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Glutathione peroxidase-like peroxiredoxin HYR1 (EC 1.11.1.15) (Glutathione peroxidase homolog 3) (GPx 3) (Hydrogen peroxide resistance protein 1) (Oxidant receptor peroxidase 1) (Phospholipid hydroperoxide glutathione peroxidase 3) (PHGPx3)

 GPX3_YEAST              Reviewed;         163 AA.
P40581; D6VVW8;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
18-JUL-2018, entry version 162.
RecName: Full=Glutathione peroxidase-like peroxiredoxin HYR1 {ECO:0000305};
EC=1.11.1.15 {ECO:0000269|PubMed:12437921, ECO:0000269|PubMed:18767166};
AltName: Full=Glutathione peroxidase homolog 3 {ECO:0000303|PubMed:10480913};
Short=GPx 3;
AltName: Full=Hydrogen peroxide resistance protein 1 {ECO:0000303|Ref.1};
AltName: Full=Oxidant receptor peroxidase 1 {ECO:0000303|PubMed:17720812};
AltName: Full=Phospholipid hydroperoxide glutathione peroxidase 3 {ECO:0000303|PubMed:9315326};
Short=PHGPx3;
Name=HYR1 {ECO:0000303|Ref.1};
Synonyms=GPX3 {ECO:0000303|PubMed:10480913},
ORP1 {ECO:0000303|PubMed:17720812};
OrderedLocusNames=YIR037W {ECO:0000312|SGD:S000001476};
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 38626 / AH22 / NRRL Y-12843;
Budde E., Stahl U.;
"Cloning and phenotypic characterization of a glutathione-peroxidase
like gene involved in the oxidative stress response of Saccharomyces
cerevisiae.";
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169870;
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N.,
Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G.,
Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N.,
Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
Nature 387:84-87(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION.
PubMed=9315326;
Ursini F., Maiorino M., Roveri A.;
"Phospholipid hydroperoxide glutathione peroxidase (PHGPx): more than
an antioxidant enzyme?";
Biomed. Environ. Sci. 10:327-332(1997).
[5]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=10480913; DOI=10.1074/jbc.274.38.27002;
Inoue Y., Matsuda T., Sugiyama K., Izawa S., Kimura A.;
"Genetic analysis of glutathione peroxidase in oxidative stress
response of Saccharomyces cerevisiae.";
J. Biol. Chem. 274:27002-27009(1999).
[6]
FUNCTION.
PubMed=11445588; DOI=10.1074/jbc.M105672200;
Avery A.M., Avery S.V.;
"Saccharomyces cerevisiae expresses three phospholipid hydroperoxide
glutathione peroxidases.";
J. Biol. Chem. 276:33730-33735(2001).
[7]
FUNCTION, AND OXIDATION OF YAP1.
PubMed=12437921; DOI=10.1016/S0092-8674(02)01048-6;
Delaunay A., Pflieger D., Barrault M.-B., Vinh J., Toledano M.B.;
"A thiol peroxidase is an H2O2 receptor and redox-transducer in gene
activation.";
Cell 111:471-481(2002).
[8]
FUNCTION, AND INTERACTION WITH YBP1.
PubMed=12743123; DOI=10.1074/jbc.M303542200;
Veal E.A., Ross S.J., Malakasi P., Peacock E., Morgan B.A.;
"Ybp1 is required for the hydrogen peroxide-induced oxidation of the
Yap1 transcription factor.";
J. Biol. Chem. 278:30896-30904(2003).
[9]
FUNCTION, AND ACTIVATING SUBSTANCES.
PubMed=14556853; DOI=10.1016/S0891-5849(03)00434-9;
Azevedo D., Tacnet F., Delaunay A., Rodrigues-Pousada C.,
Toledano M.B.;
"Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals
signaling.";
Free Radic. Biol. Med. 35:889-900(2003).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
FUNCTION.
PubMed=15337745; DOI=10.1074/jbc.M408340200;
Avery A.M., Willetts S.A., Avery S.V.;
"Genetic dissection of the phospholipid hydroperoxidase activity of
yeast gpx3 reveals its functional importance.";
J. Biol. Chem. 279:46652-46658(2004).
[13]
FUNCTION, AND ACTIVE SITE.
PubMed=17720812; DOI=10.1074/jbc.M705953200;
Ma L.H., Takanishi C.L., Wood M.J.;
"Molecular mechanism of oxidative stress perception by the Orp1
protein.";
J. Biol. Chem. 282:31429-31436(2007).
[14]
FUNCTION.
PubMed=19230722; DOI=10.1016/j.chembiol.2009.01.003;
Paulsen C.E., Carroll K.S.;
"Chemical dissection of an essential redox switch in yeast.";
Chem. Biol. 16:217-225(2009).
[15]
SUBCELLULAR LOCATION.
PubMed=22659048; DOI=10.1016/j.bbalip.2012.05.004;
Ohdate T., Inoue Y.;
"Involvement of glutathione peroxidase 1 in growth and peroxisome
formation in Saccharomyces cerevisiae in oleic acid medium.";
Biochim. Biophys. Acta 1821:1295-1305(2012).
[16]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=22984289; DOI=10.1074/mcp.M112.021105;
Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
"Intermembrane space proteome of yeast mitochondria.";
Mol. Cell. Proteomics 11:1840-1852(2012).
[17]
X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS), CATALYTIC ACTIVITY, AND
MUTAGENESIS OF CYS-82.
PubMed=18767166; DOI=10.1002/prot.22220;
Zhang W.J., He Y.-X., Yang Z., Yu J., Chen Y., Zhou C.-Z.;
"Crystal structure of glutathione-dependent phospholipid peroxidase
Hyr1 from the yeast Saccharomyces cerevisiae.";
Proteins 73:1058-1062(2008).
-!- FUNCTION: Involved in oxidative stress response and redox
homeostasis. Functions as a sensor and transducer of hydroperoxide
stress. In response to hydroperoxide stress it oxidizes
(activates) the transcription activator YAP1, which is involved in
transcription activation of genes of the oxidative stress response
pathway. May also play a direct role in hydroperoxide scavenging,
being the most active of three closely related S.cerevisiae
peroxiredoxins (GPX1, GPX2, and HYR1/GPX3) with respect to
peroxide and lipid hydroperoxide reduction. The three enzymes are
not required for the glutaredoxin-mediated antioxidant function.
In the presence of peroxides, HYR1/GPX3 is directly oxidized at
Cys-36 to form a cysteine sulfenic acid (-SOH). Cys-36-SOH then
forms either an intramolecular disulfide bond (Cys-36 with Cys-82)
or a transient, intermolecular disulfide bond with 'Cys-598' of
YAP1, which is further resolved into a YAP1 intramolecular
disulfide bond ('Cys-303' with 'Cys-598'), which causes its
nuclear accumulation and activation, and a reduced Cys-36 in
HYR1/GPX3. {ECO:0000269|PubMed:10480913,
ECO:0000269|PubMed:11445588, ECO:0000269|PubMed:12437921,
ECO:0000269|PubMed:12743123, ECO:0000269|PubMed:14556853,
ECO:0000269|PubMed:15337745, ECO:0000269|PubMed:17720812,
ECO:0000269|PubMed:19230722, ECO:0000269|PubMed:9315326}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:12437921, ECO:0000269|PubMed:18767166}.
-!- SUBUNIT: Interacts with YAP1 and probably YBP1.
{ECO:0000269|PubMed:12743123}.
-!- INTERACTION:
Q96B96:TMEM159 (xeno); NbExp=3; IntAct=EBI-7869, EBI-7055862;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}.
Peroxisome matrix {ECO:0000269|PubMed:22659048}.
-!- INDUCTION: In contrast to the other two peroxiredoxins, HYR1/GPX3
expression is constitutive, not stress-induced.
{ECO:0000269|PubMed:10480913}.
-!- DISRUPTION PHENOTYPE: Sensitive to hydrogen peroxide and tert-
butyl hydroperoxide (t-BHP). {ECO:0000269|PubMed:10480913}.
-!- MISCELLANEOUS: Present with 8000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in
the same subunit to form an intramolecular disulfide.
{ECO:0000305|PubMed:17720812}.
-!- SIMILARITY: Belongs to the glutathione peroxidase family.
{ECO:0000305}.
-!- CAUTION: Was originally thought to be a glutathione peroxidase
(PubMed:10480913) or a phospholipid hydroperoxide glutathione
peroxidase (PubMed:11445588), but functions as an atypical 2-Cys
peroxiredoxin using thioredoxin as reducing power instead
(PubMed:12437921). {ECO:0000305|PubMed:10480913,
ECO:0000305|PubMed:11445588, ECO:0000305|PubMed:12437921}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U22446; AAA64283.1; -; Genomic_DNA.
EMBL; Z38061; CAA86197.1; -; Genomic_DNA.
EMBL; BK006942; DAA08584.1; -; Genomic_DNA.
PIR; S48499; S48499.
RefSeq; NP_012303.1; NM_001179559.1.
PDB; 3CMI; X-ray; 2.02 A; A=1-163.
PDBsum; 3CMI; -.
ProteinModelPortal; P40581; -.
SMR; P40581; -.
BioGrid; 35028; 93.
DIP; DIP-1275N; -.
IntAct; P40581; 16.
MINT; P40581; -.
STRING; 4932.YIR037W; -.
PeroxiBase; 3742; SceGPx03.
iPTMnet; P40581; -.
MaxQB; P40581; -.
PaxDb; P40581; -.
PRIDE; P40581; -.
TopDownProteomics; P40581; -.
EnsemblFungi; YIR037W; YIR037W; YIR037W.
GeneID; 854855; -.
KEGG; sce:YIR037W; -.
EuPathDB; FungiDB:YIR037W; -.
SGD; S000001476; HYR1.
GeneTree; ENSGT00760000119230; -.
HOGENOM; HOG000277054; -.
InParanoid; P40581; -.
KO; K00432; -.
OMA; IAQTCHI; -.
OrthoDB; EOG092C4H0P; -.
BioCyc; YEAST:YIR037W-MONOMER; -.
Reactome; R-SCE-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
Reactome; R-SCE-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
Reactome; R-SCE-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-SCE-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-SCE-74259; Purine catabolism.
Reactome; R-SCE-9018676; Biosynthesis of D-series resolvins.
Reactome; R-SCE-9018896; Biosynthesis of E-series 18(S)-resolvins.
Reactome; R-SCE-9020265; Biosynthesis of aspirin-triggered D-series resolvins.
Reactome; R-SCE-9023661; Biosynthesis of E-series 18(R)-resolvins.
EvolutionaryTrace; P40581; -.
PRO; PR:P40581; -.
Proteomes; UP000002311; Chromosome IX.
GO; GO:0005622; C:intracellular; IPI:SGD.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
GO; GO:0005782; C:peroxisomal matrix; IDA:SGD.
GO; GO:0004602; F:glutathione peroxidase activity; IDA:SGD.
GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IDA:SGD.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
CDD; cd00340; GSH_Peroxidase; 1.
InterPro; IPR000889; Glutathione_peroxidase.
InterPro; IPR029759; GPX_AS.
InterPro; IPR029760; GPX_CS.
InterPro; IPR036249; Thioredoxin-like_sf.
PANTHER; PTHR11592; PTHR11592; 1.
Pfam; PF00255; GSHPx; 1.
PIRSF; PIRSF000303; Glutathion_perox; 1.
PRINTS; PR01011; GLUTPROXDASE.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
1: Evidence at protein level;
3D-structure; Antioxidant; Complete proteome; Cytoplasm;
Disulfide bond; Mitochondrion; Oxidoreductase; Peroxidase; Peroxisome;
Redox-active center; Reference proteome.
CHAIN 1 163 Glutathione peroxidase-like peroxiredoxin
HYR1.
/FTId=PRO_0000066643.
ACT_SITE 36 36 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000269|PubMed:17720812,
ECO:0000305|PubMed:18767166}.
DISULFID 36 82 Redox-active.
{ECO:0000305|PubMed:18767166}.
DISULFID 36 36 Interchain (with C-598 in YAP1);
transient. {ECO:0000269|PubMed:12437921,
ECO:0000269|PubMed:17720812}.
MUTAGEN 82 82 C->S: Loss of enzyme activity.
{ECO:0000269|PubMed:18767166}.
HELIX 3 6 {ECO:0000244|PDB:3CMI}.
HELIX 19 22 {ECO:0000244|PDB:3CMI}.
STRAND 26 36 {ECO:0000244|PDB:3CMI}.
HELIX 39 52 {ECO:0000244|PDB:3CMI}.
HELIX 53 55 {ECO:0000244|PDB:3CMI}.
STRAND 57 64 {ECO:0000244|PDB:3CMI}.
STRAND 97 100 {ECO:0000244|PDB:3CMI}.
HELIX 105 113 {ECO:0000244|PDB:3CMI}.
STRAND 117 119 {ECO:0000244|PDB:3CMI}.
STRAND 129 132 {ECO:0000244|PDB:3CMI}.
STRAND 134 136 {ECO:0000244|PDB:3CMI}.
STRAND 138 142 {ECO:0000244|PDB:3CMI}.
HELIX 148 151 {ECO:0000244|PDB:3CMI}.
HELIX 152 159 {ECO:0000244|PDB:3CMI}.
SEQUENCE 163 AA; 18641 MW; 46C42B81E895C1A3 CRC64;
MSEFYKLAPV DKKGQPFPFD QLKGKVVLIV NVASKCGFTP QYKELEALYK RYKDEGFTII
GFPCNQFGHQ EPGSDEEIAQ FCQLNYGVTF PIMKKIDVNG GNEDPVYKFL KSQKSGMLGL
RGIKWNFEKF LVDKKGKVYE RYSSLTKPSS LSETIEELLK EVE


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