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Q05521 (DPP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Diacylglycerol pyrophosphate phosphatase 1
Short name=DGPP phosphatase
EC=3.1.3.81
Alternative name(s):
Phosphatidate phosphatase
EC=3.1.3.4
Gene names
Name:DPP1
Synonyms:ZRG1
Ordered Locus Names:YDR284C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4 Ref.6

Catalytic activity

1,2-diacyl-sn-glycerol 3-diphosphate + H2O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate. Ref.4

A 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate. Ref.4

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.4 Ref.6

Subcellular location

Vacuole membrane; Multi-pass membrane protein Ref.4 Ref.6 Ref.10.

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.4 Ref.6 Ref.7 Ref.12

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.

Sequence similarities

Belongs to the PA-phosphatase related phosphoesterase family.

Biophysicochemical properties

Kinetic parameters:

Vmax=167 µmol/min/mg enzyme with lysophosphatidic acid as substrate Ref.5

pH dependence:

Optimum pH is 6.0-8.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 289289Diacylglycerol pyrophosphate phosphatase 1
PRO_0000220918

Regions

Topological domain1 – 2121Vacuolar Potential
Transmembrane22 – 4221Helical; Name=1; Potential
Topological domain43 – 6523Cytoplasmic Potential
Transmembrane66 – 8621Helical; Name=2; Potential
Topological domain87 – 926Vacuolar Potential
Transmembrane93 – 11321Helical; Name=3; Potential
Topological domain114 – 17259Cytoplasmic Potential
Transmembrane173 – 19321Helical; Name=4; Potential
Transmembrane194 – 21421Helical; Name=5; Potential
Topological domain215 – 2228Cytoplasmic Potential
Transmembrane223 – 24321Helical; Name=6; Potential
Topological domain244 – 28946Vacuolar Potential
Region118 – 1269Phosphatase sequence motif I
Region166 – 1694Phosphatase sequence motif II
Region216 – 22712Phosphatase sequence motif III

Amino acid modifications

Modified residue2851Phosphoserine Ref.13 Ref.14 Ref.15

Experimental info

Mutagenesis1251R → A: Complete loss of DGPP phosphatase activity. Ref.9
Mutagenesis1691H → A: 91% decrease of DGPP phosphatase activity. Ref.9
Mutagenesis2231H → A: Complete loss of DGPP phosphatase activity. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Q05521 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 9CBEA0D7A0F0E13A

FASTA28933,514
        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

« Hide

References

« Hide '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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
[5]"The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity."
Dillon D.A., Wu W.I., Riedel B., Wissing J.B., Dowhan W., Carman G.M.
J. Biol. Chem. 271:30548-30553(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, INDUCTION.
[7]"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] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[8]"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] [Europe PMC] [Abstract]
Cited for: TOPOLOGY, PHOSPHATASE SEQUENCE MOTIF.
[9]"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] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-125; HIS-169 AND HIS-223.
[10]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]"Diacylglycerol pyrophosphate phosphatase in Saccharomyces cerevisiae."
Oshiro J., Han G.-S., Carman G.M.
Biochim. Biophys. Acta 1635:1-9(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, INDUCTION.
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, MASS SPECTROMETRY.
Strain: YAL6B.
[14]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, MASS SPECTROMETRY.
Strain: ADR376.
[15]"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] [Europe PMC] [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.
BK006938 Genomic DNA. Translation: DAA12124.1.
PIRS70114.
RefSeqNP_010570.1. NM_001180592.1.

3D structure databases

ProteinModelPortalQ05521.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-8807N.
IntActQ05521. 10 interactions.
MINTMINT-1360992.
STRING4932.YDR284C.

Proteomic databases

PaxDbQ05521.
PeptideAtlasQ05521.

Protocols and materials databases

DNASU851878.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR284C; YDR284C; YDR284C.
GeneID851878.
KEGGsce:YDR284C.

Organism-specific databases

CYGDYDR284c.
SGDS000002692. DPP1.

Phylogenomic databases

eggNOGCOG0671.
GeneTreeENSGT00510000046723.
HOGENOMHOG000215098.
OMAPFERQFY.
OrthoDBEOG43NBNX.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15445.

Gene expression databases

GenevestigatorQ05521.
GermOnlineYDR284C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D1.20.144.10. 1 hit.
InterProIPR016118. P_Acid_Pase/Cl_peroxidase_N.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamPF01569. PAP2. 1 hit.
[Graphical view]
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMSSF48317. AcPase_VanPerase. 1 hit.
ProtoNetSearch...

Other

NextBio969841.

Entry information

Entry nameDPP1_YEAST
AccessionPrimary (citable) accession number: Q05521
Secondary accession number(s): D6VSR4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents