{"gene":"PF3D7_1031700","run_date":"2026-09-08T12:51:28","timeline":{"discoveries":[{"year":2011,"finding":"PfI3 (PF3D7_1031700) physically interacts with PfPP1 with high affinity (apparent Kd ~100 nM), as demonstrated by multiple in vitro binding assays. The conserved KVVRW motif (residues 41–45) is critical for this interaction; substituting Trp45 with Ala severely reduces binding to PfPP1.","method":"Multiple in vitro binding assays (biophysical/biochemical); site-directed mutagenesis of the KVVRW motif","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1 / Moderate — quantitative in vitro interaction with Kd measurement plus mutagenesis confirming critical residue, single lab but multiple orthogonal methods","pmids":["22128182"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2011,"finding":"Unlike yeast I3 (Ypi1) and human I3, which inhibit PP1, PfI3 (PF3D7_1031700) increases PfPP1 phosphatase activity in vitro, demonstrating a functionally distinct role as a positive regulator of PfPP1.","method":"In vitro phosphatase activity assay; functional complementation assay in I3-deficient yeast (Ypi1 deletion strain)","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1 / Moderate — direct enzymatic assay combined with heterologous complementation, single lab but two orthogonal methods","pmids":["22128182"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2011,"finding":"PfI3 (PF3D7_1031700) is an intrinsically disordered protein, as shown by NMR analysis.","method":"NMR spectroscopy","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — NMR structural analysis in a single study, no functional mutagenesis of disordered regions","pmids":["22128182"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2011,"finding":"PfI3 (PF3D7_1031700) localizes predominantly to the nucleus in all blood stage parasites, as determined by GFP tagging, consistent with a regulatory role on nuclear PfPP1.","method":"Live fluorescence microscopy of GFP-tagged PfI3","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — direct localization experiment with tagged protein, single lab, single method","pmids":["22128182"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2011,"finding":"PfI3 (PF3D7_1031700) is essential for blood-stage parasite survival; repeated attempts to generate knock-out parasites failed despite locus accessibility, indicating an essential role in growth and/or survival.","method":"Reverse genetics (attempted gene knockout)","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — negative KO result as indirect evidence of essentiality, single lab, single approach","pmids":["22128182"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2022,"finding":"I3 (the Plasmodium berghei ortholog of PF3D7_1031700) is drastically hypophosphorylated in PbLRR1-depleted parasites, and I3 was detected within the LRR1/PP1 interactome, suggesting that the phosphorylation status of PbI3 is regulated by the PP1–LRR1 complex.","method":"Phosphoproteomics in PbLRR1-depleted parasites; co-immunoprecipitation/interactome analysis (affinity pulldown + mass spectrometry)","journal":"Open biology","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — phosphoproteomic detection combined with interactome MS, single lab, finding is correlative regarding upstream kinase/phosphatase identity","pmids":["35920043"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]}],"current_model":"PF3D7_1031700 (I3/PfI3) is an intrinsically disordered, nuclear-localized protein that binds directly to PfPP1 via a conserved KVVRW motif and, uniquely among I3 homologs, acts as a positive regulator (activator) of PfPP1 phosphatase activity in vitro; it is essential for blood-stage parasite survival, and its phosphorylation state is influenced by the PP1–LRR1 complex in Plasmodium berghei."},"narrative":{"mechanistic_narrative":"PF3D7_1031700 (I3/PfI3) is a regulator of the Plasmodium falciparum protein phosphatase PfPP1 that, in contrast to its yeast and human homologs which inhibit PP1, uniquely acts as a positive regulator of PfPP1 phosphatase activity [PMID:22128182]. In P. falciparum it binds PfPP1 directly and with high affinity (apparent Kd ~100 nM) through a conserved KVVRW motif, and mutation of Trp45 within this motif severely disrupts the interaction [PMID:22128182]. PfI3 is an intrinsically disordered protein that localizes predominantly to the nucleus across blood-stage parasites, consistent with a role in modulating nuclear PfPP1 [PMID:22128182], and it is essential for blood-stage parasite survival [PMID:22128182]. In P. berghei, the I3 ortholog is a substrate whose phosphorylation state is controlled by the PP1–LRR1 complex, becoming hypophosphorylated upon LRR1 depletion and appearing within the LRR1/PP1 interactome [PMID:35920043]. Beyond its interaction with and activation of PfPP1, no further downstream substrates or effector mechanisms of PF3D7_1031700 have been characterized in the available corpus.","teleology":[{"year":2011,"claim":"Establishing whether PF3D7_1031700 engages the parasite PP1 catalytic subunit, and through what molecular determinant, defined it as a genuine PP1 partner and identified the residues driving the interaction.","evidence":"Multiple in vitro binding assays with Kd measurement and site-directed mutagenesis of the KVVRW motif, in P. falciparum","pmids":["22128182"],"confidence":"High","gaps":["Whether the interaction occurs and is regulated in vivo in the parasite nucleus was not tested","The structural basis of KVVRW docking onto PfPP1 was not resolved"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2011,"claim":"Determining the functional consequence of the PfI3–PfPP1 interaction revealed that, unlike its inhibitory homologs, PF3D7_1031700 is a positive regulator that activates PfPP1, reframing the family's assumed role.","evidence":"In vitro phosphatase activity assay plus functional complementation of an I3-deficient (Ypi1 deletion) yeast strain, for P. falciparum I3","pmids":["22128182"],"confidence":"High","gaps":["The physiological substrates whose dephosphorylation is enhanced by PfI3 were not identified","How activation rather than inhibition is achieved mechanistically was not defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2011,"claim":"Characterizing the biophysical state and cellular distribution of PF3D7_1031700 placed its regulatory activity in a specific compartment and structural context.","evidence":"NMR spectroscopy showing intrinsic disorder and live fluorescence microscopy of GFP-tagged PfI3 showing nuclear localization, in P. falciparum blood stages","pmids":["22128182"],"confidence":"Medium","gaps":["Whether disorder is required for PfPP1 binding or activation was not tested by mutagenesis","Nuclear targeting signals and dynamics across the cell cycle were not mapped"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2011,"claim":"Testing the genetic requirement for PF3D7_1031700 established it as essential for asexual blood-stage growth, marking it as biologically indispensable.","evidence":"Reverse genetics with repeated failed knockout attempts despite locus accessibility, in P. falciparum","pmids":["22128182"],"confidence":"Medium","gaps":["Essentiality is inferred from failed knockout rather than a conditional depletion phenotype","The essential process requiring PfI3 was not defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2022,"claim":"Probing how PF3D7_1031700 is itself regulated in vivo showed that the I3 ortholog is a phospho-target linked to the PP1–LRR1 complex, extending its role from PP1 activator to a component embedded in a regulated PP1 network.","evidence":"Phosphoproteomics in PbLRR1-depleted parasites and affinity pulldown/mass spectrometry interactome analysis, in P. berghei","pmids":["35920043"],"confidence":"Medium","gaps":["Correlative regarding which kinase phosphorylates I3 and whether PP1 directly dephosphorylates it","Functional consequence of I3 hypophosphorylation on PP1 activation was not tested","Shown in P. berghei, not confirmed in P. falciparum"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":null,"claim":"The downstream substrates whose dephosphorylation PF3D7_1031700 promotes, and how its own phosphorylation state feeds back on PfPP1 activation during the asexual cycle, remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No physiological PfPP1 substrate regulated by PfI3 has been identified","The kinase acting on I3 and the functional impact of its phosphorylation are unknown","No structure of the PfI3–PfPP1 complex has been determined"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["PP1–LRR1 complex/interactome (P. berghei ortholog detected as component/substrate) [#5]"],"partners":["PFPP1 (PROTEIN PHOSPHATASE 1, DIRECT HIGH-AFFINITY BINDING VIA KVVRW MOTIF) [#0, #1]","PP1–LRR1 COMPLEX (P. BERGHEI; REGULATES I3 PHOSPHORYLATION) [#5]"],"other_free_text":["Intrinsically disordered protein [#2]","Conserved KVVRW motif (residues 41–45); Trp45 critical for PfPP1 binding [#0]","Unique positive regulator (activator) of PfPP1, opposite to inhibitory yeast (Ypi1) and human I3 homologs [#1]","Essential for asexual blood-stage survival in P. falciparum [#4]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"22128182","id":"PMC_22128182","title":"Plasmodium falciparum inhibitor-3 homolog increases protein phosphatase type 1 activity and is essential for parasitic survival.","date":"2011","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/22128182","citation_count":18,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfI3"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"35920043","id":"PMC_35920043","title":"Plasmodium berghei leucine-rich repeat protein 1 downregulates protein phosphatase 1 activity and is required for efficient oocyst development.","date":"2022","source":"Open biology","url":"https://pubmed.ncbi.nlm.nih.gov/35920043","citation_count":5,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PbI3"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"35162991","id":"PMC_35162991","title":"Mapping PP1c and Its Inhibitor 2 Interactomes Reveals Conserved and Specific Networks in Asexual and Sexual Stages of Plasmodium.","date":"2022","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/35162991","citation_count":3,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4498,"output_tokens":1495,"usd":0.017959,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6465,"output_tokens":2673,"usd":0.049575,"stage2_stop_reason":"end_turn"},"total_usd":0.067534,"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\": 2011,\n      \"finding\": \"PfI3 (PF3D7_1031700) physically interacts with PfPP1 with high affinity (apparent Kd ~100 nM), as demonstrated by multiple in vitro binding assays. The conserved KVVRW motif (residues 41–45) is critical for this interaction; substituting Trp45 with Ala severely reduces binding to PfPP1.\",\n      \"method\": \"Multiple in vitro binding assays (biophysical/biochemical); site-directed mutagenesis of the KVVRW motif\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — quantitative in vitro interaction with Kd measurement plus mutagenesis confirming critical residue, single lab but multiple orthogonal methods\",\n      \"pmids\": [\"22128182\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"Unlike yeast I3 (Ypi1) and human I3, which inhibit PP1, PfI3 (PF3D7_1031700) increases PfPP1 phosphatase activity in vitro, demonstrating a functionally distinct role as a positive regulator of PfPP1.\",\n      \"method\": \"In vitro phosphatase activity assay; functional complementation assay in I3-deficient yeast (Ypi1 deletion strain)\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — direct enzymatic assay combined with heterologous complementation, single lab but two orthogonal methods\",\n      \"pmids\": [\"22128182\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"PfI3 (PF3D7_1031700) is an intrinsically disordered protein, as shown by NMR analysis.\",\n      \"method\": \"NMR spectroscopy\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — NMR structural analysis in a single study, no functional mutagenesis of disordered regions\",\n      \"pmids\": [\"22128182\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"PfI3 (PF3D7_1031700) localizes predominantly to the nucleus in all blood stage parasites, as determined by GFP tagging, consistent with a regulatory role on nuclear PfPP1.\",\n      \"method\": \"Live fluorescence microscopy of GFP-tagged PfI3\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — direct localization experiment with tagged protein, single lab, single method\",\n      \"pmids\": [\"22128182\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"PfI3 (PF3D7_1031700) is essential for blood-stage parasite survival; repeated attempts to generate knock-out parasites failed despite locus accessibility, indicating an essential role in growth and/or survival.\",\n      \"method\": \"Reverse genetics (attempted gene knockout)\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — negative KO result as indirect evidence of essentiality, single lab, single approach\",\n      \"pmids\": [\"22128182\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"I3 (the Plasmodium berghei ortholog of PF3D7_1031700) is drastically hypophosphorylated in PbLRR1-depleted parasites, and I3 was detected within the LRR1/PP1 interactome, suggesting that the phosphorylation status of PbI3 is regulated by the PP1–LRR1 complex.\",\n      \"method\": \"Phosphoproteomics in PbLRR1-depleted parasites; co-immunoprecipitation/interactome analysis (affinity pulldown + mass spectrometry)\",\n      \"journal\": \"Open biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — phosphoproteomic detection combined with interactome MS, single lab, finding is correlative regarding upstream kinase/phosphatase identity\",\n      \"pmids\": [\"35920043\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_1031700 (I3/PfI3) is an intrinsically disordered, nuclear-localized protein that binds directly to PfPP1 via a conserved KVVRW motif and, uniquely among I3 homologs, acts as a positive regulator (activator) of PfPP1 phosphatase activity in vitro; it is essential for blood-stage parasite survival, and its phosphorylation state is influenced by the PP1–LRR1 complex in Plasmodium berghei.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_1031700 (I3/PfI3) is a regulator of the Plasmodium falciparum protein phosphatase PfPP1 that, in contrast to its yeast and human homologs which inhibit PP1, uniquely acts as a positive regulator of PfPP1 phosphatase activity [#1]. In P. falciparum it binds PfPP1 directly and with high affinity (apparent Kd ~100 nM) through a conserved KVVRW motif, and mutation of Trp45 within this motif severely disrupts the interaction [#0]. PfI3 is an intrinsically disordered protein that localizes predominantly to the nucleus across blood-stage parasites, consistent with a role in modulating nuclear PfPP1 [#2, #3], and it is essential for blood-stage parasite survival [#4]. In P. berghei, the I3 ortholog is a substrate whose phosphorylation state is controlled by the PP1\\u2013LRR1 complex, becoming hypophosphorylated upon LRR1 depletion and appearing within the LRR1/PP1 interactome [#5]. Beyond its interaction with and activation of PfPP1, no further downstream substrates or effector mechanisms of PF3D7_1031700 have been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2011,\n      \"claim\": \"Establishing whether PF3D7_1031700 engages the parasite PP1 catalytic subunit, and through what molecular determinant, defined it as a genuine PP1 partner and identified the residues driving the interaction.\",\n      \"evidence\": \"Multiple in vitro binding assays with Kd measurement and site-directed mutagenesis of the KVVRW motif, in P. falciparum\",\n      \"pmids\": [\"22128182\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Whether the interaction occurs and is regulated in vivo in the parasite nucleus was not tested\",\n        \"The structural basis of KVVRW docking onto PfPP1 was not resolved\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Determining the functional consequence of the PfI3\\u2013PfPP1 interaction revealed that, unlike its inhibitory homologs, PF3D7_1031700 is a positive regulator that activates PfPP1, reframing the family's assumed role.\",\n      \"evidence\": \"In vitro phosphatase activity assay plus functional complementation of an I3-deficient (Ypi1 deletion) yeast strain, for P. falciparum I3\",\n      \"pmids\": [\"22128182\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"The physiological substrates whose dephosphorylation is enhanced by PfI3 were not identified\",\n        \"How activation rather than inhibition is achieved mechanistically was not defined\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Characterizing the biophysical state and cellular distribution of PF3D7_1031700 placed its regulatory activity in a specific compartment and structural context.\",\n      \"evidence\": \"NMR spectroscopy showing intrinsic disorder and live fluorescence microscopy of GFP-tagged PfI3 showing nuclear localization, in P. falciparum blood stages\",\n      \"pmids\": [\"22128182\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Whether disorder is required for PfPP1 binding or activation was not tested by mutagenesis\",\n        \"Nuclear targeting signals and dynamics across the cell cycle were not mapped\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Testing the genetic requirement for PF3D7_1031700 established it as essential for asexual blood-stage growth, marking it as biologically indispensable.\",\n      \"evidence\": \"Reverse genetics with repeated failed knockout attempts despite locus accessibility, in P. falciparum\",\n      \"pmids\": [\"22128182\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Essentiality is inferred from failed knockout rather than a conditional depletion phenotype\",\n        \"The essential process requiring PfI3 was not defined\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Probing how PF3D7_1031700 is itself regulated in vivo showed that the I3 ortholog is a phospho-target linked to the PP1\\u2013LRR1 complex, extending its role from PP1 activator to a component embedded in a regulated PP1 network.\",\n      \"evidence\": \"Phosphoproteomics in PbLRR1-depleted parasites and affinity pulldown/mass spectrometry interactome analysis, in P. berghei\",\n      \"pmids\": [\"35920043\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Correlative regarding which kinase phosphorylates I3 and whether PP1 directly dephosphorylates it\",\n        \"Functional consequence of I3 hypophosphorylation on PP1 activation was not tested\",\n        \"Shown in P. berghei, not confirmed in P. falciparum\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The downstream substrates whose dephosphorylation PF3D7_1031700 promotes, and how its own phosphorylation state feeds back on PfPP1 activation during the asexual cycle, remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No physiological PfPP1 substrate regulated by PfI3 has been identified\",\n        \"The kinase acting on I3 and the functional impact of its phosphorylation are unknown\",\n        \"No structure of the PfI3\\u2013PfPP1 complex has been determined\"\n      ],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008157\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0019212\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0019904\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0035304\", \"supporting_discovery_ids\": [1, 5]}\n    ],\n    \"complexes\": [\n      \"PP1\\u2013LRR1 complex/interactome (P. berghei ortholog detected as component/substrate) [#5]\"\n    ],\n    \"partners\": [\n      \"PfPP1 (protein phosphatase 1, direct high-affinity binding via KVVRW motif) [#0, #1]\",\n      \"PP1\\u2013LRR1 complex (P. berghei; regulates I3 phosphorylation) [#5]\"\n    ],\n    \"other_free_text\": [\n      \"Intrinsically disordered protein [#2]\",\n      \"Conserved KVVRW motif (residues 41\\u201345); Trp45 critical for PfPP1 binding [#0]\",\n      \"Unique positive regulator (activator) of PfPP1, opposite to inhibitory yeast (Ypi1) and human I3 homologs [#1]\",\n      \"Essential for asexual blood-stage survival in P. falciparum [#4]\"\n    ]\n  }\n}","audit_flag":{"gene":"PF3D7_1031700","tier":"IDENTITY_CHECK","verdict":"identity unverified","subtype":"names_other_cards","uniprot_band":"","rules_fired":"R12","issue":"No cited paper names this card; 2 of 2 cited papers name other catalogue genes (PF3D7_1414400, PF3D7_1032800). The summary may describe one of those genes."},"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1031700","name":null,"product":"protein phosphatase inhibitor 3","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0515500","name":null,"product":"protein phosphatase inhibitor 3, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0616400","name":null,"product":"protein phosphatase inhibitor 3, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"I3","evaluation":null}