Reviewed, UniProtKB/Swiss-Prot Q05521 (DPP1_YEAST)

Names and origin

Protein names

Recommended name:
    Diacylglycerol pyrophosphate phosphatase 1
      Short name=DGPP phosphatase
    EC=3.1.3.-
Alternative name(s):
    Phosphatidate phosphatase
    EC=3.1.3.4

Gene names

Name:	DPP1
Synonyms:	ZRG1
Ordered Locus Names:	YDR284C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	289 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the dephosphorylation of diacylglycerol phosphate (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) as a substrate. Substrate preference is DGPP > LPA > PA. Ref.3 Ref.4
Catalytic activity	A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate. Ref.3 Diacylglycerol pyrophosphate + H2O = phosphatidate + phosphate. Ref.3
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 Cu2+ 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. Ref.3 Ref.4
Subcellular location	Vacuole membrane; Multi-pass membrane protein Ref.3 Ref.4 Ref.8.
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. Ref.3 Ref.4 Ref.5 Ref.10
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. Ref.9
Sequence similarities	Belongs to the PA-phosphatase related phosphoesterase family.
Biophysicochemical properties	pH dependence: Optimum pH is 6.0-8.5.

Ontologies

Keywords
Cellular component	Membrane Vacuole
Domain	Transmembrane
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phospholipid metabolic process Inferred from mutant phenotype. Source: SGD signal transduction Ref.7 Traceable author statement. Source: SGD
Cellular component	fungal-type vacuole membrane Ref.4 Inferred from direct assay. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	diacylglycerol pyrophosphate phosphatase activity Ref.3 Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct phosphatidate phosphatase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-2054360,EBI-2054360
FTH1	P38310	1	EBI-2054360,EBI-20959
KEX1	P09620	1	EBI-2054360,EBI-9653
OST1	P41543	1	EBI-2054360,EBI-12651
PMC1	P38929	1	EBI-2054360,EBI-3097
PMP2	P40975	1	EBI-2054360,EBI-2043041

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 289	289	Diacylglycerol pyrophosphate phosphatase 1		PRO_0000220918
Regions
	Topological domain	1 – 21	21	Vacuolar Potential
	Transmembrane	22 – 42	21	1 Potential
	Topological domain	43 – 65	23	Cytoplasmic Potential
	Transmembrane	66 – 86	21	2 Potential
	Topological domain	87 – 92	6	Vacuolar Potential
	Transmembrane	93 – 113	21	3 Potential
	Topological domain	114 – 172	59	Cytoplasmic Potential
	Transmembrane	173 – 193	21	4 Potential
	Transmembrane	194 – 214	21	5 Potential
	Topological domain	215 – 222	8	Cytoplasmic Potential
	Transmembrane	223 – 243	21	6 Potential
	Topological domain	244 – 289	46	Vacuolar Potential
	Region	118 – 126	9	Phosphatase sequence motif I
	Region	166 – 169	4	Phosphatase sequence motif II
	Region	216 – 227	12	Phosphatase sequence motif III
Amino acid modifications
	Modified residue	285	1	Phosphoserine Ref.11 Ref.12 Ref.13
Experimental info
	Mutagenesis	125	1	R → A: Complete loss of DGPP phosphatase activity. Ref.7
	Mutagenesis	169	1	H → A: 91% decrease of DGPP phosphatase activity. Ref.7
	Mutagenesis	223	1	H → A: Complete loss of DGPP phosphatase activity. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q05521-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 9CBEA0D7A0F0E13A	FASTA	289	33,514
	10 20 30 40 50 60 MNRVSFIKTP FNIGAKWRLE DVFLLIIMIL LNYPVYYQQP FERQFYINDL TISHPYATTE 70 80 90 100 110 120 RVNNNMLFVY SFVVPSLTIL IIGSILADRR HLIFILYTSL LGLSLAWFST SFFTNFIKNW 130 140 150 160 170 180 IGRLRPDFLD RCQPVEGLPL DTLFTAKDVC TTKNHERLLD GFRTTPSGHS SESFAGLGYL 190 200 210 220 230 240 YFWLCGQLLT ESPLMPLWRK MVAFLPLLGA ALIALSRTQD YRHHFVDVIL GSMLGYIMAH 250 260 270 280 FFYRRIFPPI DDPLPFKPLM DDSDVTLEEA VTHQRIPDEE LHPLSDEGM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." 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. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." 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. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae." Wu W.-I., Liu Y., Riedel B., Wissing J.B., Fischl A.S., Carman G.M. J. Biol. Chem. 271:1868-1876(1996) [PubMed: 8567632] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
[4]	"Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc." Han G.-S., Johnston C.N., Chen X., Athenstaedt K., Daum G., Carman G.M. J. Biol. Chem. 276:10126-10133(2001) [PubMed: 11139591] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, INDUCTION.
[5]	"Regulation of the yeast DPP1-encoded diacylglycerol pyrophosphate phosphatase by transcription factor Gis1p." Oshiro J., Han G.-S., Iwanyshyn W.M., Conover K., Carman G.M. J. Biol. Chem. 278:31495-31503(2003) [PubMed: 12799368] [Abstract] Cited for: INDUCTION.
[6]	"Vacuole membrane topography of the DPP1-encoded diacylglycerol pyrophosphate phosphatase catalytic site from Saccharomyces cerevisiae." Han G.-S., Johnston C.N., Carman G.M. J. Biol. Chem. 279:5338-5345(2004) [PubMed: 14630917] [Abstract] Cited for: TOPOLOGY, PHOSPHATASE SEQUENCE MOTIF.
[7]	"Mutagenesis of the phosphatase sequence motif in diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae." Toke D.A., McClintick M.L., Carman G.M. Biochemistry 38:14606-14613(1999) [PubMed: 10545184] [Abstract] Cited for: MUTAGENESIS OF ARG-125; HIS-169 AND HIS-223.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Diacylglycerol pyrophosphate phosphatase in Saccharomyces cerevisiae." Oshiro J., Han G.-S., Carman G.M. Biochim. Biophys. Acta 1635:1-9(2003) [PubMed: 14642771] [Abstract] Cited for: REVIEW, INDUCTION.
[11]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, MASS SPECTROMETRY.
[12]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, MASS SPECTROMETRY.
[13]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U51031 Genomic DNA. Translation: AAB64475.1. AY557744 Genomic DNA. Translation: AAS56070.1.
PIR	S70114.
RefSeq	NP_010570.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-8807N.
IntAct	Q05521. 25 interactions.
STRING	Q05521.
Proteomic databases
PeptideAtlas	Q05521.
Genome annotation databases
Ensembl	YDR284C; YDR284C; YDR284C; Saccharomyces cerevisiae. [Genome view]
GeneID	851878.
KEGG	sce:YDR284C.
NMPDR	fig|4932.3.peg.1332.
Organism-specific databases
CYGD	YDR284c.
SGD	S000002692. DPP1.
Phylogenomic databases
eggNOG	fuNOG04236.
HOGENOM	HBG395619.
OMA	VASVCYL.
OrthoDB	EOG97H761.
PhylomeDB	Q05521.
Enzyme and pathway databases
BRENDA	3.1.3.4. 250.
Gene expression databases
ArrayExpress	Q05521.
Genevestigator	Q05521.
GermOnline	YDR284C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000326. P_Acid_Pase_2/haloperoxidase. [Graphical view]
Pfam	PF01569. PAP2. 1 hit. [Graphical view]
SMART	SM00014. acidPPc. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	969841.

Entry information

Entry name

DPP1_YEAST

Accession

Primary (citable) accession number: Q05521

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)