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UniProtKB - Q05521 (DPP1_YEAST)
Protein
Diacylglycerol pyrophosphate phosphatase 1
Gene
DPP1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
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.
5 PublicationsMiscellaneous
Present with 3038 molecules/cell in log phase SD medium.1 Publication
Catalytic activityi
- a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + H+ + phosphate3 PublicationsEC:3.1.3.813 PublicationsThis reaction proceeds in the forward3 Publications direction.
- EC:3.1.3.42 PublicationsThis reaction proceeds in the forward2 Publications direction.
- EC:3.1.3.1061 PublicationThis reaction proceeds in the forward1 Publication direction.
Activity regulationi
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.2 Publications
Kineticsi
- Vmax=167 µmol/min/mg enzyme with lysophosphatidic acid as substrate1 Publication
pH dependencei
Optimum pH is 6.0-8.5 (PubMed:8940025). Optimum pH for geranylgeranyl-P-P phosphatase reaction is 5.0-5.5 (PubMed:10329682).2 Publications
GO - Molecular functioni
- diacylglycerol diphosphate phosphatase activity Source: SGD
- identical protein binding Source: IntAct
- phosphatidate phosphatase activity Source: SGD
GO - Biological processi
- phospholipid metabolic process Source: SGD
Keywordsi
Molecular function | Hydrolase |
Enzyme and pathway databases
BRENDAi | 3.1.3.81, 984 |
Reactomei | R-SCE-1660661, Sphingolipid de novo biosynthesis R-SCE-2029485, Role of phospholipids in phagocytosis R-SCE-419408, Lysosphingolipid and LPA receptors |
Protein family/group databases
TCDBi | 9.B.105.3.2, the lead resistance fusion protein (pbrbc) family |
Chemistry databases
SwissLipidsi | SLP:000000057 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:DPP1 Synonyms:ZRG1 Ordered Locus Names:YDR284C |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000002692, DPP1 |
VEuPathDBi | FungiDB:YDR284C |
Subcellular locationi
Vacuole
- Vacuole membrane 3 Publications; Multi-pass membrane protein 3 Publications
Vacuole
- fungal-type vacuole membrane Source: SGD
Other locations
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 21 | VacuolarSequence analysisAdd BLAST | 21 | |
Transmembranei | 22 – 42 | Helical; Name=1Sequence analysisAdd BLAST | 21 | |
Topological domaini | 43 – 65 | CytoplasmicSequence analysisAdd BLAST | 23 | |
Transmembranei | 66 – 86 | Helical; Name=2Sequence analysisAdd BLAST | 21 | |
Topological domaini | 87 – 92 | VacuolarSequence analysis | 6 | |
Transmembranei | 93 – 113 | Helical; Name=3Sequence analysisAdd BLAST | 21 | |
Topological domaini | 114 – 172 | CytoplasmicSequence analysisAdd BLAST | 59 | |
Transmembranei | 173 – 193 | Helical; Name=4Sequence analysisAdd BLAST | 21 | |
Transmembranei | 194 – 214 | Helical; Name=5Sequence analysisAdd BLAST | 21 | |
Topological domaini | 215 – 222 | CytoplasmicSequence analysis | 8 | |
Transmembranei | 223 – 243 | Helical; Name=6Sequence analysisAdd BLAST | 21 | |
Topological domaini | 244 – 289 | VacuolarSequence analysisAdd BLAST | 46 |
Keywords - Cellular componenti
Membrane, VacuolePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 125 | R → A: Complete loss of DGPP phosphatase activity. 1 Publication | 1 | |
Mutagenesisi | 169 | H → A: 91% decrease of DGPP phosphatase activity. 1 Publication | 1 | |
Mutagenesisi | 223 | H → A: Complete loss of DGPP phosphatase activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000220918 | 1 – 289 | Diacylglycerol pyrophosphate phosphatase 1Add BLAST | 289 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 285 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
MaxQBi | Q05521 |
PaxDbi | Q05521 |
PRIDEi | Q05521 |
TopDownProteomicsi | Q05521 |
PTM databases
iPTMneti | Q05521 |
Expressioni
Inductioni
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.3 Publications
Interactioni
Binary interactionsi
Q05521
With | #Exp. | IntAct |
---|---|---|
itself | 3 | EBI-2054360,EBI-2054360 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 32337, 65 interactors |
DIPi | DIP-8807N |
IntActi | Q05521, 11 interactors |
MINTi | Q05521 |
STRINGi | 4932.YDR284C |
Miscellaneous databases
RNActi | Q05521, protein |
Structurei
3D structure databases
AlphaFoldDBi | Q05521 |
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 118 – 126 | Phosphatase sequence motif I | 9 | |
Regioni | 166 – 169 | Phosphatase sequence motif II | 4 | |
Regioni | 216 – 227 | Phosphatase sequence motif IIIAdd BLAST | 12 |
Domaini
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.
Sequence similaritiesi
Belongs to the PA-phosphatase related phosphoesterase family.Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG3030, Eukaryota |
GeneTreei | ENSGT00940000174574 |
HOGENOMi | CLU_021458_6_1_1 |
InParanoidi | Q05521 |
OMAi | CTPLIVI |
Family and domain databases
InterProi | View protein in InterPro IPR036938, P_Acid_Pase_2/haloperoxi_sf IPR000326, P_Acid_Pase_2/haloperoxidase IPR043216, PA_PP_rel |
PANTHERi | PTHR10165, PTHR10165, 1 hit |
Pfami | View protein in Pfam PF01569, PAP2, 1 hit |
SMARTi | View protein in SMART SM00014, acidPPc, 1 hit |
SUPFAMi | SSF48317, SSF48317, 1 hit |
i Sequence
Sequence statusi: Complete.
Q05521-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MNRVSFIKTP FNIGAKWRLE DVFLLIIMIL LNYPVYYQQP FERQFYINDL
60 70 80 90 100
TISHPYATTE RVNNNMLFVY SFVVPSLTIL IIGSILADRR HLIFILYTSL
110 120 130 140 150
LGLSLAWFST SFFTNFIKNW IGRLRPDFLD RCQPVEGLPL DTLFTAKDVC
160 170 180 190 200
TTKNHERLLD GFRTTPSGHS SESFAGLGYL YFWLCGQLLT ESPLMPLWRK
210 220 230 240 250
MVAFLPLLGA ALIALSRTQD YRHHFVDVIL GSMLGYIMAH FFYRRIFPPI
260 270 280
DDPLPFKPLM DDSDVTLEEA VTHQRIPDEE LHPLSDEGM
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U51031 Genomic DNA Translation: AAB64475.1 AY557744 Genomic DNA Translation: AAS56070.1 BK006938 Genomic DNA Translation: DAA12124.1 |
PIRi | S70114 |
RefSeqi | NP_010570.1, NM_001180592.1 |
Genome annotation databases
EnsemblFungii | YDR284C_mRNA; YDR284C; YDR284C |
GeneIDi | 851878 |
KEGGi | sce:YDR284C |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U51031 Genomic DNA Translation: AAB64475.1 AY557744 Genomic DNA Translation: AAS56070.1 BK006938 Genomic DNA Translation: DAA12124.1 |
PIRi | S70114 |
RefSeqi | NP_010570.1, NM_001180592.1 |
3D structure databases
AlphaFoldDBi | Q05521 |
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
BioGRIDi | 32337, 65 interactors |
DIPi | DIP-8807N |
IntActi | Q05521, 11 interactors |
MINTi | Q05521 |
STRINGi | 4932.YDR284C |
Chemistry databases
SwissLipidsi | SLP:000000057 |
Protein family/group databases
TCDBi | 9.B.105.3.2, the lead resistance fusion protein (pbrbc) family |
PTM databases
iPTMneti | Q05521 |
Proteomic databases
MaxQBi | Q05521 |
PaxDbi | Q05521 |
PRIDEi | Q05521 |
TopDownProteomicsi | Q05521 |
Protocols and materials databases
DNASUi | 851878 |
Genome annotation databases
EnsemblFungii | YDR284C_mRNA; YDR284C; YDR284C |
GeneIDi | 851878 |
KEGGi | sce:YDR284C |
Organism-specific databases
SGDi | S000002692, DPP1 |
VEuPathDBi | FungiDB:YDR284C |
Phylogenomic databases
eggNOGi | KOG3030, Eukaryota |
GeneTreei | ENSGT00940000174574 |
HOGENOMi | CLU_021458_6_1_1 |
InParanoidi | Q05521 |
OMAi | CTPLIVI |
Enzyme and pathway databases
BRENDAi | 3.1.3.81, 984 |
Reactomei | R-SCE-1660661, Sphingolipid de novo biosynthesis R-SCE-2029485, Role of phospholipids in phagocytosis R-SCE-419408, Lysosphingolipid and LPA receptors |
Miscellaneous databases
PROi | PR:Q05521 |
RNActi | Q05521, protein |
Family and domain databases
InterProi | View protein in InterPro IPR036938, P_Acid_Pase_2/haloperoxi_sf IPR000326, P_Acid_Pase_2/haloperoxidase IPR043216, PA_PP_rel |
PANTHERi | PTHR10165, PTHR10165, 1 hit |
Pfami | View protein in Pfam PF01569, PAP2, 1 hit |
SMARTi | View protein in SMART SM00014, acidPPc, 1 hit |
SUPFAMi | SSF48317, SSF48317, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DPP1_YEAST | |
Accessioni | Q05521Primary (citable) accession number: Q05521 Secondary accession number(s): D6VSR4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 11, 2004 |
Last sequence update: | November 1, 1996 | |
Last modified: | May 25, 2022 | |
This is version 170 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- 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