Reviewed,
UniProtKB/Swiss-Prot Q05521 (DPP1_YEAST)
Last modified
January 19, 2010.
Version 76.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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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 |
| ||||||
| 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.7Traceable author statement. Source: SGD |
| Cellular component | fungal-type vacuole membrane Ref.4 Inferred from direct assay. Source: SGD integral to membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | diacylglycerol pyrophosphate phosphatase activity Ref.3 Inferred from direct assay. Source: SGD identical protein bindingInferred from physical interaction. Source: IntAct phosphatidate phosphatase activityInferred 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
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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. 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. 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 |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |

Clusters with


