ID   GRE2_YEAST              Reviewed;         342 AA.
AC   Q12068;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=NADPH-dependent methylglyoxal reductase GRE2;
DE            EC=1.1.1.283;
DE   AltName: Full=Genes de respuesta a estres protein 2;
GN   Name=GRE2; OrderedLocusNames=YOL151W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=96132030; PubMed=8553699; DOI=10.1002/yea.320111308;
RA   Casamayor A., Aldea M., Casas C., Herrero E., Gamo F.-J.,
RA   Lafuente M.J., Gancedo C., Arino J.;
RT   "DNA sequence analysis of a 13 kbp fragment of the left arm of yeast
RT   chromosome XV containing seven new open reading frames.";
RL   Yeast 11:1281-1288(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=97313270; PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
RA   Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
RA   Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
RA   Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
RA   Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
RA   Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
RA   Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
RA   Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
RA   Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
RA   Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
RA   Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
RA   Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
RA   Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
RA   Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
RA   Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
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.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=3896793; DOI=10.1111/j.1432-1033.1985.tb09151.x;
RA   Murata K., Fukuda Y., Simosaka M., Watanabe K., Saikusa T., Kimura A.;
RT   "Metabolism of 2-oxoaldehyde in yeasts. Purification and
RT   characterization of NADPH-dependent methylglyoxal-reducing enzyme from
RT   Saccharomyces cerevisiae.";
RL   Eur. J. Biochem. 151:631-636(1985).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=12722185; DOI=10.1002/yea.979;
RA   Chen C.N., Porubleva L., Shearer G., Svrakic M., Holden L.G.,
RA   Dover J.L., Johnston M., Chitnis P.R., Kohl D.H.;
RT   "Associating protein activities with their genes: rapid identification
RT   of a gene encoding a methylglyoxal reductase in the yeast
RT   Saccharomyces cerevisiae.";
RL   Yeast 20:545-554(2003).
RN   [6]
RP   INDUCTION.
RX   MEDLINE=99337886; PubMed=10407268;
RX   DOI=10.1002/(SICI)1097-0061(199907)15:10A<879::AID-YEA428>3.3.CO;2-H;
RA   Garay-Arroyo A., Covarrubias A.A.;
RT   "Three genes whose expression is induced by stress in Saccharomyces
RT   cerevisiae.";
RL   Yeast 15:879-892(1999).
RN   [7]
RP   INDUCTION.
RX   MEDLINE=99278365; PubMed=10347154; DOI=10.1074/jbc.274.23.16040;
RA   Lee J., Godon C., Lagniel G., Spector D., Garin J., Labarre J.,
RA   Toledano M.B.;
RT   "Yap1 and Skn7 control two specialized oxidative stress response
RT   regulons in yeast.";
RL   J. Biol. Chem. 274:16040-16046(1999).
RN   [8]
RP   INDUCTION.
RX   PubMed=11401713; DOI=10.1046/j.1365-2958.2001.02384.x;
RA   Rep M., Proft M., Remize F., Tamas M., Serrano R., Thevelein J.M.,
RA   Hohmann S.;
RT   "The Saccharomyces cerevisiae Sko1p transcription factor mediates HOG
RT   pathway-dependent osmotic regulation of a set of genes encoding
RT   enzymes implicated in protection from oxidative damage.";
RL   Mol. Microbiol. 40:1067-1083(2001).
RN   [9]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923954; 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   [10]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND MASS
RP   SPECTROMETRY.
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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Catalyzes the irreversible reduction of the cytotoxic
CC       compound methylglyoxal (MG) to (R)-lactaldehyde as an alternative
CC       to detoxification of MG by glyoxalase I GLO1. MG is synthesized
CC       via a bypath of glycolysis from dihydroxyacetone phosphate and is
CC       believed to play a role in cell cycle regulation and stress
CC       adaptation.
CC   -!- CATALYTIC ACTIVITY: Lactaldehyde + NADP(+) = methylglyoxal +
CC       NADPH.
CC   -!- ENZYME REGULATION: Activated by glutathione.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- INDUCTION: Repressed by SKO1. During osmotic stress, this
CC       repression is relieved. Induced by transcription factor YAP1
CC       during oxidative stress, and induced by ionic and heat stress.
CC   -!- MISCELLANEOUS: Present with 5458 molecules/cell in log phase SD
CC       medium.
CC   -!- MISCELLANEOUS: 'De respuesta a estres' means stress response in
CC       Spanish.
CC   -!- SIMILARITY: Belongs to the dihydroflavonol-4-reductase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Z48239; CAA88277.1; -; Genomic_DNA.
DR   EMBL; Z74893; CAA99172.1; -; Genomic_DNA.
DR   EMBL; AY558040; AAS56366.1; -; Genomic_DNA.
DR   PIR; S60386; S60386.
DR   RefSeq; NP_014490.1; -.
DR   DIP; DIP:2645N; -.
DR   IntAct; Q12068; 2.
DR   PeptideAtlas; Q12068; -.
DR   Ensembl; YOL151W; Saccharomyces cerevisiae.
DR   GeneID; 854014; -.
DR   GenomeReviews; Y13140_GR; YOL151W.
DR   KEGG; sce:YOL151W; -.
DR   NMPDR; fig|4932.3.peg.5576; -.
DR   CYGD; YOL151w; -.
DR   SGD; S000005511; GRE2.
DR   HOGENOM; Q12068; -.
DR   OMA; Q12068; INPVYVF.
DR   BioCyc; MetaCyc:MON-12909; -.
DR   BRENDA; 1.1.1.283; 250.
DR   NextBio; 975535; -.
DR   GermOnline; YOL151W; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0046568; F:3-methylbutanal reductase activity; IMP:SGD.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0043892; F:methylglyoxal reductase (NADPH-dependent) a...; IDA:SGD.
DR   GO; GO:0008204; P:ergosterol metabolic process; IGI:SGD.
DR   GO; GO:0030447; P:filamentous growth; IMP:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; IEP:SGD.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01370; Epimerase; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; NADP; Nucleus; Oxidoreductase;
KW   Phosphoprotein.
FT   CHAIN         1    342       NADPH-dependent methylglyoxal reductase
FT                                GRE2.
FT                                /FTId=PRO_0000215576.
FT   MOD_RES     333    333       Phosphoserine.
SQ   SEQUENCE   342 AA;  38170 MW;  84DC286AAD8C88D2 CRC64;
     MSVFVSGANG FIAQHIVDLL LKEDYKVIGS ARSQEKAENL TEAFGNNPKF SMEVVPDISK
     LDAFDHVFQK HGKDIKIVLH TASPFCFDIT DSERDLLIPA VNGVKGILHS IKKYAADSVE
     RVVLTSSYAA VFDMAKENDK SLTFNEESWN PATWESCQSD PVNAYCGSKK FAEKAAWEFL
     EENRDSVKFE LTAVNPVYVF GPQMFDKDVK KHLNTSCELV NSLMHLSPED KIPELFGGYI
     DVRDVAKAHL VAFQKRETIG QRLIVSEARF TMQDVLDILN EDFPVLKGNI PVGKPGSGAT
     HNTLGATLDN KKSKKLLGFK FRNLKETIDD TASQILKFEG RI
//