GPX2_YEAST
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 03-AUG-2022, entry version 179.
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}; 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=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + 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; 77.
DR DIP; DIP-8180N; -.
DR IntAct; P38143; 12.
DR MINT; P38143; -.
DR STRING; 4932.YBR244W; -.
DR PeroxiBase; 3741; SceGPx02.
DR iPTMnet; P38143; -.
DR MaxQB; P38143; -.
DR PaxDb; P38143; -.
DR PRIDE; P38143; -.
DR EnsemblFungi; YBR244W_mRNA; YBR244W; YBR244W.
DR GeneID; 852546; -.
DR KEGG; sce:YBR244W; -.
DR SGD; S000000448; GPX2.
DR VEuPathDB; FungiDB:YBR244W; -.
DR eggNOG; KOG1651; Eukaryota.
DR GeneTree; ENSGT00940000165680; -.
DR HOGENOM; CLU_029507_2_2_1; -.
DR InParanoid; P38143; -.
DR OMA; LAPFKGQ; -.
DR BioCyc; YEAST:YBR244W-MON; -.
DR PRO; PR:P38143; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38143; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:SGD.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR CDD; cd00340; GSH_Peroxidase; 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; PTHR11592; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; SSF52833; 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
