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UniProtKB/Swiss-Prot entry Q00055


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

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Entry information
Entry name GPD1_YEAST
Primary accession number Q00055
Secondary accession numbers Q6J5J2 Q6J5J5
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    July 22, 2008 (Entry version 89)
Name and origin of the protein
Protein name Glycerol-3-phosphate dehydrogenase [NAD+] 1
Synonym EC 1.1.1.8
Gene name
Name: GPD1
Synonyms: DAR1, HOR1, OSG1
OrderedLocusNames: YDL022W
ORFNames: D2830
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], AND PROTEIN SEQUENCE OF 30-49.
PubMed=7934860 [NCBI, ExPASy, EBI, Israel, Japan]
Larsson K., Ansell R., Eriksson P., Adler L.;
"A gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) complements an osmosensitive mutant of Saccharomyces cerevisiae.";
Mol. Microbiol. 10:1101-1111(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
PubMed=8196651 [NCBI, ExPASy, EBI, Israel, Japan]
Albertyn J., Hohmann S., Thevelein J.M., Prior B.A.;
"GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway.";
Mol. Cell. Biol. 14:4135-4144(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Diastaticus / ATCC 62933 / NRC 5704 / J132b;
PubMed=7961476 [NCBI, ExPASy, EBI, Israel, Japan]
Wang H.T., Rahaim P., Robbins P., Yocum R.R.;
"Cloning, sequence, and disruption of the Saccharomyces diastaticus DAR1 gene encoding a glycerol-3-phosphate dehydrogenase.";
J. Bacteriol. 176:7091-7095(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-16; ALA-143; PRO-164; SER-183; SER-225 AND VAL-256.
STRAIN=FHS, and WFB;
Ma X., Guo Y., Zhang F., Yu H., Kuang J., Yao J., Li Z., He G.;
"Research on the mechanism of osmotolerance and thermotolerance of yeast.";
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107.
DOI=10.1016/0378-1119(91)90228-4; PubMed=1676389 [NCBI, ExPASy, EBI, Israel, Japan]
Sleep D., Ogden J.E., Roberts N.A., Goodey A.R.;
"Cloning and characterisation of the Saccharomyces cerevisiae glycerol-3-phosphate dehydrogenase (GUT2) promoter.";
Gene 101:89-96(1991).
[7]
PROTEIN SEQUENCE OF 2-19 AND 271-278, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
Bienvenut W.V., Peters C.;
Submitted (JUN-2005) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 8-16; 95-108 AND 160-173.
STRAIN=ATCC 38531 / Y41;
DOI=10.1016/0378-1097(96)00006-7; PubMed=8935650 [NCBI, ExPASy, EBI, Israel, Japan]
Norbeck J., Blomberg A.;
"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae.";
FEMS Microbiol. Lett. 137:1-8(1996).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-27, 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).
[10]
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).
[11]
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).
[12]
SUBCELLULAR LOCATION.
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).
[13]
INDUCTION.
DOI=10.1111/j.1365-2958.2005.04533.x; PubMed=15773992 [NCBI, ExPASy, EBI, Israel, Japan]
Aguilera J., Rodriguez-Vargas S., Prieto J.A.;
"The HOG MAP kinase pathway is required for the induction of methylglyoxal-responsive genes and determines methylglyoxal resistance in Saccharomyces cerevisiae.";
Mol. Microbiol. 56:228-239(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-27, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25 AND SER-27, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-24; SER-25 AND SER-27, 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 0:0-0(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
Z24454; CAA80827.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76859; CAA54189.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U04621; AAA64936.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY598965; AAT27375.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY598968; AAT27378.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z48432; CAA88337.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74071; CAA98582.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M38740; AAA18631.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S40059; S40059.
RefSeq NP_010262.1; -.
3D structure databases
HSSP P90551; 1EVY. [HSSP ENTRY / PDB]
ModBase Q00055.
Protein-protein interaction databases
DIP DIP:6393N; -.
IntAct Q00055; -.
Organism-specific databases
CYGD YDL022w; -.
SGD S000002180; GPD1.
Yeast-GFP YDL022W.
Gene expression databases
ArrayExpress Q00055; -.
GermOnline YDL022W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from SGD).
GO:0005777; Cellular component: peroxisome (inferred from direct assay from SGD).
GO:0004367; Molecular function: glycerol-3-phosphate dehydrogenase (NAD+) activity (inferred from mutant phenotype from SGD).
GO:0006973; Biological process: intracellular accumulation of glycerol (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.
PIRSF PIRSF000114; Glycerol-3-P_dh; 1.
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 Q00055.
Proteomic databases
PeptideAtlas Q00055; -.
Genome annotation databases
Ensembl YDL022W; Saccharomyces cerevisiae. [Contig view]
GeneID 851539; -.
KEGG sce:YDL022W; -.
NMPDR fig|4932.3.peg.1004; -.
Phylogenomic databases
HOGENOM Q00055; -.
Other
LinkHub Q00055; -.
ProtoNet Q00055.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; Peroxisome; Phosphoprotein; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   391  390     Glycerol-3-phosphate dehydrogenase [NAD+] 1. PRO_0000138100
NP_BIND   41    46  6     NAD (By similarity). 
REGION   310   311  2     Substrate binding (By similarity). 
ACT_SITE   245   245        Proton acceptor (By similarity). 
BINDING   129   129        NAD (By similarity). 
BINDING   152   152        NAD; via amide nitrogen (By similarity). 
BINDING   152   152        Substrate (By similarity). 
BINDING   185   185        NAD; via amide nitrogen (By similarity). 
BINDING   310   310        NAD (By similarity). 
BINDING   339   339        NAD (By similarity). 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   12    12        Phosphoserine. 
MOD_RES   23    23        Phosphoserine. 
MOD_RES   24    24        Phosphoserine. 
MOD_RES   25    25        Phosphoserine. 
MOD_RES   27    27        Phosphoserine. 
VARIANT   16    16  1     N -> D (in strain: WFB). 
VARIANT   143   143  1     S -> A (in strain: WFB). 
VARIANT   164   164  1     L -> P (in strain: WFB). 
VARIANT   183   183  1     N -> S (in strain: WFB). 
VARIANT   225   225  1     P -> S (in strain: WFB). 
VARIANT   256   256  1     E -> V (in strain: WFB). 
CONFLICT   103   107        DNLVA -> TIWLL (in Ref. 6; AAA18631). 
Sequence information
Length: 391 AA [This is the length of the unprocessed precursor] Molecular weight: 42869 Da [This is the MW of the unprocessed precursor] CRC64: F5F1F7F111F707D1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSAAADRLNL TSGHLNAGRK RSSSSVSLKA AEKPFKVTVI GSGNWGTTIA KVVAENCKGY 

        70         80         90        100        110        120 
PEVFAPIVQM WVFEEEINGE KLTEIINTRH QNVKYLPGIT LPDNLVANPD LIDSVKDVDI 

       130        140        150        160        170        180 
IVFNIPHQFL PRICSQLKGH VDSHVRAISC LKGFEVGAKG VQLLSSYITE ELGIQCGALS 

       190        200        210        220        230        240 
GANIATEVAQ EHWSETTVAY HIPKDFRGEG KDVDHKVLKA LFHRPYFHVS VIEDVAGISI 

       250        260        270        280        290        300 
CGALKNVVAL GCGFVEGLGW GNNASAAIQR VGLGEIIRFG QMFFPESREE TYYQESAGVA 

       310        320        330        340        350        360 
DLITTCAGGR NVKVARLMAT SGKDAWECEK ELLNGQSAQG LITCKEVHEW LETCGSVEDF 

       370        380        390 
PLFEAVYQIV YNNYPMKNLP DMIEELDLHE D 

Q00055 in FASTA format

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