{"gene":"PF3D7_1123100","run_date":"2026-09-08T12:51:28","timeline":{"discoveries":[{"year":2014,"finding":"PfCDPK7 (PF3D7_1123100) has an atypical domain architecture comprising a pleckstrin homology (PH) domain adjacent to the kinase domain and two calcium-binding EF-hands at its N terminus; the PH domain was demonstrated to interact with PI(4,5)P2, which may guide its subcellular localization.","method":"Domain analysis and biochemical interaction assay (PI(4,5)P2 binding via PH domain)","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct binding assay for PI(4,5)P2 interaction demonstrated, single lab, but localization consequence inferred rather than directly shown","pmids":["24895132"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2014,"finding":"Disruption of PfCDPK7 (PF3D7_1123100) caused a marked reduction in blood-stage parasite growth, with maturation of rings to trophozoites stalled, and significantly attenuated parasite proliferation, establishing an essential role in the erythrocytic asexual cycle.","method":"Reverse genetics (disruption of PfCDPK7) with blood-stage growth and stage-progression phenotypic readout","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean loss-of-function with defined cellular phenotype, single lab","pmids":["24895132"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"finding":"PfCDPK7 (PF3D7_1123100) promotes phosphatidylcholine (PC) synthesis by regulating two key enzymes in the PC synthesis pathway, phosphoethanolamine-N-methyltransferase (PMT) and ethanolamine kinase (EK); in the absence of PfCDPK7 both enzymes are hypophosphorylated and PMT is degraded.","method":"Quantitative phosphoproteomics and phospholipid analysis in PfCDPK7 conditional knockdown/disruption parasites","journal":"EMBO reports","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (phosphoproteomics, phospholipid lipidomics, genetic disruption) in a single rigorous study establishing pathway mechanism","pmids":["34866326"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"finding":"PfCDPK7 (PF3D7_1123100) interacts with 4'-phosphorylated phosphoinositides (PIPs) generated by PI4-kinase (PfPI4K), and inhibition of PfPI4K activity disrupts the vesicular localization of PfCDPK7, placing PfCDPK7 downstream of PfPI4K in a signaling pathway that controls phospholipid biosynthesis.","method":"PIP-binding assay, inhibitor (MMV39048) treatment with subcellular localization imaging, and phospholipid analysis","journal":"EMBO reports","confidence":"High","confidence_rationale":"Tier 2 / Strong — direct PIP-binding assay, pharmacological epistasis with PI4K inhibitor, localization imaging, and functional lipidomic readout — multiple orthogonal methods in one study","pmids":["34866326"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2018,"finding":"The RCC1-motif-containing region of the P. falciparum protein PfRCC-PIP was demonstrated to interact with PfCDPK7 (PF3D7_1123100), suggesting PfRCC-PIP acts as a kinase anchoring protein that may provide a platform for phosphorylation/dephosphorylation regulation involving PfCDPK7.","method":"Protein interaction assay (co-immunoprecipitation / pull-down between RCC1-motif region and CDPK7)","journal":"Frontiers in microbiology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single interaction assay, single lab, no functional follow-up specifically for the CDPK7 interaction","pmids":["30429842"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PfCDPK7 (PF3D7_1123100) is an atypical calcium-dependent protein kinase that is recruited to vesicular membranes through binding of its pleckstrin homology domain to 4'-phosphorylated phosphoinositides generated by PfPI4K; once localized, it phosphorylates and stabilizes key enzymes of the phosphatidylcholine biosynthesis pathway (PMT and EK), and its activity is essential for the ring-to-trophozoite transition and proliferation during the erythrocytic asexual cycle of P. falciparum."},"narrative":{"mechanistic_narrative":"PfCDPK7 (PF3D7_1123100) is an atypical calcium-dependent protein kinase that couples phosphoinositide signaling to phospholipid biosynthesis and is essential for progression through the erythrocytic asexual cycle of P. falciparum [PMID:24895132, PMID:34866326]. It has a non-canonical domain organization in which a pleckstrin homology (PH) domain lies adjacent to the kinase domain, with two N-terminal calcium-binding EF-hands; the PH domain binds PI(4,5)P2, providing a lipid-recognition module that guides its subcellular targeting [PMID:24895132]. Functionally, PfCDPK7 is placed downstream of the lipid kinase PfPI4K: it binds 4'-phosphorylated phosphoinositides generated by PfPI4K, and pharmacological inhibition of PfPI4K disrupts the vesicular localization of PfCDPK7 [PMID:34866326]. Once localized, PfCDPK7 promotes phosphatidylcholine synthesis by phosphorylating and stabilizing two enzymes of the PC biosynthetic pathway, phosphoethanolamine-N-methyltransferase (PMT) and ethanolamine kinase (EK); loss of PfCDPK7 leaves both enzymes hypophosphorylated and leads to PMT degradation [PMID:34866326]. Genetic disruption stalls the ring-to-trophozoite transition and attenuates proliferation, establishing PfCDPK7 as essential for blood-stage growth [PMID:24895132].","teleology":[{"year":2014,"claim":"Establishing that PfCDPK7 is a structurally atypical kinase with a lipid-binding module addressed how a calcium-dependent kinase might be spatially targeted rather than acting diffusely in the cytosol.","evidence":"Domain analysis plus a biochemical PI(4,5)P2-binding assay on the PH domain","pmids":["24895132"],"confidence":"Medium","gaps":["Localization consequence of PI(4,5)P2 binding was inferred, not directly shown","Kinase substrates and calcium dependence of activity not defined at this stage"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2014,"claim":"Genetic disruption tested whether PfCDPK7 is required in asexual blood stages, revealing an essential role with a defined block at the ring-to-trophozoite transition.","evidence":"Reverse genetics disruption of PfCDPK7 with blood-stage growth and stage-progression readouts","pmids":["24895132"],"confidence":"Medium","gaps":["Molecular basis linking loss of kinase activity to the maturation block not resolved in this study","Single lab, single genetic strategy"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2018,"claim":"Identifying a physical interaction with the RCC1-motif protein PfRCC-PIP raised the possibility of a scaffolding/anchoring platform for PfCDPK7 regulation.","evidence":"Co-immunoprecipitation/pull-down between the RCC1-motif region and PfCDPK7","pmids":["30429842"],"confidence":"Low","gaps":["Single interaction assay with no functional follow-up for the CDPK7 interaction","No reciprocal validation or in vivo relevance to kinase activity established"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"claim":"Phosphoproteomics and lipidomics defined the downstream output of PfCDPK7, showing it drives phosphatidylcholine synthesis by phosphorylating and stabilizing PMT and EK.","evidence":"Quantitative phosphoproteomics and phospholipid analysis in PfCDPK7 knockdown/disruption parasites","pmids":["34866326"],"confidence":"High","gaps":["Direct kinase-substrate relationship versus indirect regulation not fully separated for each enzyme","Mechanism linking PMT hypophosphorylation to its degradation unresolved"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"claim":"Pharmacological epistasis placed PfCDPK7 downstream of PfPI4K, showing that PfPI4K-generated 4'-phosphorylated phosphoinositides recruit PfCDPK7 to vesicular membranes.","evidence":"PIP-binding assay, PfPI4K inhibitor (MMV390048) treatment with localization imaging, and phospholipid analysis","pmids":["34866326"],"confidence":"High","gaps":["Precise vesicular compartment identity not defined","Whether calcium/EF-hand engagement modulates lipid-dependent recruitment not addressed"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"The role of the N-terminal EF-hands and calcium signaling in controlling PfCDPK7 activation, and the full complement of its direct substrates, remain uncharacterized in the available corpus.","evidence":"","pmids":[],"confidence":"Low","gaps":["No demonstration that calcium binding regulates PfCDPK7 kinase activity in vivo","Direct substrate repertoire beyond PMT/EK not mapped","No structural model of the multidomain enzyme"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["PFPI4K (PI4-KINASE; GENERATES 4'-PHOSPHORYLATED PHOSPHOINOSITIDES THAT RECRUIT PFCDPK7) [#3]","PMT (PHOSPHOETHANOLAMINE-N-METHYLTRANSFERASE; SUBSTRATE STABILIZED BY PFCDPK7) [#2]","EK (ETHANOLAMINE KINASE; SUBSTRATE REGULATED BY PFCDPK7) [#2]","PFRCC-PIP (RCC1-MOTIF PROTEIN INTERACTING WITH PFCDPK7) [#4]"],"other_free_text":["Atypical CDPK domain architecture: PH domain adjacent to kinase domain with two N-terminal EF-hands [#0]","Genetic disruption stalls ring-to-trophozoite transition and attenuates asexual proliferation [#1]","Functions in a PfPI4K-to-phosphatidylcholine-biosynthesis signaling axis during the erythrocytic cycle [#2, #3]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"24895132","id":"PMC_24895132","title":"Regulation of Plasmodium falciparum development by calcium-dependent protein kinase 7 (PfCDPK7).","date":"2014","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/24895132","citation_count":43,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfCDPK7"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"34866326","id":"PMC_34866326","title":"PI4-kinase and PfCDPK7 signaling regulate phospholipid biosynthesis in Plasmodium falciparum.","date":"2021","source":"EMBO reports","url":"https://pubmed.ncbi.nlm.nih.gov/34866326","citation_count":13,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfCDPK7"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"30429842","id":"PMC_30429842","title":"Characterization of a Protein Phosphatase Type-1 and a Kinase Anchoring Protein in Plasmodium falciparum.","date":"2018","source":"Frontiers in microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/30429842","citation_count":11,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CDPK7"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4244,"output_tokens":1479,"usd":0.017458,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6446,"output_tokens":2812,"usd":0.051265,"stage2_stop_reason":"end_turn"},"total_usd":0.068723,"stage1_batch_id":"msgbatch_01DisAaTypwmC8QwdMBuePHo","stage2_batch_id":"msgbatch_0184zxZTqxiEfdYYfPMfkqjb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2014,\n      \"finding\": \"PfCDPK7 (PF3D7_1123100) has an atypical domain architecture comprising a pleckstrin homology (PH) domain adjacent to the kinase domain and two calcium-binding EF-hands at its N terminus; the PH domain was demonstrated to interact with PI(4,5)P2, which may guide its subcellular localization.\",\n      \"method\": \"Domain analysis and biochemical interaction assay (PI(4,5)P2 binding via PH domain)\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct binding assay for PI(4,5)P2 interaction demonstrated, single lab, but localization consequence inferred rather than directly shown\",\n      \"pmids\": [\"24895132\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"Disruption of PfCDPK7 (PF3D7_1123100) caused a marked reduction in blood-stage parasite growth, with maturation of rings to trophozoites stalled, and significantly attenuated parasite proliferation, establishing an essential role in the erythrocytic asexual cycle.\",\n      \"method\": \"Reverse genetics (disruption of PfCDPK7) with blood-stage growth and stage-progression phenotypic readout\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean loss-of-function with defined cellular phenotype, single lab\",\n      \"pmids\": [\"24895132\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"PfCDPK7 (PF3D7_1123100) promotes phosphatidylcholine (PC) synthesis by regulating two key enzymes in the PC synthesis pathway, phosphoethanolamine-N-methyltransferase (PMT) and ethanolamine kinase (EK); in the absence of PfCDPK7 both enzymes are hypophosphorylated and PMT is degraded.\",\n      \"method\": \"Quantitative phosphoproteomics and phospholipid analysis in PfCDPK7 conditional knockdown/disruption parasites\",\n      \"journal\": \"EMBO reports\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (phosphoproteomics, phospholipid lipidomics, genetic disruption) in a single rigorous study establishing pathway mechanism\",\n      \"pmids\": [\"34866326\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"PfCDPK7 (PF3D7_1123100) interacts with 4'-phosphorylated phosphoinositides (PIPs) generated by PI4-kinase (PfPI4K), and inhibition of PfPI4K activity disrupts the vesicular localization of PfCDPK7, placing PfCDPK7 downstream of PfPI4K in a signaling pathway that controls phospholipid biosynthesis.\",\n      \"method\": \"PIP-binding assay, inhibitor (MMV39048) treatment with subcellular localization imaging, and phospholipid analysis\",\n      \"journal\": \"EMBO reports\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — direct PIP-binding assay, pharmacological epistasis with PI4K inhibitor, localization imaging, and functional lipidomic readout — multiple orthogonal methods in one study\",\n      \"pmids\": [\"34866326\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"The RCC1-motif-containing region of the P. falciparum protein PfRCC-PIP was demonstrated to interact with PfCDPK7 (PF3D7_1123100), suggesting PfRCC-PIP acts as a kinase anchoring protein that may provide a platform for phosphorylation/dephosphorylation regulation involving PfCDPK7.\",\n      \"method\": \"Protein interaction assay (co-immunoprecipitation / pull-down between RCC1-motif region and CDPK7)\",\n      \"journal\": \"Frontiers in microbiology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single interaction assay, single lab, no functional follow-up specifically for the CDPK7 interaction\",\n      \"pmids\": [\"30429842\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PfCDPK7 (PF3D7_1123100) is an atypical calcium-dependent protein kinase that is recruited to vesicular membranes through binding of its pleckstrin homology domain to 4'-phosphorylated phosphoinositides generated by PfPI4K; once localized, it phosphorylates and stabilizes key enzymes of the phosphatidylcholine biosynthesis pathway (PMT and EK), and its activity is essential for the ring-to-trophozoite transition and proliferation during the erythrocytic asexual cycle of P. falciparum.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PfCDPK7 (PF3D7_1123100) is an atypical calcium-dependent protein kinase that couples phosphoinositide signaling to phospholipid biosynthesis and is essential for progression through the erythrocytic asexual cycle of P. falciparum [#0, #1, #2]. It has a non-canonical domain organization in which a pleckstrin homology (PH) domain lies adjacent to the kinase domain, with two N-terminal calcium-binding EF-hands; the PH domain binds PI(4,5)P2, providing a lipid-recognition module that guides its subcellular targeting [#0]. Functionally, PfCDPK7 is placed downstream of the lipid kinase PfPI4K: it binds 4'-phosphorylated phosphoinositides generated by PfPI4K, and pharmacological inhibition of PfPI4K disrupts the vesicular localization of PfCDPK7 [#3]. Once localized, PfCDPK7 promotes phosphatidylcholine synthesis by phosphorylating and stabilizing two enzymes of the PC biosynthetic pathway, phosphoethanolamine-N-methyltransferase (PMT) and ethanolamine kinase (EK); loss of PfCDPK7 leaves both enzymes hypophosphorylated and leads to PMT degradation [#2]. Genetic disruption stalls the ring-to-trophozoite transition and attenuates proliferation, establishing PfCDPK7 as essential for blood-stage growth [#1].\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Establishing that PfCDPK7 is a structurally atypical kinase with a lipid-binding module addressed how a calcium-dependent kinase might be spatially targeted rather than acting diffusely in the cytosol.\",\n      \"evidence\": \"Domain analysis plus a biochemical PI(4,5)P2-binding assay on the PH domain\",\n      \"pmids\": [\"24895132\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Localization consequence of PI(4,5)P2 binding was inferred, not directly shown\",\n        \"Kinase substrates and calcium dependence of activity not defined at this stage\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Genetic disruption tested whether PfCDPK7 is required in asexual blood stages, revealing an essential role with a defined block at the ring-to-trophozoite transition.\",\n      \"evidence\": \"Reverse genetics disruption of PfCDPK7 with blood-stage growth and stage-progression readouts\",\n      \"pmids\": [\"24895132\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Molecular basis linking loss of kinase activity to the maturation block not resolved in this study\",\n        \"Single lab, single genetic strategy\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Identifying a physical interaction with the RCC1-motif protein PfRCC-PIP raised the possibility of a scaffolding/anchoring platform for PfCDPK7 regulation.\",\n      \"evidence\": \"Co-immunoprecipitation/pull-down between the RCC1-motif region and PfCDPK7\",\n      \"pmids\": [\"30429842\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Single interaction assay with no functional follow-up for the CDPK7 interaction\",\n        \"No reciprocal validation or in vivo relevance to kinase activity established\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Phosphoproteomics and lipidomics defined the downstream output of PfCDPK7, showing it drives phosphatidylcholine synthesis by phosphorylating and stabilizing PMT and EK.\",\n      \"evidence\": \"Quantitative phosphoproteomics and phospholipid analysis in PfCDPK7 knockdown/disruption parasites\",\n      \"pmids\": [\"34866326\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Direct kinase-substrate relationship versus indirect regulation not fully separated for each enzyme\",\n        \"Mechanism linking PMT hypophosphorylation to its degradation unresolved\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Pharmacological epistasis placed PfCDPK7 downstream of PfPI4K, showing that PfPI4K-generated 4'-phosphorylated phosphoinositides recruit PfCDPK7 to vesicular membranes.\",\n      \"evidence\": \"PIP-binding assay, PfPI4K inhibitor (MMV390048) treatment with localization imaging, and phospholipid analysis\",\n      \"pmids\": [\"34866326\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Precise vesicular compartment identity not defined\",\n        \"Whether calcium/EF-hand engagement modulates lipid-dependent recruitment not addressed\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The role of the N-terminal EF-hands and calcium signaling in controlling PfCDPK7 activation, and the full complement of its direct substrates, remain uncharacterized in the available corpus.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No demonstration that calcium binding regulates PfCDPK7 kinase activity in vivo\",\n        \"Direct substrate repertoire beyond PMT/EK not mapped\",\n        \"No structural model of the multidomain enzyme\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0004672\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"GO:0005509\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0005546\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0080025\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0030133\", \"supporting_discovery_ids\": [3]},\n      {\"term_id\": \"GO:0016020\", \"supporting_discovery_ids\": [0, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006656\", \"supporting_discovery_ids\": [2]},\n      {\"term_id\": \"GO:0046488\", \"supporting_discovery_ids\": [3]},\n      {\"term_id\": \"GO:0016310\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\n      \"PfPI4K (PI4-kinase; generates 4'-phosphorylated phosphoinositides that recruit PfCDPK7) [#3]\",\n      \"PMT (phosphoethanolamine-N-methyltransferase; substrate stabilized by PfCDPK7) [#2]\",\n      \"EK (ethanolamine kinase; substrate regulated by PfCDPK7) [#2]\",\n      \"PfRCC-PIP (RCC1-motif protein interacting with PfCDPK7) [#4]\"\n    ],\n    \"other_free_text\": [\n      \"Atypical CDPK domain architecture: PH domain adjacent to kinase domain with two N-terminal EF-hands [#0]\",\n      \"Genetic disruption stalls ring-to-trophozoite transition and attenuates asexual proliferation [#1]\",\n      \"Functions in a PfPI4K-to-phosphatidylcholine-biosynthesis signaling axis during the erythrocytic cycle [#2, #3]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1123100","name":null,"product":"calcium-dependent protein kinase 7","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0925200","name":null,"product":"calcium-dependent protein kinase 7","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0920900","name":null,"product":"calcium-dependent protein kinase 7, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"CDPK7","evaluation":null}