ID   GPX2_YEAST              Reviewed;         162 AA.
AC   P38143; D6VQP0;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   02-SEP-2026, entry version 194.
DE   RecName: Full=Glutathione peroxidase-like peroxiredoxin 2 {ECO:0000303|PubMed:10480913};
DE            EC=1.11.1.24 {ECO:0000269|PubMed:16251189};
DE   AltName: Full=Glutathione peroxidase homolog 2 {ECO:0000303|PubMed:10480913};
DE            Short=GPx 2;
GN   Name=GPX2 {ECO:0000303|PubMed:10480913};
GN   OrderedLocusNames=YBR244W {ECO:0000312|SGD:S000000448};
GN   ORFNames=YBR1632;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=10480913; DOI=10.1074/jbc.274.38.27002;
RA   Inoue Y., Matsuda T., Sugiyama K., Izawa S., Kimura A.;
RT   "Genetic analysis of glutathione peroxidase in oxidative stress response of
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 274:27002-27009(1999).
RN   [5]
RP   FUNCTION.
RX   PubMed=11445588; DOI=10.1074/jbc.m105672200;
RA   Avery A.M., Avery S.V.;
RT   "Saccharomyces cerevisiae expresses three phospholipid hydroperoxide
RT   glutathione peroxidases.";
RL   J. Biol. Chem. 276:33730-33735(2001).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   MUTAGENESIS OF CYS-37 AND CYS-83.
RX   PubMed=16251189; DOI=10.1074/jbc.m508622200;
RA   Tanaka T., Izawa S., Inoue Y.;
RT   "GPX2, encoding a phospholipid hydroperoxide glutathione peroxidase
RT   homologue, codes for an atypical 2-Cys peroxiredoxin in Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 280:42078-42087(2005).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=21763276; DOI=10.1016/j.bbrc.2011.06.189;
RA   Ukai Y., Kishimoto T., Ohdate T., Izawa S., Inoue Y.;
RT   "Glutathione peroxidase 2 in Saccharomyces cerevisiae is distributed in
RT   mitochondria and involved in sporulation.";
RL   Biochem. Biophys. Res. Commun. 411:580-585(2011).
CC   -!- FUNCTION: Glutathione peroxidase-like protein that protects cells from
CC       phospholipid hydroperoxides and nonphospholipid peroxides during
CC       oxidative stress (PubMed:10480913, PubMed:11445588). Plays an important
CC       role in the oxidative stress-induced response in the presence of
CC       Ca(2+). Has peroxidase activity using preferentially thioredoxin as a
CC       reducing power. The redox state of the mitochondrial GPX2 is regulated
CC       by TRX1 and TRX2 (cytoplasmic thioredoxin), and by TRX3 (mitochondrial
CC       matrix thioredoxin) (PubMed:16251189). Involved in sporulation
CC       (PubMed:21763276). {ECO:0000269|PubMed:10480913,
CC       ECO:0000269|PubMed:11445588, ECO:0000269|PubMed:16251189,
CC       ECO:0000269|PubMed:21763276}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxide + [thioredoxin]-dithiol = an alcohol +
CC         [thioredoxin]-disulfide + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.24;
CC         Evidence={ECO:0000269|PubMed:16251189};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=170 uM for H(2)O(2) (using glutathione as electron donor)
CC         {ECO:0000269|PubMed:16251189};
CC         KM=313 uM for tert-butyl hydroperoxide (using glutathione as electron
CC         donor) {ECO:0000269|PubMed:16251189};
CC         KM=20 uM for H(2)O(2) (using thioredoxin as electron donor)
CC         {ECO:0000269|PubMed:16251189};
CC         KM=62.5 uM for tert-butyl hydroperoxide (using glutathione as
CC         electron donor) {ECO:0000269|PubMed:16251189};
CC         Vmax=0.27 umol/min/mg enzyme for H(2)O(2) (using glutathione as
CC         electron donor) {ECO:0000269|PubMed:16251189};
CC         Vmax=0.295 umol/min/mg enzyme for tert-butyl hydroperoxide (using
CC         glutathione as electron donor) {ECO:0000269|PubMed:16251189};
CC         Vmax=2.6 umol/min/mg enzyme for H(2)O(2) (using thioredoxin as
CC         electron donor) {ECO:0000269|PubMed:16251189};
CC         Vmax=1 umol/min/mg enzyme for tert-butyl hydroperoxide (using
CC         thioredoxin as electron donor) {ECO:0000269|PubMed:16251189};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16251189}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:21763276}. Nucleus {ECO:0000269|PubMed:14562095}.
CC       Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic
CC       side {ECO:0000269|PubMed:21763276}. Mitochondrion inner membrane;
CC       Peripheral membrane protein; Matrix side {ECO:0000269|PubMed:21763276}.
CC   -!- INDUCTION: By oxidative stress, dependent on transcription factor YAP1
CC       (PubMed:10480913). By oleic acid (PubMed:21763276).
CC       {ECO:0000269|PubMed:10480913, ECO:0000269|PubMed:21763276}.
CC   -!- MISCELLANEOUS: Present with 2010 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC       residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC       attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC       cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC       cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC       bridge. The disulfide is subsequently reduced by an appropriate
CC       electron donor to complete the catalytic cycle. In this atypical 2-Cys
CC       peroxiredoxin, C(R) is present in the same subunit to form an
CC       intramolecular disulfide. {ECO:0000305|PubMed:16251189}.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be a glutathione peroxidase
CC       (PubMed:10480913) or a phospholipid hydroperoxide glutathione
CC       peroxidase (PubMed:11445588), but functions as an atypical 2-Cys
CC       peroxiredoxin using thioredoxin as reducing power instead
CC       (PubMed:16251189). {ECO:0000305|PubMed:10480913,
CC       ECO:0000305|PubMed:11445588, ECO:0000305|PubMed:16251189}.
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DR   EMBL; Z36113; CAA85207.1; -; Genomic_DNA.
DR   EMBL; AY557641; AAS55967.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07360.1; -; Genomic_DNA.
DR   PIR; S46121; S46121.
DR   RefSeq; NP_009803.3; NM_001178592.3.
DR   AlphaFoldDB; P38143; -.
DR   SMR; P38143; -.
DR   BioGRID; 32939; 79.
DR   DIP; DIP-8180N; -.
DR   FunCoup; P38143; 600.
DR   IntAct; P38143; 13.
DR   MINT; P38143; -.
DR   STRING; 4932.YBR244W; -.
DR   PeroxiBase; 3741; SceGPx02.
DR   iPTMnet; P38143; -.
DR   PaxDb; 4932-YBR244W; -.
DR   PeptideAtlas; P38143; -.
DR   EnsemblFungi; YBR244W_mRNA; YBR244W; YBR244W.
DR   GeneID; 852546; -.
DR   KEGG; sce:YBR244W; -.
DR   AGR; SGD:S000000448; -.
DR   SGD; S000000448; GPX2.
DR   VEuPathDB; FungiDB:YBR244W; -.
DR   eggNOG; KOG1651; Eukaryota.
DR   HOGENOM; CLU_029507_2_2_1; -.
DR   InParanoid; P38143; -.
DR   OMA; QCGLTKQ; -.
DR   OrthoDB; 446890at2759; -.
DR   BioCyc; YEAST:YBR244W-MONOMER; -.
DR   BioGRID-ORCS; 852546; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38143; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38143; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IDA:SGD.
DR   GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IDA:SGD.
DR   GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; EXP:UniProtKB.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   FunFam; 3.40.30.10:FF:000010; Glutathione peroxidase; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR029760; GPX_CS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR   PANTHER; PTHR11592:SF78; GLUTATHIONE PEROXIDASE; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   1: Evidence at protein level;
KW   Antioxidant; Cytoplasm; Disulfide bond; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Mitochondrion outer membrane; Nucleus;
KW   Oxidoreductase; Peroxidase; Redox-active center; Reference proteome.
FT   CHAIN           1..162
FT                   /note="Glutathione peroxidase-like peroxiredoxin 2"
FT                   /id="PRO_0000066642"
FT   ACT_SITE        37
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000305|PubMed:16251189"
FT   DISULFID        37..83
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000305|PubMed:16251189"
FT   MUTAGEN         37
FT                   /note="C->A: Prevents oxidation of the protein."
FT                   /evidence="ECO:0000269|PubMed:16251189"
FT   MUTAGEN         83
FT                   /note="C->A: Prevents oxidation of the protein."
FT                   /evidence="ECO:0000269|PubMed:16251189"
SQ   SEQUENCE   162 AA;  18406 MW;  BD02E7E6D38527A6 CRC64;
     MTTSFYDLEC KDKKGESFKF DQLKGKVVLI VNVASKCGFT PQYKELEELY KKYQDKGFVI
     LGFPCNQFGK QEPGSDEQIT EFCQLNYGVT FPIMKKIDVN GSNADSVYNY LKSQKAGLLG
     FKGIKWNFEK FLVDSNGKVV QRFSSLTKPS SLDQEIQSLL SK
//