{"gene":"PF3D7_0802800","run_date":"2026-09-08T12:51:27","timeline":{"discoveries":[{"year":2005,"finding":"P. falciparum CNA (calcineurin catalytic subunit A) associates with Hsp90 in vivo; geldanamycin disrupts this association while cyclosporin A does not. Mutations in CNA found in CsA-resistant parasite clones confer CsA-resistant phosphatase activity in vitro, demonstrating that CNA's phosphatase activity is the molecular target of the CsA/cyclophilin inhibitory complex.","method":"Co-immunoprecipitation (in vivo CNA–Hsp90 association), in vitro phosphatase activity assay with CsA-resistant mutant CnA, sequencing of CsA-resistant clones","journal":"Molecular and biochemical parasitology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal co-IP for Hsp90 association and in vitro phosphatase assay with resistance mutant, single lab, two orthogonal methods","pmids":["15811524"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2004,"finding":"P. falciparum CNA (PP2B catalytic subunit) is post-translationally processed by proteolytic cleavage to generate a constitutively active catalytic core that is unresponsive or less responsive to Ca²⁺, whereas the full-length phosphatase requires Ca²⁺ for stimulation; this processing occurs rapidly and in vivo.","method":"Biochemical fractionation and in vitro phosphatase activity assays comparing full-length and proteolytically processed forms; in vivo processing demonstrated in parasite lysates","journal":"BMC molecular biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — in vitro enzymatic assays plus in vivo processing demonstration, single lab, two orthogonal methods","pmids":["15230980"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2013,"finding":"P. falciparum calcineurin (PfCN, encoded by CNA and its regulatory subunit) acts as a Ca²⁺-dependent phosphatase essential for microneme exocytosis: its activity increases upon low-K⁺ stimulus, and its inhibition by FK506 or cyclosporin A blocks dephosphorylation and depolymerization of apical actin, thereby preventing AMA-1 secretion and erythrocyte invasion.","method":"Calcineurin activity assay in merozoites after low-K⁺ treatment; pharmacological inhibition (FK506, CsA) with readout of AMA-1 secretion (ELISA/Western) and actin phosphorylation/polymerization state","journal":"Cellular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — functional phosphatase activity assay combined with specific inhibitors and multiple downstream readouts, single lab","pmids":["23910910"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"finding":"P. falciparum calcineurin (the complex including CNA) critically regulates and stabilizes attachment of extracellular merozoites to host erythrocytes before intracellular entry, functioning specifically in receptor-mediated host cell recognition, as determined by reverse-genetic and chemical-genetic approaches.","method":"Reverse-genetics (conditional knockdown/disruption of calcineurin subunits) and chemical-genetic approaches; parasite attachment and invasion assays distinguishing receptor-dependent and receptor-independent adhesion modes","journal":"Cell host & microbe","confidence":"High","confidence_rationale":"Tier 2 / Strong — reverse-genetic and chemical-genetic approaches in two apicomplexan systems with defined phenotypic readouts; published in high-impact peer-reviewed journal with 72 citations","pmids":["26118996"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_0802800 (CNA), the catalytic subunit A of P. falciparum calcineurin (PP2B), functions as a Ca²⁺-regulated serine/threonine phosphatase that: (1) associates with Hsp90 in vivo and is inhibited by CsA/cyclophilin complexes; (2) is post-translationally cleaved to yield a constitutively active, Ca²⁺-independent catalytic core; (3) dephosphorylates apical actin to drive Ca²⁺-triggered microneme exocytosis (AMA-1 secretion) during invasion; and (4) stabilizes receptor-dependent attachment of merozoites to host erythrocytes, placing CNA at the intersection of Ca²⁺ signaling and host cell invasion machinery."},"narrative":{"mechanistic_narrative":"PF3D7_0802800 (CNA) is the catalytic subunit A of Plasmodium falciparum calcineurin (PP2B), a Ca²⁺-regulated serine/threonine phosphatase that couples Ca²⁺ signaling to erythrocyte invasion by the malaria parasite [PMID:23910910, PMID:26118996]. Its phosphatase activity is the direct molecular target of the cyclosporin A/cyclophilin inhibitory complex, established by CsA-resistant CNA mutants that confer CsA-resistant phosphatase activity in vitro; CNA also associates in vivo with Hsp90, an interaction disrupted by geldanamycin but not CsA [PMID:15811524]. CNA activity is controlled at two levels: it is stimulated by Ca²⁺ in the full-length enzyme, and it is subject to rapid in vivo proteolytic processing that liberates a constitutively active catalytic core largely uncoupled from Ca²⁺ [PMID:15230980]. Functionally, Ca²⁺-activated calcineurin dephosphorylates and depolymerizes apical actin to drive microneme exocytosis and AMA-1 secretion, a step blocked by FK506 or CsA [PMID:23910910], and it stabilizes receptor-dependent attachment of extracellular merozoites to host erythrocytes prior to entry [PMID:26118996]. Beyond these roles in invasion signaling, the direct substrate repertoire and structural basis of CNA regulation have not been further characterized in the available corpus.","teleology":[{"year":2004,"claim":"It was unknown how CNA phosphatase activity is regulated; this work showed that proteolytic processing generates a constitutively active catalytic core, establishing a Ca²⁺-independent activation mechanism distinct from allosteric Ca²⁺ stimulation of the full-length enzyme.","evidence":"Biochemical fractionation and in vitro phosphatase assays comparing full-length and processed forms, with in vivo processing shown in parasite lysates","pmids":["15230980"],"confidence":"Medium","gaps":["Protease responsible for cleavage and the cleavage site are not identified","Physiological trigger and timing of processing during the parasite cycle are unresolved","Whether processed and Ca²⁺-regulated forms act on distinct substrates is unknown"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2005,"claim":"The molecular target of the CsA/cyclophilin inhibitory complex was uncertain; demonstrating that CsA-resistance mutations in CNA confer CsA-resistant phosphatase activity established CNA's catalytic activity as the direct target, while co-IP revealed an Hsp90 association.","evidence":"Reciprocal co-immunoprecipitation of CNA with Hsp90, in vitro phosphatase assays with CsA-resistant mutant CNA, and sequencing of CsA-resistant clones","pmids":["15811524"],"confidence":"Medium","gaps":["Functional consequence of the CNA–Hsp90 interaction for phosphatase activity is not defined","Whether Hsp90 modulates CNA folding, stability, or substrate targeting is untested"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2013,"claim":"The cellular process controlled by calcineurin was undefined; this work linked Ca²⁺-activated CNA-containing phosphatase to microneme exocytosis by showing it dephosphorylates and depolymerizes apical actin to enable AMA-1 secretion and invasion.","evidence":"Calcineurin activity assay in low-K⁺-stimulated merozoites plus FK506/CsA inhibition with AMA-1 secretion and actin phosphorylation/polymerization readouts","pmids":["23910910"],"confidence":"Medium","gaps":["Direct dephosphorylation of actin (or an actin regulator) by CNA is inferred, not shown at the substrate level","The specific CNA phosphosite substrate driving depolymerization is not identified"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"claim":"It was unclear which invasion step calcineurin governs; reverse- and chemical-genetic disruption showed calcineurin specifically stabilizes receptor-dependent attachment of merozoites to erythrocytes before entry.","evidence":"Conditional disruption/knockdown of calcineurin subunits and chemical-genetic approaches with attachment/invasion assays distinguishing receptor-dependent and -independent adhesion","pmids":["26118996"],"confidence":"High","gaps":["The CNA substrates governing attachment stabilization are unidentified","The individual contribution of the CNA subunit versus the regulatory subunit to this phenotype is not resolved"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"The direct physiological substrate set of CNA and the structural/regulatory basis linking Ca²⁺ sensing, proteolytic activation, and Hsp90 association remain open.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No CNA phosphosite substrate has been biochemically defined","No structural model of CNA or its complex is available in the corpus","Whether processed catalytic core operates in invasion in vivo is untested"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Calcineurin (PP2B) holoenzyme comprising CNA catalytic subunit and its regulatory subunit"],"partners":["HSP90 (IN VIVO ASSOCIATION)","CYCLOPHILIN/CYCLOSPORIN A INHIBITORY COMPLEX (INHIBITORY TARGET)"],"other_free_text":["CNA phosphatase activity is inhibited by FK506 and cyclosporin A [#2]; CsA-resistance mutations in CNA confer resistant activity [#0].","Full-length CNA is Ca²⁺-stimulated; proteolytic processing yields a constitutively active, largely Ca²⁺-independent catalytic core [#1].","Functionally implicated in dephosphorylation/depolymerization of apical actin, AMA-1 microneme secretion, and receptor-dependent merozoite attachment to erythrocytes [#2, #3]."]}},"prefetch_data":{},"corpus_meta":[{"pmid":"26118996","id":"PMC_26118996","title":"Parasite Calcineurin Regulates Host Cell Recognition and Attachment by Apicomplexans.","date":"2015","source":"Cell host & microbe","url":"https://pubmed.ncbi.nlm.nih.gov/26118996","citation_count":72,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"18793411","id":"PMC_18793411","title":"The protein-phosphatome of the human malaria parasite Plasmodium falciparum.","date":"2008","source":"BMC genomics","url":"https://pubmed.ncbi.nlm.nih.gov/18793411","citation_count":57,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"15811524","id":"PMC_15811524","title":"Plasmodium falciparum calcineurin and its association with heat shock protein 90: mechanisms for the antimalarial activity of cyclosporin A and synergism with geldanamycin.","date":"2005","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/15811524","citation_count":52,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CNA"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"23910910","id":"PMC_23910910","title":"Role of calcineurin and actin dynamics in regulated secretion of microneme proteins in Plasmodium falciparum merozoites during erythrocyte invasion.","date":"2013","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/23910910","citation_count":24,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"15230980","id":"PMC_15230980","title":"Post-translational generation of constitutively active cores from larger phosphatases in the malaria parasite, Plasmodium falciparum: implications for proteomics.","date":"2004","source":"BMC molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/15230980","citation_count":24,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5303,"output_tokens":1366,"usd":0.0182,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6353,"output_tokens":2542,"usd":0.047657,"stage2_stop_reason":"end_turn"},"total_usd":0.065857,"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\": 2005,\n      \"finding\": \"P. falciparum CNA (calcineurin catalytic subunit A) associates with Hsp90 in vivo; geldanamycin disrupts this association while cyclosporin A does not. Mutations in CNA found in CsA-resistant parasite clones confer CsA-resistant phosphatase activity in vitro, demonstrating that CNA's phosphatase activity is the molecular target of the CsA/cyclophilin inhibitory complex.\",\n      \"method\": \"Co-immunoprecipitation (in vivo CNA–Hsp90 association), in vitro phosphatase activity assay with CsA-resistant mutant CnA, sequencing of CsA-resistant clones\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal co-IP for Hsp90 association and in vitro phosphatase assay with resistance mutant, single lab, two orthogonal methods\",\n      \"pmids\": [\"15811524\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2004,\n      \"finding\": \"P. falciparum CNA (PP2B catalytic subunit) is post-translationally processed by proteolytic cleavage to generate a constitutively active catalytic core that is unresponsive or less responsive to Ca²⁺, whereas the full-length phosphatase requires Ca²⁺ for stimulation; this processing occurs rapidly and in vivo.\",\n      \"method\": \"Biochemical fractionation and in vitro phosphatase activity assays comparing full-length and proteolytically processed forms; in vivo processing demonstrated in parasite lysates\",\n      \"journal\": \"BMC molecular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — in vitro enzymatic assays plus in vivo processing demonstration, single lab, two orthogonal methods\",\n      \"pmids\": [\"15230980\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"P. falciparum calcineurin (PfCN, encoded by CNA and its regulatory subunit) acts as a Ca²⁺-dependent phosphatase essential for microneme exocytosis: its activity increases upon low-K⁺ stimulus, and its inhibition by FK506 or cyclosporin A blocks dephosphorylation and depolymerization of apical actin, thereby preventing AMA-1 secretion and erythrocyte invasion.\",\n      \"method\": \"Calcineurin activity assay in merozoites after low-K⁺ treatment; pharmacological inhibition (FK506, CsA) with readout of AMA-1 secretion (ELISA/Western) and actin phosphorylation/polymerization state\",\n      \"journal\": \"Cellular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — functional phosphatase activity assay combined with specific inhibitors and multiple downstream readouts, single lab\",\n      \"pmids\": [\"23910910\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"P. falciparum calcineurin (the complex including CNA) critically regulates and stabilizes attachment of extracellular merozoites to host erythrocytes before intracellular entry, functioning specifically in receptor-mediated host cell recognition, as determined by reverse-genetic and chemical-genetic approaches.\",\n      \"method\": \"Reverse-genetics (conditional knockdown/disruption of calcineurin subunits) and chemical-genetic approaches; parasite attachment and invasion assays distinguishing receptor-dependent and receptor-independent adhesion modes\",\n      \"journal\": \"Cell host & microbe\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reverse-genetic and chemical-genetic approaches in two apicomplexan systems with defined phenotypic readouts; published in high-impact peer-reviewed journal with 72 citations\",\n      \"pmids\": [\"26118996\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_0802800 (CNA), the catalytic subunit A of P. falciparum calcineurin (PP2B), functions as a Ca²⁺-regulated serine/threonine phosphatase that: (1) associates with Hsp90 in vivo and is inhibited by CsA/cyclophilin complexes; (2) is post-translationally cleaved to yield a constitutively active, Ca²⁺-independent catalytic core; (3) dephosphorylates apical actin to drive Ca²⁺-triggered microneme exocytosis (AMA-1 secretion) during invasion; and (4) stabilizes receptor-dependent attachment of merozoites to host erythrocytes, placing CNA at the intersection of Ca²⁺ signaling and host cell invasion machinery.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_0802800 (CNA) is the catalytic subunit A of Plasmodium falciparum calcineurin (PP2B), a Ca²⁺-regulated serine/threonine phosphatase that couples Ca²⁺ signaling to erythrocyte invasion by the malaria parasite [#2, #3]. Its phosphatase activity is the direct molecular target of the cyclosporin A/cyclophilin inhibitory complex, established by CsA-resistant CNA mutants that confer CsA-resistant phosphatase activity in vitro; CNA also associates in vivo with Hsp90, an interaction disrupted by geldanamycin but not CsA [#0]. CNA activity is controlled at two levels: it is stimulated by Ca²⁺ in the full-length enzyme, and it is subject to rapid in vivo proteolytic processing that liberates a constitutively active catalytic core largely uncoupled from Ca²⁺ [#1]. Functionally, Ca²⁺-activated calcineurin dephosphorylates and depolymerizes apical actin to drive microneme exocytosis and AMA-1 secretion, a step blocked by FK506 or CsA [#2], and it stabilizes receptor-dependent attachment of extracellular merozoites to host erythrocytes prior to entry [#3]. Beyond these roles in invasion signaling, the direct substrate repertoire and structural basis of CNA regulation have not been further characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2004,\n      \"claim\": \"It was unknown how CNA phosphatase activity is regulated; this work showed that proteolytic processing generates a constitutively active catalytic core, establishing a Ca²⁺-independent activation mechanism distinct from allosteric Ca²⁺ stimulation of the full-length enzyme.\",\n      \"evidence\": \"Biochemical fractionation and in vitro phosphatase assays comparing full-length and processed forms, with in vivo processing shown in parasite lysates\",\n      \"pmids\": [\"15230980\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Protease responsible for cleavage and the cleavage site are not identified\", \"Physiological trigger and timing of processing during the parasite cycle are unresolved\", \"Whether processed and Ca²⁺-regulated forms act on distinct substrates is unknown\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2005,\n      \"claim\": \"The molecular target of the CsA/cyclophilin inhibitory complex was uncertain; demonstrating that CsA-resistance mutations in CNA confer CsA-resistant phosphatase activity established CNA's catalytic activity as the direct target, while co-IP revealed an Hsp90 association.\",\n      \"evidence\": \"Reciprocal co-immunoprecipitation of CNA with Hsp90, in vitro phosphatase assays with CsA-resistant mutant CNA, and sequencing of CsA-resistant clones\",\n      \"pmids\": [\"15811524\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Functional consequence of the CNA–Hsp90 interaction for phosphatase activity is not defined\", \"Whether Hsp90 modulates CNA folding, stability, or substrate targeting is untested\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"The cellular process controlled by calcineurin was undefined; this work linked Ca²⁺-activated CNA-containing phosphatase to microneme exocytosis by showing it dephosphorylates and depolymerizes apical actin to enable AMA-1 secretion and invasion.\",\n      \"evidence\": \"Calcineurin activity assay in low-K⁺-stimulated merozoites plus FK506/CsA inhibition with AMA-1 secretion and actin phosphorylation/polymerization readouts\",\n      \"pmids\": [\"23910910\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct dephosphorylation of actin (or an actin regulator) by CNA is inferred, not shown at the substrate level\", \"The specific CNA phosphosite substrate driving depolymerization is not identified\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"It was unclear which invasion step calcineurin governs; reverse- and chemical-genetic disruption showed calcineurin specifically stabilizes receptor-dependent attachment of merozoites to erythrocytes before entry.\",\n      \"evidence\": \"Conditional disruption/knockdown of calcineurin subunits and chemical-genetic approaches with attachment/invasion assays distinguishing receptor-dependent and -independent adhesion\",\n      \"pmids\": [\"26118996\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"The CNA substrates governing attachment stabilization are unidentified\", \"The individual contribution of the CNA subunit versus the regulatory subunit to this phenotype is not resolved\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The direct physiological substrate set of CNA and the structural/regulatory basis linking Ca²⁺ sensing, proteolytic activation, and Hsp90 association remain open.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No CNA phosphosite substrate has been biochemically defined\", \"No structural model of CNA or its complex is available in the corpus\", \"Whether processed catalytic core operates in invasion in vivo is untested\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0004723\", \"supporting_discovery_ids\": [0, 1, 2]},\n      {\"term_id\": \"GO:0005509\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"localization\": [],\n    \"pathway\": [\n      {\"term_id\": \"GO:0019722\", \"supporting_discovery_ids\": [2, 3]},\n      {\"term_id\": \"GO:0044409\", \"supporting_discovery_ids\": [2, 3]}\n    ],\n    \"complexes\": [\"Calcineurin (PP2B) holoenzyme comprising CNA catalytic subunit and its regulatory subunit\"],\n    \"partners\": [\"Hsp90 (in vivo association)\", \"cyclophilin/cyclosporin A inhibitory complex (inhibitory target)\"],\n    \"other_free_text\": [\n      \"CNA phosphatase activity is inhibited by FK506 and cyclosporin A [#2]; CsA-resistance mutations in CNA confer resistant activity [#0].\",\n      \"Full-length CNA is Ca²⁺-stimulated; proteolytic processing yields a constitutively active, largely Ca²⁺-independent catalytic core [#1].\",\n      \"Functionally implicated in dephosphorylation/depolymerization of apical actin, AMA-1 microneme secretion, and receptor-dependent merozoite attachment to erythrocytes [#2, #3].\"\n    ]\n  }\n}","audit_flag":{"gene":"PF3D7_0802800","tier":"IDENTITY_CHECK","verdict":"identity unverified","subtype":"names_other_cards","uniprot_band":"","rules_fired":"R12","issue":"No cited paper names this card; 3 of 4 cited papers name other catalogue genes (PF3D7_0322000, PF3D7_0708400, PF3D7_0804800). The summary may describe one of those genes."},"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0802800","name":null,"product":"serine/threonine protein phosphatase 2B catalytic subunit A","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1227400","name":null,"product":"serine/threonine protein phosphatase 2B catalytic subunit A","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0116100","name":null,"product":"serine/threonine protein phosphatase 2B catalytic subunit A, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"CNA","evaluation":null}