{"gene":"PF3D7_1456800","run_date":"2026-09-08T14:19:07","timeline":{"discoveries":[{"year":2001,"finding":"VP1 (PfVP1) is a type I (K⁺-dependent) V-type H⁺-pyrophosphatase that localizes to the parasite plasma membrane and punctate intracellular inclusions in P. falciparum-infected erythrocytes, as demonstrated by immunofluorescence microscopy and transient transfection of a PfVP1-GFP fusion protein. K⁺-stimulated, AMDP-inhibitable PPase activity was detected in trophozoite membranes, consistent with VP1 catalyzing pyrophosphate hydrolysis coupled to proton translocation.","method":"Immunofluorescence microscopy, PfVP1-GFP transient transfection, Western blot with V-PPase antibodies, K⁺-stimulation and AMDP-inhibition enzymatic assays on trophozoite membranes","journal":"Molecular and biochemical parasitology","confidence":"High","confidence_rationale":"Tier 2 / Moderate — direct localization by both antibody-based imaging and GFP fusion, enzymatic activity confirmed with pharmacological inhibitor and K⁺ dependence, multiple orthogonal methods in one study","pmids":["11378198"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2023,"finding":"VP1 (PfVP1) functions as an essential proton pump at the parasite plasma membrane during the ring stage and ring-to-trophozoite transition. Conditional deletion of PfVP1 causes a prolonged ring stage (~48 hours instead of ~20 hours) and complete blockage of the ring-to-trophozoite transition followed by parasite death. Rescue with an orthologous proton-pumping pyrophosphatase from Arabidopsis thaliana (but not the non-proton-pumping soluble pyrophosphatase from Saccharomyces cerevisiae) confirmed that the proton-pumping activity of VP1, using pyrophosphate as fuel, is the essential function.","method":"Conditional genetic deletion (reverse genetics), phenotypic rescue with heterologous V-PPases (A. thaliana proton-pumping vs. S. cerevisiae soluble pyrophosphatase), parasite stage progression assays","journal":"PLoS pathogens","confidence":"High","confidence_rationale":"Tier 2 / Strong — conditional KO with defined stage-specific phenotype, mechanistic rescue experiment distinguishing proton-pumping from hydrolytic activity; multiple orthogonal approaches in one rigorous study","pmids":["38048362"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"VP1 (PfVP1, referred to as PfPPase-VP1) was successfully expressed in a baculovirus/insect cell system, purified (0.3 mg/L culture), and shown to retain catalytic (pyrophosphate hydrolysis) activity in multiple detergents. Among 35 compounds screened, only three pyrazolo[1,5-a]pyrimidine-based Thermotoga maritima mPPase inhibitors showed micromolar IC50 activity against PfPPase-VP1, establishing VP1 as biochemically tractable for structure-based drug discovery.","method":"Baculovirus/insect cell heterologous expression, protein purification, detergent-solubilization assays, enzymatic activity assays, pharmacological screening (14 antimalarial drugs + 21 mPPase inhibitors/unknowns)","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — in vitro enzymatic reconstitution with purified protein and inhibitor profiling, single lab, single study","pmids":["40424284"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"VP1 (PfVP1) localizes to the parasite plasma membrane and functions as a proton pump in asexual blood stages. Maintenance of pyrophosphate homeostasis by VP1 in the plasma membrane compartment is essential for parasite survival, distinct from the roles of soluble pyrophosphatases in the cytoplasm and organelles.","method":"Reverse genetics and biochemical approaches (subcellular localization and functional studies in the context of comparative pyrophosphatase biology)","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — preprint, single lab, confirms prior localization and essentiality findings but in a broader comparative context; no new orthogonal method specific to VP1","pmids":["40027813"],"is_preprint":true,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"VP1 (PF3D7_1456800) is an essential, K⁺-dependent, type I membrane-bound vacuolar H⁺-pyrophosphatase that localizes to the P. falciparum parasite plasma membrane, where it hydrolyzes pyrophosphate to drive proton export, thereby maintaining intracellular pH and enabling the ring-to-trophozoite developmental transition during asexual blood-stage growth."},"narrative":{"mechanistic_narrative":"VP1 (PF3D7_1456800) is a type I, K⁺-dependent, membrane-bound V-type H⁺-translocating pyrophosphatase of Plasmodium falciparum that couples pyrophosphate hydrolysis to proton translocation across the parasite plasma membrane [PMID:11378198]. It localizes to the parasite plasma membrane and punctate intracellular inclusions, and its K⁺-stimulated, AMDP-inhibitable PPase activity is detectable in trophozoite membranes [PMID:11378198]. VP1 is essential for asexual blood-stage development: conditional deletion prolongs the ring stage and completely blocks the ring-to-trophozoite transition, culminating in parasite death, and this defect is rescued by a heterologous proton-pumping pyrophosphatase from Arabidopsis thaliana but not by a non-proton-pumping soluble yeast pyrophosphatase, demonstrating that proton pumping fueled by pyrophosphate—not mere hydrolysis—is the essential function [PMID:38048362]. Its role in maintaining pyrophosphate homeostasis at the plasma membrane is distinct from that of soluble cytoplasmic and organellar pyrophosphatases [PMID:40027813]. VP1 has been heterologously expressed, purified, and shown to retain catalytic activity in detergent, and is selectively inhibited by pyrazolo[1,5-a]pyrimidine-based mPPase inhibitors, establishing it as tractable for structure-based drug discovery [PMID:40424284].","teleology":[{"year":2001,"claim":"Establishing whether P. falciparum encodes a functional membrane proton-pumping pyrophosphatase and where it acts defined VP1 as a candidate energizer of the parasite membrane.","evidence":"Immunofluorescence, PfVP1-GFP transient transfection, and K⁺-stimulated, AMDP-inhibitable enzymatic assays on trophozoite membranes","pmids":["11378198"],"confidence":"High","gaps":["Physiological consequence of the activity for parasite viability not tested","Punctate intracellular inclusions not molecularly identified","No genetic loss-of-function to confirm the assigned catalytic role in vivo"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2023,"claim":"Conditional deletion resolved whether VP1 is essential and which biochemical activity is required, showing that its proton-pumping function drives the ring-to-trophozoite developmental transition.","evidence":"Conditional genetic deletion with stage-progression assays and heterologous rescue distinguishing proton-pumping from soluble hydrolytic pyrophosphatase","pmids":["38048362"],"confidence":"High","gaps":["Mechanistic link between proton pumping and the developmental block not defined","Downstream pH/ion effects not directly measured","Whether VP1 has stage-specific roles beyond the ring stage untested"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"Reconstituting purified VP1 and profiling inhibitors established it as a biochemically tractable and druggable target.","evidence":"Baculovirus/insect cell expression, detergent-solubilized purification, activity assays, and screening of antimalarials and mPPase inhibitors","pmids":["40424284"],"confidence":"Medium","gaps":["No structure of the purified protein reported","Only three hit compounds at micromolar IC50","Proton-pumping activity of the purified enzyme not directly demonstrated in this system"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"Comparative analysis placed VP1's essential role in maintaining pyrophosphate homeostasis at the plasma membrane, distinct from soluble pyrophosphatases in other compartments.","evidence":"Reverse genetics and biochemical/localization studies in a comparative pyrophosphatase framework (preprint)","pmids":["40027813"],"confidence":"Medium","gaps":["Preprint, not peer-reviewed","No new VP1-specific orthogonal method beyond prior work","Functional interplay with soluble pyrophosphatases not directly demonstrated"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"The structural basis of VP1's proton pumping and the mechanistic chain linking its activity to the developmental transition remain open.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No experimental structure of VP1","Molecular mechanism coupling proton export to ring-to-trophozoite progression unresolved","Identity/role of the punctate intracellular VP1 pool undefined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":[],"other_free_text":["K⁺-dependent, AMDP-inhibitable type I V-PPase activity in trophozoite membranes [#0]","Conditional deletion prolongs ring stage and blocks ring-to-trophozoite transition, causing death [#1]","Proton-pumping activity (rescued by A. thaliana V-PPase, not by soluble yeast pyrophosphatase) is the essential function [#1]","Heterologously expressed and purified; selectively inhibited by pyrazolo[1,5-a]pyrimidine mPPase inhibitors [#2]","Maintains plasma-membrane pyrophosphate homeostasis distinct from soluble pyrophosphatases [#3]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"11378198","id":"PMC_11378198","title":"Two classes of plant-like vacuolar-type H(+)-pyrophosphatases in malaria parasites.","date":"2001","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/11378198","citation_count":69,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfVP1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"38048362","id":"PMC_38048362","title":"Plasmodium falciparum utilizes pyrophosphate to fuel an essential proton pump in the ring stage and the transition to trophozoite stage.","date":"2023","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/38048362","citation_count":14,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfVP1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"40424284","id":"PMC_40424284","title":"Expression, purification and preliminary pharmacological characterization of the Plasmodium falciparum membrane-bound pyrophosphatase type 1.","date":"2025","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/40424284","citation_count":2,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["VP1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"40027813","id":"PMC_40027813","title":"Maintenance of pyrophosphate homeostasis in multiple subcellular compartments is essential in Plasmodium falciparum.","date":"2025","source":"bioRxiv : the preprint server for biology","url":"https://pubmed.ncbi.nlm.nih.gov/40027813","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfVP1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"42017676","id":"PMC_42017676","title":"Pyrophosphate homeostasis in multiple subcellular compartments is essential in Plasmodium falciparum.","date":"2026","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/42017676","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfVP1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5885,"output_tokens":1472,"usd":0.019867,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6451,"output_tokens":2372,"usd":0.045777,"stage2_stop_reason":"end_turn"},"total_usd":0.065644,"stage1_batch_id":"msgbatch_011BPjN2BL33F8cJXD1r7V7T","stage2_batch_id":"msgbatch_01Qwg6vP7qxkpL6Gsc7tajsb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2001,\n      \"finding\": \"VP1 (PfVP1) is a type I (K⁺-dependent) V-type H⁺-pyrophosphatase that localizes to the parasite plasma membrane and punctate intracellular inclusions in P. falciparum-infected erythrocytes, as demonstrated by immunofluorescence microscopy and transient transfection of a PfVP1-GFP fusion protein. K⁺-stimulated, AMDP-inhibitable PPase activity was detected in trophozoite membranes, consistent with VP1 catalyzing pyrophosphate hydrolysis coupled to proton translocation.\",\n      \"method\": \"Immunofluorescence microscopy, PfVP1-GFP transient transfection, Western blot with V-PPase antibodies, K⁺-stimulation and AMDP-inhibition enzymatic assays on trophozoite membranes\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization by both antibody-based imaging and GFP fusion, enzymatic activity confirmed with pharmacological inhibitor and K⁺ dependence, multiple orthogonal methods in one study\",\n      \"pmids\": [\"11378198\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"VP1 (PfVP1) functions as an essential proton pump at the parasite plasma membrane during the ring stage and ring-to-trophozoite transition. Conditional deletion of PfVP1 causes a prolonged ring stage (~48 hours instead of ~20 hours) and complete blockage of the ring-to-trophozoite transition followed by parasite death. Rescue with an orthologous proton-pumping pyrophosphatase from Arabidopsis thaliana (but not the non-proton-pumping soluble pyrophosphatase from Saccharomyces cerevisiae) confirmed that the proton-pumping activity of VP1, using pyrophosphate as fuel, is the essential function.\",\n      \"method\": \"Conditional genetic deletion (reverse genetics), phenotypic rescue with heterologous V-PPases (A. thaliana proton-pumping vs. S. cerevisiae soluble pyrophosphatase), parasite stage progression assays\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — conditional KO with defined stage-specific phenotype, mechanistic rescue experiment distinguishing proton-pumping from hydrolytic activity; multiple orthogonal approaches in one rigorous study\",\n      \"pmids\": [\"38048362\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"VP1 (PfVP1, referred to as PfPPase-VP1) was successfully expressed in a baculovirus/insect cell system, purified (0.3 mg/L culture), and shown to retain catalytic (pyrophosphate hydrolysis) activity in multiple detergents. Among 35 compounds screened, only three pyrazolo[1,5-a]pyrimidine-based Thermotoga maritima mPPase inhibitors showed micromolar IC50 activity against PfPPase-VP1, establishing VP1 as biochemically tractable for structure-based drug discovery.\",\n      \"method\": \"Baculovirus/insect cell heterologous expression, protein purification, detergent-solubilization assays, enzymatic activity assays, pharmacological screening (14 antimalarial drugs + 21 mPPase inhibitors/unknowns)\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — in vitro enzymatic reconstitution with purified protein and inhibitor profiling, single lab, single study\",\n      \"pmids\": [\"40424284\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"VP1 (PfVP1) localizes to the parasite plasma membrane and functions as a proton pump in asexual blood stages. Maintenance of pyrophosphate homeostasis by VP1 in the plasma membrane compartment is essential for parasite survival, distinct from the roles of soluble pyrophosphatases in the cytoplasm and organelles.\",\n      \"method\": \"Reverse genetics and biochemical approaches (subcellular localization and functional studies in the context of comparative pyrophosphatase biology)\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — preprint, single lab, confirms prior localization and essentiality findings but in a broader comparative context; no new orthogonal method specific to VP1\",\n      \"pmids\": [\"40027813\"],\n      \"is_preprint\": true,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"VP1 (PF3D7_1456800) is an essential, K⁺-dependent, type I membrane-bound vacuolar H⁺-pyrophosphatase that localizes to the P. falciparum parasite plasma membrane, where it hydrolyzes pyrophosphate to drive proton export, thereby maintaining intracellular pH and enabling the ring-to-trophozoite developmental transition during asexual blood-stage growth.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"VP1 (PF3D7_1456800) is a type I, K⁺-dependent, membrane-bound V-type H⁺-translocating pyrophosphatase of Plasmodium falciparum that couples pyrophosphate hydrolysis to proton translocation across the parasite plasma membrane [#0]. It localizes to the parasite plasma membrane and punctate intracellular inclusions, and its K⁺-stimulated, AMDP-inhibitable PPase activity is detectable in trophozoite membranes [#0]. VP1 is essential for asexual blood-stage development: conditional deletion prolongs the ring stage and completely blocks the ring-to-trophozoite transition, culminating in parasite death, and this defect is rescued by a heterologous proton-pumping pyrophosphatase from Arabidopsis thaliana but not by a non-proton-pumping soluble yeast pyrophosphatase, demonstrating that proton pumping fueled by pyrophosphate—not mere hydrolysis—is the essential function [#1]. Its role in maintaining pyrophosphate homeostasis at the plasma membrane is distinct from that of soluble cytoplasmic and organellar pyrophosphatases [#3]. VP1 has been heterologously expressed, purified, and shown to retain catalytic activity in detergent, and is selectively inhibited by pyrazolo[1,5-a]pyrimidine-based mPPase inhibitors, establishing it as tractable for structure-based drug discovery [#2].\",\n  \"teleology\": [\n    {\n      \"year\": 2001,\n      \"claim\": \"Establishing whether P. falciparum encodes a functional membrane proton-pumping pyrophosphatase and where it acts defined VP1 as a candidate energizer of the parasite membrane.\",\n      \"evidence\": \"Immunofluorescence, PfVP1-GFP transient transfection, and K⁺-stimulated, AMDP-inhibitable enzymatic assays on trophozoite membranes\",\n      \"pmids\": [\"11378198\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Physiological consequence of the activity for parasite viability not tested\", \"Punctate intracellular inclusions not molecularly identified\", \"No genetic loss-of-function to confirm the assigned catalytic role in vivo\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Conditional deletion resolved whether VP1 is essential and which biochemical activity is required, showing that its proton-pumping function drives the ring-to-trophozoite developmental transition.\",\n      \"evidence\": \"Conditional genetic deletion with stage-progression assays and heterologous rescue distinguishing proton-pumping from soluble hydrolytic pyrophosphatase\",\n      \"pmids\": [\"38048362\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Mechanistic link between proton pumping and the developmental block not defined\", \"Downstream pH/ion effects not directly measured\", \"Whether VP1 has stage-specific roles beyond the ring stage untested\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Reconstituting purified VP1 and profiling inhibitors established it as a biochemically tractable and druggable target.\",\n      \"evidence\": \"Baculovirus/insect cell expression, detergent-solubilized purification, activity assays, and screening of antimalarials and mPPase inhibitors\",\n      \"pmids\": [\"40424284\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No structure of the purified protein reported\", \"Only three hit compounds at micromolar IC50\", \"Proton-pumping activity of the purified enzyme not directly demonstrated in this system\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Comparative analysis placed VP1's essential role in maintaining pyrophosphate homeostasis at the plasma membrane, distinct from soluble pyrophosphatases in other compartments.\",\n      \"evidence\": \"Reverse genetics and biochemical/localization studies in a comparative pyrophosphatase framework (preprint)\",\n      \"pmids\": [\"40027813\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Preprint, not peer-reviewed\", \"No new VP1-specific orthogonal method beyond prior work\", \"Functional interplay with soluble pyrophosphatases not directly demonstrated\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The structural basis of VP1's proton pumping and the mechanistic chain linking its activity to the developmental transition remain open.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No experimental structure of VP1\", \"Molecular mechanism coupling proton export to ring-to-trophozoite progression unresolved\", \"Identity/role of the punctate intracellular VP1 pool undefined\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0009678\", \"supporting_discovery_ids\": [0, 1, 3]},\n      {\"term_id\": \"GO:0004427\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"GO:0015078\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0020039\", \"supporting_discovery_ids\": [0, 1, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:1902600\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0051453\", \"supporting_discovery_ids\": [1, 3]}\n    ],\n    \"complexes\": [],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"K⁺-dependent, AMDP-inhibitable type I V-PPase activity in trophozoite membranes [#0]\",\n      \"Conditional deletion prolongs ring stage and blocks ring-to-trophozoite transition, causing death [#1]\",\n      \"Proton-pumping activity (rescued by A. thaliana V-PPase, not by soluble yeast pyrophosphatase) is the essential function [#1]\",\n      \"Heterologously expressed and purified; selectively inhibited by pyrazolo[1,5-a]pyrimidine mPPase inhibitors [#2]\",\n      \"Maintains plasma-membrane pyrophosphate homeostasis distinct from soluble pyrophosphatases [#3]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1456800","name":null,"product":"V-type H(+)-translocating pyrophosphatase, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1320500","name":null,"product":"V-type H(+)-translocating pyrophosphatase, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1225000","name":null,"product":"V-type H(+)-translocating pyrophosphatase, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"VP1","evaluation":null}