DPP1 encodes diacylglycerol pyrophosphate (DGPP) phosphatase, a Mg2+-independent lipid phosphate phosphatase of the PAP2 (lipid phosphate phosphatase) superfamily. It is an integral multi-pass membrane protein of the vacuolar membrane, and its catalytic motifs follow the three-domain KX6RP/PSGH/SRX5HX3D consensus. Dpp1 removes the beta-phosphate of DGPP to give phosphatidate (PA), then dephosphorylates PA to diacylglycerol. It also hydrolyses lysophosphatidate and phosphatidylglycerophosphate, and isoprenoid diphosphates (farnesyl-PP, geranylgeranyl-PP, dolichyl-PP), with DGPP as the preferred substrate. Together with the Golgi paralogue Lpp1 it accounts for nearly all Mg2+-independent PA, LPA and DGPP phosphatase activity in the cell, and loss of Dpp1 causes DGPP to accumulate. DPP1 is induced by zinc depletion through Zap1, and also by inositol and in stationary phase. Zinc inhibits the enzyme by forming DGPP-zinc complexes. The Mg2+-dependent lipin Pah1, not Dpp1, supplies the diacylglycerol used for bulk triacylglycerol synthesis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000329 fungal-type vacuole membrane | HDA PMID:26928762 One library to make them all: streamlining the creation of y... | ACCEPT | Summary: HDA from the SWAT N-terminal GFP endomembrane library (Yofe et al. 2016) placing Dpp1 on the vacuole membrane. Supporting Evidence: PMID:26928762 carrying SWAT-GFP modules at the amino termini of endomembrane proteins PMID:11139591 Studies with well characterized subcellular fractions and by indirect immunofluorescence microscopy revealed that the DGPP phosphatase enzyme was localized to the vacuolar membrane. |
| GO:0000329 fungal-type vacuole membrane | IDA PMID:11139591 Regulation of the Saccharomyces cerevisiae DPP1-encoded diac... | ACCEPT | Summary: IDA from Han et al. 2001; fractionation and immunofluorescence localised Dpp1 to the vacuolar membrane. Supporting Evidence: PMID:11139591 Studies with well characterized subcellular fractions and by indirect immunofluorescence microscopy revealed that the DGPP phosphatase enzyme was localized to the vacuolar membrane. |
| GO:0000329 fungal-type vacuole membrane | IDA PMID:23836928 Direct imaging reveals stable, micrometer-scale lipid domain... | ACCEPT | Summary: IDA from Toulmay and Prinz 2013, who imaged a panel of vacuolar membrane proteins segregating into micrometre-scale domains under stress. Supporting Evidence: PMID:23836928 All vacuolar membrane proteins tested segregated to one of two domains. |
| GO:0000810 diacylglycerol diphosphate phosphatase activity | EXP PMID:10329682 The LPP1 and DPP1 gene products account for most of the isop... | ACCEPT | Summary: SGD EXP from Faulkner et al. 1999; purified Dpp1 and dpp1/lpp1 mutants show DGPP phosphatase (and broader lipid/isoprenoid diphosphate phosphatase) activity. Supporting Evidence: PMID:10329682 The action of Dpp1p on isoprenyl pyrophosphates was confirmed by characterization of the hydrolysis of geranylgeranyl-P-P by the purified protein. PMID:10329682 the disruption of DPP1 and LPP1 produced profound losses of Mg2+-independent PA phosphatase activity |
| GO:0000810 diacylglycerol diphosphate phosphatase activity | EXP PMID:8940025 The Escherichia coli pgpB gene encodes for a diacylglycerol ... | ACCEPT | Summary: SGD EXP from Dillon et al. 1996; the comparison with E. coli PgpB used pure yeast DGPP phosphatase (the Dpp1 protein) and confirmed its DGPP phosphatase activity. Supporting Evidence: PMID:8940025 Pure DGPP phosphatase from Saccharomyces cerevisiae was shown to be similar to the E. coli DGPP phosphatase in its ability to utilize lyso-PA and phosphatidylglycerophosphate as substrates in vitro. |
| GO:0000810 diacylglycerol diphosphate phosphatase activity | IDA PMID:8567632 Purification and characterization of diacylglycerol pyrophos... | ACCEPT | Summary: IDA from Wu et al. 1996, who purified the 34-kDa DGPP phosphatase (later shown to be Dpp1) and characterised its DGPP beta-phosphate hydrolysis. Supporting Evidence: PMID:8567632 Diacylglycerol pyrophosphate (DGPP) phosphatase is a novel membrane-associated enzyme that catalyzes the dephosphorylation of the beta phosphate of DGPP to yield phosphatidate and Pi. PMID:8567632 DGPP was the preferred substrate for the enzyme with a specificity constant (Vmax/Km) 10-fold greater than that for phosphatidate. |
| GO:0000810 diacylglycerol diphosphate phosphatase activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from RHEA/EC 3.6.1.75 mapping derived from UniProt's DGPP phosphatase reaction. Correct. Supporting Evidence: file:yeast/DPP1/DPP1-uniprot.txt Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl- |
| GO:0000810 diacylglycerol diphosphate phosphatase activity | IMP PMID:9452443 Isolation and characterization of the Saccharomyces cerevisi... | ACCEPT | Summary: IMP from Toke et al. 1998; dpp1 deletion abolished DGPP phosphatase activity and caused DGPP to accumulate. Supporting Evidence: PMID:9452443 The mutant was devoid of DGPP phosphatase activity and accumulated (4-fold) DGPP. |
| GO:0005774 vacuolar membrane | EXP PMID:11139591 Regulation of the Saccharomyces cerevisiae DPP1-encoded diac... | ACCEPT | Summary: SGD EXP from Han et al. 2001 (vacuolar membrane by fractionation and immunofluorescence). Supporting Evidence: PMID:11139591 Studies with well characterized subcellular fractions and by indirect immunofluorescence microscopy revealed that the DGPP phosphatase enzyme was localized to the vacuolar membrane. |
| GO:0005774 vacuolar membrane | EXP PMID:8567632 Purification and characterization of diacylglycerol pyrophos... | ACCEPT | Summary: SGD EXP from Wu et al. 1996 (membrane-associated enzyme purified from detergent-solubilised membranes). The curator assigned vacuolar membrane, which is consistent with later work. Supporting Evidence: PMID:8567632 Diacylglycerol pyrophosphate (DGPP) phosphatase is a novel membrane-associated enzyme that catalyzes the dephosphorylation of the beta phosphate of DGPP to yield phosphatidate and Pi. PMID:11139591 Studies with well characterized subcellular fractions and by indirect immunofluorescence microscopy revealed that the DGPP phosphatase enzyme was localized to the vacuolar membrane. |
| GO:0005774 vacuolar membrane | IEA GO_REF:0000044 | ACCEPT | Summary: IEA from UniProt subcellular location (SL-0271 vacuole membrane). Correct. Supporting Evidence: PMID:11139591 Studies with well characterized subcellular fractions and by indirect immunofluorescence microscopy revealed that the DGPP phosphatase enzyme was localized to the vacuolar membrane. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | REMOVE | Summary: YeastPathways RCA placing Dpp1's PA phosphatase step of TRIGLSYN-PWY in the cytosol. Dpp1 is an integral vacuolar membrane protein. Reason: Pathway default location that contradicts the established vacuolar membrane localisation of this six-transmembrane enzyme. Supporting Evidence: PMID:11139591 Studies with well characterized subcellular fractions and by indirect immunofluorescence microscopy revealed that the DGPP phosphatase enzyme was localized to the vacuolar membrane. PMID:9452443 DGPP phosphatase was predicted to be an integral membrane protein with six transmembrane-spanning domains. |
| GO:0006629 lipid metabolic process | IEA GO_REF:0000117 | TOO GENERAL | Summary: IEA from ARBA rule ARBA00028591 for lipid metabolic process. Correct but very general. Supporting Evidence: PMID:8567632 Diacylglycerol pyrophosphate (DGPP) phosphatase is a novel membrane-associated enzyme that catalyzes the dephosphorylation of the beta phosphate of DGPP to yield phosphatidate and Pi. |
| GO:0006644 phospholipid metabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for phospholipid metabolic process at the lipid phosphate phosphatase node (PTN000017950), grounded in Dpp1, Lpp1 and the mammalian PLPP enzymes. Supporting Evidence: PMID:10329682 the disruption of DPP1 and LPP1 produced profound losses of Mg2+-independent PA phosphatase activity |
| GO:0006644 phospholipid metabolic process | IEA GO_REF:0000002 | ACCEPT | Summary: IEA from InterPro IPR043216 (PAP2/lipid phosphate phosphatase family) for phospholipid metabolic process. Correct for Dpp1. Supporting Evidence: PMID:8567632 Diacylglycerol pyrophosphate (DGPP) phosphatase is a novel membrane-associated enzyme that catalyzes the dephosphorylation of the beta phosphate of DGPP to yield phosphatidate and Pi. |
| GO:0006644 phospholipid metabolic process | IMP PMID:10329682 The LPP1 and DPP1 gene products account for most of the isop... | ACCEPT | Summary: IMP from Faulkner et al. 1999; dpp1 and lpp1 disruption abolished most Mg2+-independent PA and isoprenoid phosphate phosphatase activity. Supporting Evidence: PMID:10329682 the disruption of DPP1 and LPP1 produced profound losses of Mg2+-independent PA phosphatase activity |
| GO:0008195 phosphatidate phosphatase activity | EXP PMID:8567632 Purification and characterization of diacylglycerol pyrophos... | ACCEPT | Summary: SGD EXP from Wu et al. 1996; the purified enzyme also dephosphorylated PA, although DGPP was the preferred substrate. Supporting Evidence: PMID:8567632 DGPP phosphatase also catalyzed the dephosphorylation of phosphatidate, but this dephosphorylation was subsequent to the dephosphorylation of the beta phosphate of DGPP. PMID:8567632 DGPP was the preferred substrate for the enzyme with a specificity constant (Vmax/Km) 10-fold greater than that for phosphatidate. |
| GO:0008195 phosphatidate phosphatase activity | EXP PMID:8940025 The Escherichia coli pgpB gene encodes for a diacylglycerol ... | ACCEPT | Summary: SGD EXP from Dillon et al. 1996, which compared pure yeast DGPP phosphatase with E. coli PgpB (both dephosphorylate DGPP and then PA). Supporting Evidence: PMID:8940025 Pure DGPP phosphatase from Saccharomyces cerevisiae was shown to be similar to the E. coli DGPP phosphatase in its ability to utilize lyso-PA and phosphatidylglycerophosphate as substrates in vitro. |
| GO:0008195 phosphatidate phosphatase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for phosphatidate phosphatase activity at the LPP family node (PTN000017950), grounded in yeast Dpp1/Lpp1 and the mammalian PLPP1-3 enzymes. Correct. Supporting Evidence: PMID:9452443 DGPP phosphatase possesses a Mg2+-independent PA phosphatase activity |
| GO:0008195 phosphatidate phosphatase activity | IDA PMID:10329682 The LPP1 and DPP1 gene products account for most of the isop... | ACCEPT | Summary: IDA from Faulkner et al. 1999 for PA phosphatase activity of Dpp1 (Mg2+-independent). Supporting Evidence: PMID:10329682 the disruption of DPP1 and LPP1 produced profound losses of Mg2+-independent PA phosphatase activity |
| GO:0008195 phosphatidate phosphatase activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from RHEA/EC 3.1.3.4 mapping derived from UniProt's PA phosphatase reaction for Dpp1. Correct. Supporting Evidence: file:yeast/DPP1/DPP1-uniprot.txt Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn- |
| GO:0008195 phosphatidate phosphatase activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (TRIGLSYN-PWY) assigning the PA -> DAG step (EC 3.1.3.4) to Dpp1. Dpp1 does have PA phosphatase activity, so the MF is correct. Reason: The activity is real. Its quantitative contribution to TAG synthesis is small compared with Pah1, which is handled at the BP row (GO:0019432). Supporting Evidence: PMID:9452443 DGPP phosphatase possesses a Mg2+-independent PA phosphatase activity PMID:24196957 showed the essential role of PAH1 in triacylglycerol synthesis throughout growth |
| GO:0016020 membrane | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA (is_active_in membrane) for the LPP clade of integral membrane phosphatases. Correct though general. Supporting Evidence: PMID:9452443 DGPP phosphatase was predicted to be an integral membrane protein with six transmembrane-spanning domains. |
| GO:0019432 triglyceride biosynthetic process | RCA GO_REF:0000123 | MARK AS OVER ANNOTATED | Summary: YeastPathways RCA placing Dpp1 in triglyceride biosynthesis (TRIGLSYN-PWY) because it can dephosphorylate PA in vitro. Reason: The Mg2+-dependent lipin Pah1 is the PA phosphatase that supplies DAG for TAG synthesis throughout growth. Dpp1 is a vacuolar, Mg2+-independent enzyme whose physiological substrates appear to be DGPP, LPA and isoprenoid diphosphates, and no TAG-synthesis defect has been attributed to dpp1 loss. Membership of the TAG pathway is inferred only from in vitro substrate range. Supporting Evidence: PMID:24196957 showed the essential role of PAH1 in triacylglycerol synthesis throughout growth PMID:24196957 are integral membrane enzymes that are localized to the vacuole and Golgi compartments, respectively |
| GO:0042802 identical protein binding | IPI PMID:18467557 An in vivo map of the yeast protein interactome. | KEEP AS NON CORE | Summary: IPI (identical protein binding) from the Tarassov et al. 2008 DHFR protein-fragment complementation screen, detecting Dpp1 self-association. Reason: Suggests homo-oligomerisation of Dpp1 but conveys no catalytic function; non-core. Supporting Evidence: PMID:18467557 We identified 2770 interactions among 1124 endogenously expressed proteins. |
| GO:0042802 identical protein binding | IPI PMID:18719252 High-quality binary protein interaction map of the yeast int... | KEEP AS NON CORE | Summary: IPI (identical protein binding) from the Yu et al. 2008 high-quality binary Y2H map. Reason: Self-interaction from a high-throughput screen; non-core. Supporting Evidence: PMID:18719252 high-throughput yeast two-hybrid (Y2H) screening provides high-quality binary interaction information |
| GO:0042802 identical protein binding | IPI PMID:31454312 The role of structural pleiotropy and regulatory evolution i... | KEEP AS NON CORE | Summary: IPI (identical protein binding) from the Marchant et al. 2019 DHFR-PCA survey of homomers and heteromers of paralogues (Dpp1/Lpp1 are paralogues). Reason: Consistent homomer detection across assays, but it describes oligomeric state, not function. Supporting Evidence: PMID:31454312 heteromerization is frequent among duplicated homomers |
| GO:0045121 membrane raft | IDA PMID:23836928 Direct imaging reveals stable, micrometer-scale lipid domain... | KEEP AS NON CORE | Summary: IDA from Toulmay and Prinz 2013 assigning membrane raft; vacuolar membrane proteins partition into sterol-enriched liquid-ordered or disordered domains under nutrient stress. Reason: This is a stress-induced partitioning of vacuolar membrane proteins and is not specific to Dpp1 function. The cached text does not show which domain Dpp1 entered, so the annotation is retained as non-core on the curator's authority. Supporting Evidence: PMID:23836928 All vacuolar membrane proteins tested segregated to one of two domains. PMID:23836928 we found that one of these domains is probably sterol enriched and Lo |
| GO:0046839 phospholipid dephosphorylation | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for phospholipid dephosphorylation at the LPP family node. Directly describes Dpp1's DGPP/PA/LPA phosphatase activity. Supporting Evidence: PMID:8567632 Diacylglycerol pyrophosphate (DGPP) phosphatase is a novel membrane-associated enzyme that catalyzes the dephosphorylation of the beta phosphate of DGPP to yield phosphatidate and Pi. PMID:8940025 Pure DGPP phosphatase from Saccharomyces cerevisiae was shown to be similar to the E. coli DGPP phosphatase in its ability to utilize lyso-PA and phosphatidylglycerophosphate as substrates in vitro. |
| GO:0052642 lysophosphatidic acid phosphatase activity | EXP PMID:8940025 The Escherichia coli pgpB gene encodes for a diacylglycerol ... | ACCEPT | Summary: SGD EXP from Dillon et al. 1996; pure yeast DGPP phosphatase used lyso-PA as a substrate in vitro. Supporting Evidence: PMID:8940025 Pure DGPP phosphatase from Saccharomyces cerevisiae was shown to be similar to the E. coli DGPP phosphatase in its ability to utilize lyso-PA and phosphatidylglycerophosphate as substrates in vitro. file:yeast/DPP1/DPP1-uniprot.txt preference is DGPP > LPA > PA. |
| GO:0052642 lysophosphatidic acid phosphatase activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from RHEA/EC 3.1.3.106 mapping derived from UniProt's LPA phosphatase reaction. Correct. Supporting Evidence: file:yeast/DPP1/DPP1-uniprot.txt Reaction=a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol + |
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Download this section (compressed HTML)Q: What is the physiological substrate of vacuolar Dpp1 in vivo (DGPP, LPA, PA or isoprenoid diphosphates), and does it supply diacylglycerol for vacuole membrane function rather than for bulk TAG synthesis?
Q: How does zinc-regulated induction of DPP1 via Zap1 relate to its lipid phosphatase function under zinc limitation?
Experiment: Lipidomic profiling of vacuolar membranes from dpp1, lpp1 and dpp1 lpp1 strains under zinc-replete and zinc-limited conditions, including DGPP, LPA, PA, DAG and dolichyl phosphates.
Hypothesis: Dpp1 controls vacuolar DGPP/PA levels under zinc limitation, but does not contribute to bulk TAG synthesis.
Type: lipidomics/genetics
Diacylglycerol pyrophosphate (DGPP) phosphatase; zinc-regulated vacuolar membrane-associated lipid phosphatase, dephosphorylates DGPP to phosphatidate (PA) and Pi, then PA to diacylglycerol; involved in lipid signaling and cell metabolism
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