K., Schymkowitz J., De Deyn P.P.,
Cras P., Rousseau F., Theuns J., Van Broeckhoven C.;
"Genetic variability in the mitochondrial serine protease HTRA2
contributes to risk for Parkinson disease.";
Hum. Mutat. 29:832-840(2008).
[16]
VARIANTS CYS-12; LEU-128; SER-141; SER-227 AND SER-399.
PubMed=18364387; DOI=10.1093/hmg/ddn096;
Simon-Sanchez J., Singleton A.B.;
"Sequencing analysis of OMI/HTRA2 shows previously reported pathogenic
mutations in neurologically normal controls.";
Hum. Mol. Genet. 17:1988-1993(2008).
[17]
VARIANT SER-399.
PubMed=25422467; DOI=10.1073/pnas.1419581111;
Unal Gulsuner H., Gulsuner S., Mercan F.N., Onat O.E., Walsh T.,
Shahin H., Lee M.K., Dogu O., Kansu T., Topaloglu H., Elibol B.,
Akbostanci C., King M.C., Ozcelik T., Tekinay A.B.;
"Mitochondrial serine protease HTRA2 p.G399S in a kindred with
essential tremor and Parkinson disease.";
Proc. Natl. Acad. Sci. U.S.A. 111:18285-18290(2014).
[18]
INVOLVEMENT IN MGCA8, VARIANT MGCA8 GLN-404, AND CHARACTERIZATION OF
VARIANT MGCA8 GLN-404.
PubMed=27208207; DOI=10.1136/jmedgenet-2016-103922;
Mandel H., Saita S., Edvardson S., Jalas C., Shaag A., Goldsher D.,
Vlodavsky E., Langer T., Elpeleg O.;
"Deficiency of HTRA2/Omi is associated with infantile
neurodegeneration and 3-methylglutaconic aciduria.";
J. Med. Genet. 53:690-696(2016).
[19]
VARIANT SER-399.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
[20]
VARIANT MGCA8 243-LEU-PRO-244 DELINS PRO-SER, AND CHARACTERIZATION OF
VARIANT MGCA8 243-LEU-PRO-244 DELINS PRO-SER.
PubMed=27696117; DOI=10.1007/s10545-016-9977-2;
Olahova M., Thompson K., Hardy S.A., Barbosa I.A., Besse A.,
Anagnostou M.E., White K., Davey T., Simpson M.A., Champion M.,
Enns G., Schelley S., Lightowlers R.N., Chrzanowska-Lightowlers Z.M.,
McFarland R., Deshpande C., Bonnen P.E., Taylor R.W.;
"Pathogenic variants in HTRA2 cause an early-onset mitochondrial
syndrome associated with 3-methylglutaconic aciduria.";
J. Inherit. Metab. Dis. 40:121-130(2017).
-!- 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. Isoform 2 seems to be proteolytically inactive.
{ECO:0000269|PubMed:15200957, ECO:0000269|PubMed:19502560}.
-!- 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. The mature protein, but not the
precursor, binds to BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4.
Interacts with BIRC6/bruce. {ECO:0000269|PubMed:11583623,
ECO:0000269|PubMed:11967569, ECO:0000269|PubMed:15200957,
ECO:0000269|PubMed:19502560}.
-!- INTERACTION:
Q96CA5:BIRC7; NbExp=2; IntAct=EBI-517086, EBI-517623;
P02666:CSN2 (xeno); NbExp=5; IntAct=EBI-517086, EBI-5260183;
Q9P0J0:NDUFA13; NbExp=6; IntAct=EBI-517086, EBI-372742;
Q60855:Ripk1 (xeno); NbExp=2; IntAct=EBI-517086, EBI-529119;
P98170:XIAP; NbExp=18; IntAct=EBI-517086, EBI-517127;
-!- 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 caspase-8
truncated BID/tBID.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=13B;
IsoId=O43464-1; Sequence=Displayed;
Name=2; Synonyms=D-Omi;
IsoId=O43464-2; Sequence=VSP_005359, VSP_005361;
Name=3; Synonyms=p7;
IsoId=O43464-3; Sequence=VSP_005360, VSP_005361;
Name=4; Synonyms=p4;
IsoId=O43464-4; Sequence=VSP_005362;
-!- TISSUE SPECIFICITY: Isoform 1 is ubiquitous. Isoform 2 is
expressed predominantly in the kidney, colon and thyroid.
-!- DOMAIN: The mature N-terminus is involved in the interaction with
XIAP.
-!- DOMAIN: The PDZ domain mediates interaction with MXI2.
-!- PTM: Autoproteolytically activated.
-!- DISEASE: 3-methylglutaconic aciduria 8 (MGCA8) [MIM:617248]: An
autosomal recessive inborn error of metabolism resulting in early
death. Clinical features include extreme hypertonia observed at
birth, alternating with hypotonia, subsequent appearance of
extrapyramidal symptoms, lack of psychomotor development,
microcephaly, and intractable seizures. Patients show lactic
acidemia, 3-methylglutaconic aciduria, intermittent neutropenia,
and progressive brain atrophy. {ECO:0000269|PubMed:27208207,
ECO:0000269|PubMed:27696117}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Parkinson disease 13 (PARK13) [MIM:610297]: A complex
neurodegenerative disorder characterized by bradykinesia, resting
tremor, muscular rigidity and postural instability, as well as by
a clinically significant response to treatment with levodopa. The
pathology involves the loss of dopaminergic neurons in the
substantia nigra and the presence of Lewy bodies (intraneuronal
accumulations of aggregated proteins), in surviving neurons in
various areas of the brain. {ECO:0000269|PubMed:15961413,
ECO:0000269|PubMed:18401856}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HTRA2ID41879ch2p13.html";
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EMBL; AF020760; AAB94569.2; -; mRNA.
EMBL; AF141305; AAF66596.1; -; mRNA.
EMBL; AF141306; AAF66597.1; -; mRNA.
EMBL; AF141307; AAF66598.1; -; mRNA.
EMBL; AF184911; AAG13126.1; -; mRNA.
EMBL; AC006544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000096; AAH00096.1; -; mRNA.
CCDS; CCDS1951.1; -. [O43464-1]
CCDS; CCDS1952.1; -. [O43464-2]
RefSeq; NP_001308656.1; NM_001321727.1. [O43464-3]
RefSeq; NP_037379.1; NM_013247.4. [O43464-1]
RefSeq; NP_659540.1; NM_145074.2. [O43464-2]
UniGene; Hs.469045; -.
UniGene; Hs.744841; -.
PDB; 1LCY; X-ray; 2.00 A; A=134-458.
PDB; 2PZD; X-ray; 2.75 A; A/B=359-458.
PDB; 5FHT; X-ray; 1.95 A; A=134-458.
PDBsum; 1LCY; -.
PDBsum; 2PZD; -.
PDBsum; 5FHT; -.
DisProt; DP00315; -.
ProteinModelPortal; O43464; -.
SMR; O43464; -.
BioGrid; 118165; 70.
CORUM; O43464; -.
ELM; O43464; -.
IntAct; O43464; 43.
MINT; MINT-216075; -.
STRING; 9606.ENSP00000258080; -.
MEROPS; S01.278; -.
iPTMnet; O43464; -.
PhosphoSitePlus; O43464; -.
BioMuta; HTRA2; -.
OGP; O43464; -.
EPD; O43464; -.
MaxQB; O43464; -.
PaxDb; O43464; -.
PeptideAtlas; O43464; -.
PRIDE; O43464; -.
TopDownProteomics; O43464-2; -. [O43464-2]
DNASU; 27429; -.
Ensembl; ENST00000258080; ENSP00000258080; ENSG00000115317. [O43464-1]
Ensembl; ENST00000352222; ENSP00000312893; ENSG00000115317. [O43464-2]
GeneID; 27429; -.
KEGG; hsa:27429; -.
UCSC; uc002smi.2; human. [O43464-1]
CTD; 27429; -.
DisGeNET; 27429; -.
EuPathDB; HostDB:ENSG00000115317.11; -.
GeneCards; HTRA2; -.
GeneReviews; HTRA2; -.
HGNC; HGNC:14348; HTRA2.
HPA; CAB004004; -.
HPA; HPA006602; -.
HPA; HPA027366; -.
MalaCards; HTRA2; -.
MIM; 168600; phenotype.
MIM; 606441; gene.
MIM; 610297; phenotype.
MIM; 617248; phenotype.
neXtProt; NX_O43464; -.
OpenTargets; ENSG00000115317; -.
Orphanet; 2828; Young adult-onset Parkinsonism.
PharmGKB; PA33836; -.
eggNOG; KOG1320; Eukaryota.
eggNOG; COG0265; LUCA.
GeneTree; ENSGT00510000046315; -.
HOGENOM; HOG000223641; -.
HOVERGEN; HBG052044; -.
InParanoid; O43464; -.
KO; K08669; -.
OMA; AHVVINK; -.
OrthoDB; EOG091G0LXR; -.
PhylomeDB; O43464; -.
TreeFam; TF323480; -.
BRENDA; 3.4.21.108; 2681.
SIGNOR; O43464; -.
ChiTaRS; HTRA2; human.
EvolutionaryTrace; O43464; -.
GeneWiki; HtrA_serine_peptidase_2; -.
GenomeRNAi; 27429; -.
PMAP-CutDB; O43464; -.
PRO; PR:O43464; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115317; -.
CleanEx; HS_HTRA2; -.
ExpressionAtlas; O43464; baseline and differential.
Genevisible; O43464; HS.
GO; GO:0035631; C:CD40 receptor complex; ISS:BHF-UCL.
GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:BHF-UCL.
GO; GO:0005856; C:cytoskeleton; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
GO; GO:0005783; C:endoplasmic reticulum; NAS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:MGI.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:1905370; C:serine-type endopeptidase complex; IMP:CAFA.
GO; GO:0042802; F:identical protein binding; IMP:CAFA.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0044257; P:cellular protein catabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:UniProtKB.
GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
GO; GO:0035458; P:cellular response to interferon-beta; IDA:ParkinsonsUK-UCL.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:ParkinsonsUK-UCL.
GO; GO:0071300; P:cellular response to retinoic acid; IDA:ParkinsonsUK-UCL.
GO; GO:0006672; P:ceramide metabolic process; IEA:Ensembl.
GO; GO:0097194; P:execution phase of apoptosis; TAS:UniProtKB.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:ParkinsonsUK-UCL.
GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
GO; GO:0045786; P:negative regulation of cell cycle; TAS:UniProtKB.
GO; GO:1904924; P:negative regulation of mitophagy in response to mitochondrial depolarization; IEA:Ensembl.
GO; GO:1901215; P:negative regulation of neuron death; TAS:ParkinsonsUK-UCL.
GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; NAS:ParkinsonsUK-UCL.
GO; GO:0048666; P:neuron development; IEA:Ensembl.
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; IDA:UniProtKB.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:UniProtKB.
GO; GO:0010822; P:positive regulation of mitochondrion organization; IMP:ParkinsonsUK-UCL.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0016540; P:protein autoprocessing; TAS:ParkinsonsUK-UCL.
GO; GO:0070207; P:protein homotrimerization; IMP:CAFA.
GO; GO:0006508; P:proteolysis; IDA:ParkinsonsUK-UCL.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; TAS:ParkinsonsUK-UCL.
GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
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;
3D-structure; Alternative splicing; Apoptosis; Autocatalytic cleavage;
Complete proteome; Direct protein sequencing; Disease mutation;
Hydrolase; Membrane; Mitochondrion; Neurodegeneration;
Parkinson disease; Parkinsonism; Polymorphism; Protease;
Reference proteome; Serine protease; Transit peptide; Transmembrane;
Transmembrane helix; Zymogen.
TRANSIT 1 31 Mitochondrion.
PROPEP 32 133 {ECO:0000269|PubMed:11583623}.
/FTId=PRO_0000026945.
CHAIN 134 458 Serine protease HTRA2, mitochondrial.
/FTId=PRO_0000026946.
TRANSMEM 105 125 Helical. {ECO:0000255}.
DOMAIN 364 445 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
REGION 166 342 Serine protease.
MOTIF 134 137 IAP-binding motif.
ACT_SITE 198 198 Charge relay system.
{ECO:0000269|PubMed:11967569}.
ACT_SITE 228 228 Charge relay system.
{ECO:0000269|PubMed:11967569}.
ACT_SITE 306 306 Charge relay system.
{ECO:0000269|PubMed:11967569}.
VAR_SEQ 238 302 Missing (in isoform 2).
{ECO:0000303|PubMed:10995577}.
/FTId=VSP_005359.
VAR_SEQ 313 313 L -> LARELGAVSLQ (in isoform 3).
{ECO:0000303|PubMed:10971580}.
/FTId=VSP_005360.
VAR_SEQ 314 458 DGEVIGVNTMKVTAGISFAIPSDRLREFLHRGEKKNSSSGI
SGSQRRYIGVMMLTLSPSILAELQLREPSFPDVQHGVLIHK
VILGSPAHRAGLRPGDVILAIGEQMVQNAEDVYEAVRTQSQ
LAVQIRRGRETLTLYVTPEVTE -> VSETSFLPRIPAPGQ
CGKGRFPLIQGCLVKFLSSSLLAISQYPTRSPQHLLVLLFG
CPHPLLFV (in isoform 4).
{ECO:0000303|PubMed:10971580}.
/FTId=VSP_005362.
VAR_SEQ 372 403 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:10971580,
ECO:0000303|PubMed:10995577}.
/FTId=VSP_005361.
VARIANT 12 12 W -> C (in dbSNP:rs775840965).
{ECO:0000269|PubMed:18364387}.
/FTId=VAR_076967.
VARIANT 72 72 L -> P (in dbSNP:rs150047108).
{ECO:0000269|PubMed:18401856}.
/FTId=VAR_046134.
VARIANT 128 128 P -> L (in dbSNP:rs757704467).
{ECO:0000269|PubMed:18364387}.
/FTId=VAR_076968.
VARIANT 141 141 A -> S (polymorphism; may be a risk
factor for Parkinson disease; reduced
protease activity; dbSNP:rs72470544).
{ECO:0000269|PubMed:15961413,
ECO:0000269|PubMed:18364387,
ECO:0000269|PubMed:18401856}.
/FTId=VAR_027349.
VARIANT 227 227 A -> S (in dbSNP:rs375322953).
{ECO:0000269|PubMed:18364387}.
/FTId=VAR_076969.
VARIANT 243 244 LP -> PS (in MGCA8; loss of protein
expression).
{ECO:0000269|PubMed:27696117}.
/FTId=VAR_077960.
VARIANT 399 399 G -> S (polymorphism; may be a risk
factor for Parkinson disease; reduced
protease activity; dbSNP:rs72470545).
{ECO:0000269|PubMed:15961413,
ECO:0000269|PubMed:18364387,
ECO:0000269|PubMed:25422467,
ECO:0000269|PubMed:27535533}.
/FTId=VAR_027350.
VARIANT 404 404 R -> Q (in MGCA8; may lead to skipping of
exon 7 and the resultant protein may be
truncated; loss of protein expression in
patient cells homozygous for the
mutation; dbSNP:rs767006508).
{ECO:0000269|PubMed:27208207}.
/FTId=VAR_077961.
VARIANT 404 404 R -> W (in PARK13).
{ECO:0000269|PubMed:18401856}.
/FTId=VAR_046135.
MUTAGEN 134 134 A->M: Loss of interaction with XIAP. Loss
of inhibition of XIAP activity.
{ECO:0000269|PubMed:11583623}.
MUTAGEN 306 306 S->A: Loss of protease activity.
{ECO:0000269|PubMed:10644717}.
HELIX 143 147 {ECO:0000244|PDB:5FHT}.
HELIX 149 157 {ECO:0000244|PDB:5FHT}.
HELIX 158 160 {ECO:0000244|PDB:5FHT}.
STRAND 161 170 {ECO:0000244|PDB:5FHT}.
TURN 171 174 {ECO:0000244|PDB:5FHT}.
STRAND 175 188 {ECO:0000244|PDB:5FHT}.
TURN 189 191 {ECO:0000244|PDB:5FHT}.
STRAND 192 195 {ECO:0000244|PDB:5FHT}.
HELIX 197 200 {ECO:0000244|PDB:5FHT}.
STRAND 204 209 {ECO:0000244|PDB:5FHT}.
STRAND 215 224 {ECO:0000244|PDB:5FHT}.
TURN 225 228 {ECO:0000244|PDB:5FHT}.
STRAND 229 233 {ECO:0000244|PDB:5FHT}.
HELIX 248 250 {ECO:0000244|PDB:5FHT}.
STRAND 256 259 {ECO:0000244|PDB:5FHT}.
STRAND 265 268 {ECO:0000244|PDB:5FHT}.
STRAND 271 275 {ECO:0000244|PDB:5FHT}.
STRAND 295 299 {ECO:0000244|PDB:5FHT}.
TURN 303 307 {ECO:0000244|PDB:5FHT}.
STRAND 308 312 {ECO:0000244|PDB:5FHT}.
STRAND 317 326 {ECO:0000244|PDB:5FHT}.
STRAND 329 334 {ECO:0000244|PDB:5FHT}.
HELIX 335 343 {ECO:0000244|PDB:5FHT}.
STRAND 359 361 {ECO:0000244|PDB:5FHT}.
STRAND 364 368 {ECO:0000244|PDB:5FHT}.
HELIX 371 380 {ECO:0000244|PDB:5FHT}.
STRAND 391 396 {ECO:0000244|PDB:5FHT}.
HELIX 401 405 {ECO:0000244|PDB:5FHT}.
STRAND 412 416 {ECO:0000244|PDB:5FHT}.
HELIX 424 433 {ECO:0000244|PDB:5FHT}.
STRAND 435 443 {ECO:0000244|PDB:5FHT}.
STRAND 446 452 {ECO:0000244|PDB:5FHT}.
STRAND 455 457 {ECO:0000244|PDB:5FHT}.
SEQUENCE 458 AA; 48841 MW; CEA955A7D0DD8C0D CRC64;
MAAPRAGRGA GWSLRAWRAL GGIRWGRRPR LTPDLRALLT SGTSDPRARV TYGTPSLWAR
LSVGVTEPRA CLTSGTPGPR AQLTAVTPDT RTREASENSG TRSRAWLAVA LGAGGAVLLL
LWGGGRGPPA VLAAVPSPPP ASPRSQYNFI ADVVEKTAPA VVYIEILDRH PFLGREVPIS
NGSGFVVAAD GLIVTNAHVV ADRRRVRVRL LSGDTYEAVV TAVDPVADIA TLRIQTKEPL
PTLPLGRSAD VRQGEFVVAM GSPFALQNTI TSGIVSSAQR PARDLGLPQT NVEYIQTDAA
IDFGNSGGPL VNLDGEVIGV NTMKVTAGIS FAIPSDRLRE FLHRGEKKNS SSGISGSQRR
YIGVMMLTLS PSILAELQLR EPSFPDVQHG VLIHKVILGS PAHRAGLRPG DVILAIGEQM
VQNAEDVYEA VRTQSQLAVQ IRRGRETLTL YVTPEVTE


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