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Diacylglycerol pyrophosphate phosphatase 1 (DGPP phosphatase) (EC 3.1.3.81) (Phosphatidate phosphatase) (EC 3.1.3.4)

 DPP1_YEAST              Reviewed;         289 AA.
Q05521; D6VSR4;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 142.
RecName: Full=Diacylglycerol pyrophosphate phosphatase 1;
Short=DGPP phosphatase;
EC=3.1.3.81;
AltName: Full=Phosphatidate phosphatase;
EC=3.1.3.4;
Name=DPP1; Synonyms=ZRG1; OrderedLocusNames=YDR284C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
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).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
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).
[4]
FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, AND CATALYTIC
ACTIVITY.
PubMed=8567632; DOI=10.1074/jbc.271.4.1868;
Wu W.-I., Liu Y., Riedel B., Wissing J.B., Fischl A.S., Carman G.M.;
"Purification and characterization of diacylglycerol pyrophosphate
phosphatase from Saccharomyces cerevisiae.";
J. Biol. Chem. 271:1868-1876(1996).
[5]
SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8940025; DOI=10.1074/jbc.271.48.30548;
Dillon D.A., Wu W.I., Riedel B., Wissing J.B., Dowhan W., Carman G.M.;
"The Escherichia coli pgpB gene encodes for a diacylglycerol
pyrophosphate phosphatase activity.";
J. Biol. Chem. 271:30548-30553(1996).
[6]
FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=11139591; DOI=10.1074/jbc.M011421200;
Han G.-S., Johnston C.N., Chen X., Athenstaedt K., Daum G.,
Carman G.M.;
"Regulation of the Saccharomyces cerevisiae DPP1-encoded
diacylglycerol pyrophosphate phosphatase by zinc.";
J. Biol. Chem. 276:10126-10133(2001).
[7]
INDUCTION.
PubMed=12799368; DOI=10.1074/jbc.M305452200;
Oshiro J., Han G.-S., Iwanyshyn W.M., Conover K., Carman G.M.;
"Regulation of the yeast DPP1-encoded diacylglycerol pyrophosphate
phosphatase by transcription factor Gis1p.";
J. Biol. Chem. 278:31495-31503(2003).
[8]
TOPOLOGY, AND PHOSPHATASE SEQUENCE MOTIF.
PubMed=14630917; DOI=10.1074/jbc.M311779200;
Han G.-S., Johnston C.N., Carman G.M.;
"Vacuole membrane topography of the DPP1-encoded diacylglycerol
pyrophosphate phosphatase catalytic site from Saccharomyces
cerevisiae.";
J. Biol. Chem. 279:5338-5345(2004).
[9]
MUTAGENESIS OF ARG-125; HIS-169 AND HIS-223.
PubMed=10545184; DOI=10.1021/bi991472x;
Toke D.A., McClintick M.L., Carman G.M.;
"Mutagenesis of the phosphatase sequence motif in diacylglycerol
pyrophosphate phosphatase from Saccharomyces cerevisiae.";
Biochemistry 38:14606-14613(1999).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
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].
PubMed=14562106; DOI=10.1038/nature02046;
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]
REVIEW, AND INDUCTION.
PubMed=14642771; DOI=10.1016/j.bbalip.2003.10.002;
Oshiro J., Han G.-S., Carman G.M.;
"Diacylglycerol pyrophosphate phosphatase in Saccharomyces
cerevisiae.";
Biochim. Biophys. Acta 1635:1-9(2003).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
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-285, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Catalyzes the dephosphorylation of diacylglycerol
diphosphate (DGPP) to phosphatidate (PA) and the subsequent
dephosphorylation of PA to diacylglycerol (DAG). Together with
LPP1, regulates intracellular DGPP and PA levels, which are
phospholipid molecules believed to play a signaling role in stress
response. Can also use lysophosphatidic acid (LPA) and
phosphatidylglycerophosphate as substrates. Substrate preference
is DGPP > LPA > PA. Activity is independent of a divalent cation
ion and insensitive to inhibition by N-ethylmaleimide.
{ECO:0000269|PubMed:11139591, ECO:0000269|PubMed:8567632}.
-!- CATALYTIC ACTIVITY: 1,2-diacyl-sn-glycerol 3-diphosphate + H(2)O =
1,2-diacyl-sn-glycerol 3-phosphate + phosphate.
{ECO:0000269|PubMed:8567632}.
-!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
1,2-diacyl-sn-glycerol + phosphate. {ECO:0000269|PubMed:8567632}.
-!- ENZYME REGULATION: Inhibited by sodium fluoride (NaF) and
pyrophosphate. Strongly inhibited by manganese ion and, to a lower
extent, by magnesium and calcium ions. Also inhibited by Cu(2+)
ion. In an indirect manner, it is also inhibited by the zinc ion
which is able to form a complex with DGPP and prevent the enzyme
from removing the phosphate from the substrate. Not inhibited by
N-ethylmaleimide. {ECO:0000269|PubMed:11139591,
ECO:0000269|PubMed:8567632}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Vmax=167 umol/min/mg enzyme with lysophosphatidic acid as
substrate {ECO:0000269|PubMed:8940025};
pH dependence:
Optimum pH is 6.0-8.5. {ECO:0000269|PubMed:8940025};
-!- SUBCELLULAR LOCATION: Vacuole membrane
{ECO:0000269|PubMed:11139591, ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:8567632}; Multi-pass membrane protein
{ECO:0000269|PubMed:11139591, ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:8567632}.
-!- INDUCTION: Induced by the transcription factor ZAP1 during zinc
depletion and negatively regulated by the transcription factor
GIS1 predominantly during nutrient limitation. Induced by inositol
supplementation. {ECO:0000269|PubMed:11139591,
ECO:0000269|PubMed:12799368, ECO:0000269|PubMed:14642771}.
-!- DOMAIN: The phosphatase sequence motif I (including Arg-125) and
II (including His-169) are part of the cytoplasmic loop 2 and
phosphatase sequence motif III (including His-223) is part of the
cytoplasmic loop 3.
-!- MISCELLANEOUS: Present with 3038 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U51031; AAB64475.1; -; Genomic_DNA.
EMBL; AY557744; AAS56070.1; -; Genomic_DNA.
EMBL; BK006938; DAA12124.1; -; Genomic_DNA.
PIR; S70114; S70114.
RefSeq; NP_010570.1; NM_001180592.1.
ProteinModelPortal; Q05521; -.
BioGrid; 32337; 61.
DIP; DIP-8807N; -.
IntAct; Q05521; 11.
MINT; MINT-1360992; -.
STRING; 4932.YDR284C; -.
SwissLipids; SLP:000000057; -.
TCDB; 9.B.105.3.2; the lead resistance fusion protein (pbrbc) family.
iPTMnet; Q05521; -.
MaxQB; Q05521; -.
PRIDE; Q05521; -.
TopDownProteomics; Q05521; -.
DNASU; 851878; -.
EnsemblFungi; YDR284C; YDR284C; YDR284C.
GeneID; 851878; -.
KEGG; sce:YDR284C; -.
EuPathDB; FungiDB:YDR284C; -.
SGD; S000002692; DPP1.
GeneTree; ENSGT00510000046723; -.
HOGENOM; HOG000215098; -.
InParanoid; Q05521; -.
KO; K18693; -.
OMA; EMWLYKF; -.
OrthoDB; EOG092C29DM; -.
BioCyc; MetaCyc:YDR284C-MONOMER; -.
BioCyc; YEAST:YDR284C-MONOMER; -.
BRENDA; 3.1.3.81; 984.
Reactome; R-SCE-2029485; Role of phospholipids in phagocytosis.
PRO; PR:Q05521; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; IDA:SGD.
GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:SGD.
GO; GO:0006644; P:phospholipid metabolic process; IMP:SGD.
InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
Pfam; PF01569; PAP2; 1.
SMART; SM00014; acidPPc; 1.
SUPFAM; SSF48317; SSF48317; 1.
1: Evidence at protein level;
Complete proteome; Hydrolase; Membrane; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Vacuole.
CHAIN 1 289 Diacylglycerol pyrophosphate phosphatase
1.
/FTId=PRO_0000220918.
TOPO_DOM 1 21 Vacuolar. {ECO:0000255}.
TRANSMEM 22 42 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 43 65 Cytoplasmic. {ECO:0000255}.
TRANSMEM 66 86 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 87 92 Vacuolar. {ECO:0000255}.
TRANSMEM 93 113 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 114 172 Cytoplasmic. {ECO:0000255}.
TRANSMEM 173 193 Helical; Name=4. {ECO:0000255}.
TRANSMEM 194 214 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 215 222 Cytoplasmic. {ECO:0000255}.
TRANSMEM 223 243 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 244 289 Vacuolar. {ECO:0000255}.
REGION 118 126 Phosphatase sequence motif I.
REGION 166 169 Phosphatase sequence motif II.
REGION 216 227 Phosphatase sequence motif III.
MOD_RES 285 285 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MUTAGEN 125 125 R->A: Complete loss of DGPP phosphatase
activity. {ECO:0000269|PubMed:10545184}.
MUTAGEN 169 169 H->A: 91% decrease of DGPP phosphatase
activity. {ECO:0000269|PubMed:10545184}.
MUTAGEN 223 223 H->A: Complete loss of DGPP phosphatase
activity. {ECO:0000269|PubMed:10545184}.
SEQUENCE 289 AA; 33514 MW; 9CBEA0D7A0F0E13A CRC64;
MNRVSFIKTP FNIGAKWRLE DVFLLIIMIL LNYPVYYQQP FERQFYINDL TISHPYATTE
RVNNNMLFVY SFVVPSLTIL IIGSILADRR HLIFILYTSL LGLSLAWFST SFFTNFIKNW
IGRLRPDFLD RCQPVEGLPL DTLFTAKDVC TTKNHERLLD GFRTTPSGHS SESFAGLGYL
YFWLCGQLLT ESPLMPLWRK MVAFLPLLGA ALIALSRTQD YRHHFVDVIL GSMLGYIMAH
FFYRRIFPPI DDPLPFKPLM DDSDVTLEEA VTHQRIPDEE LHPLSDEGM


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