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UniProtKB/Swiss-Prot entry P41911


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GPD2_YEAST
Primary accession number P41911
Secondary accession number P50905
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on October 1, 1996 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 83)
Name and origin of the protein
Protein name Glycerol-3-phosphate dehydrogenase [NAD+] 2, mitochondrial [Precursor]
Synonym EC 1.1.1.8
Gene name
Name: GPD2
Synonyms: GPD3
OrderedLocusNames: YOL059W
ORFNames: O1222
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7476212 [NCBI, ExPASy, EBI, Israel, Japan]
Eriksson P., Andre L., Ansell R., Blomberg A., Adler L.;
"Cloning and characterization of GPD2, a second gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) in Saccharomyces cerevisiae, and its comparison with GPD1.";
Mol. Microbiol. 17:95-107(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 90843 / S288c / FY73;
DOI=10.1002/(SICI)1097-0061(199601)12:1<67::AID-YEA884>3.0.CO;2-F; PubMed=8789261 [NCBI, ExPASy, EBI, Israel, Japan]
Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.;
"Analysis of a 26 kb region on the left arm of yeast chromosome XV.";
Yeast 12:67-76(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 90843 / S288c / FY73;
PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
FUNCTION.
PubMed=8979347 [NCBI, ExPASy, EBI, Israel, Japan]
Bjoerkqvist S., Ansell R., Adler L., Liden G.;
"Physiological response to anaerobicity of glycerol-3-phosphate dehydrogenase mutants of Saccharomyces cerevisiae.";
Appl. Environ. Microbiol. 63:128-132(1997).
[6]
INDUCTION.
DOI=10.1093/emboj/16.9.2179; PubMed=9171333 [NCBI, ExPASy, EBI, Israel, Japan]
Ansell R., Granath K., Hohmann S., Thevelein J.M., Adler L.;
"The two isoenzymes for yeast NAD+-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation.";
EMBO J. 16:2179-2187(1997).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, AND MASS SPECTROMETRY.
DOI=10.1038/nbt0302-301; PubMed=11875433 [NCBI, ExPASy, EBI, Israel, Japan]
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M.;
"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae.";
Nat. Biotechnol. 20:301-305(2002).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2135385100; PubMed=14576278 [NCBI, ExPASy, EBI, Israel, Japan]
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[11]
SUBCELLULAR LOCATION, AND INDUCTION.
DOI=10.1074/jbc.M403310200; PubMed=15210723 [NCBI, ExPASy, EBI, Israel, Japan]
Valadi A., Granath K., Gustafsson L., Adler L.;
"Distinct intracellular localization of Gpd1p and Gpd2p, the two yeast isoforms of NAD+-dependent glycerol-3-phosphate dehydrogenase, explains their different contributions to redox-driven glycerol production.";
J. Biol. Chem. 279:39677-39685(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-72 AND SER-75, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-72 AND SER-75, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z35169; CAA84532.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X91067; CAA62526.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74801; CAA99068.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY558560; AAS56886.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S61719; S61719.
RefSeq NP_014582.1; -.
3D structure databases
ModBase P41911.
Protein-protein interaction databases
DIP DIP:1348N; -.
IntAct P41911; -.
Organism-specific databases
CYGD YOL059w; -.
SGD S000005420; GPD2.
Yeast-GFP YOL059W.
Gene expression databases
ArrayExpress P41911; -.
GermOnline YOL059W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from SGD).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0004367; Molecular function: glycerol-3-phosphate dehydrogenase (NAD+) activity (inferred from mutant phenotype from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006071; Biological process: glycerol metabolic process (inferred from mutant phenotype from SGD).
GO:0006116; Biological process: NADH oxidation (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR013328; DHase_multihelical.
IPR016040; NAD(P)-bd.
IPR017751; NAD-dep_Gly3P_DH_euk.
IPR006168; NAD-dep_Gly3P_DHase.
IPR011128; NAD-dep_Gly3P_DHase_N.
IPR006109; NAD_Gly3P_DHase_C.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
PANTHER PTHR11728; NAD_Gly3P_DH; 1.
Pfam PF07479; NAD_Gly3P_dh_C; 1.
PF01210; NAD_Gly3P_dh_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00077; GPDHDRGNASE.
ProDom PD001278; NAD_Gly3P_C; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00957; NAD_G3PDH; 1.
BLOCKS P41911.
ProtoNet P41911.
Proteomic databases
PeptideAtlas P41911; -.
Genome annotation databases
Ensembl YOL059W; Saccharomyces cerevisiae. [Contig view]
GeneID 854095; -.
GenomeReviews Y13140_GR; YOL059W.
KEGG sce:YOL059W; -.
NMPDR fig|4932.3.peg.5674; -.
Phylogenomic databases
HOGENOM P41911; -.
Other
LinkHub P41911; -.
NextBio 975758; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Mitochondrion; NAD; Oxidoreductase; Phosphoprotein; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    16  16     Mitochondrion (Potential). 
CHAIN   17   440  424     Glycerol-3-phosphate dehydrogenase [NAD+] 2, mitochondrial. PRO_0000043410
NP_BIND   90    95  6     NAD (By similarity). 
REGION   359   360  2     Substrate binding (By similarity). 
ACT_SITE   294   294        Proton acceptor (By similarity). 
BINDING   178   178        NAD (By similarity). 
BINDING   201   201        NAD; via amide nitrogen (By similarity). 
BINDING   201   201        Substrate (By similarity). 
BINDING   234   234        NAD; via amide nitrogen (By similarity). 
BINDING   359   359        NAD (By similarity). 
BINDING   388   388        NAD (By similarity). 
MOD_RES   70    70        Phosphoserine. 
MOD_RES   72    72        Phosphoserine. 
MOD_RES   75    75        Phosphoserine. 
Sequence information
Length: 440 AA [This is the length of the unprocessed precursor] Molecular weight: 49422 Da [This is the MW of the unprocessed precursor] CRC64: FA6C07034D3EC720 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLAVRRLTRY TFLKRTHPVL YTRRAYKILP SRSTFLRRSL LQTQLHSKMT AHTNIKQHKH 

        70         80         90        100        110        120 
CHEDHPIRRS DSAVSIVHLK RAPFKVTVIG SGNWGTTIAK VIAENTELHS HIFEPEVRMW 

       130        140        150        160        170        180 
VFDEKIGDEN LTDIINTRHQ NVKYLPNIDL PHNLVADPDL LHSIKGADIL VFNIPHQFLP 

       190        200        210        220        230        240 
NIVKQLQGHV APHVRAISCL KGFELGSKGV QLLSSYVTDE LGIQCGALSG ANLAPEVAKE 

       250        260        270        280        290        300 
HWSETTVAYQ LPKDYQGDGK DVDHKILKLL FHRPYFHVNV IDDVAGISIA GALKNVVALA 

       310        320        330        340        350        360 
CGFVEGMGWG NNASAAIQRL GLGEIIKFGR MFFPESKVET YYQESAGVAD LITTCSGGRN 

       370        380        390        400        410        420 
VKVATYMAKT GKSALEAEKE LLNGQSAQGI ITCREVHEWL QTCELTQEFP LFEAVYQIVY 

       430        440 
NNVRMEDLPE MIEELDIDDE 

P41911 in FASTA format

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