{"gene":"TG_225490","gene_symbol":"CDPK2","run_date":"2026-09-08T11:06:44","timeline":{"discoveries":[{"year":2001,"finding":"TgCDPK2 mRNA is expressed in tachyzoites but no TgCDPK2 protein was detected, indicating TgCDPK2 is not the KT5926-sensitive kinase responsible for regulating Toxoplasma motility and host cell attachment in tachyzoites (that role belongs to TgCDPK1).","method":"Immunodetection / protein fractionation; RT-PCR for mRNA detection","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — direct protein detection experiment in a single study; negative result for protein expression is mechanistically informative","pmids":["11154702"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2015,"finding":"CDPK2 is a Ca2+-dependent protein kinase that localizes to amylopectin stores via a carbohydrate-binding module 20 (CBM20), and its kinase activity is regulated by EF-hands in response to Ca2+; loss of CDPK2 causes hyperaccumulation of amylopectin due to increased synthesis and loss of degradation, identifying CDPK2 as a critical regulator of amylopectin metabolism.","method":"Genetic knockout (CDPK2-deficient parasites), domain function analysis (CBM20 targeting, EF-hand regulation), phosphoproteomics to identify substrates whose phosphorylation is CDPK2-dependent, carbohydrate analysis","journal":"Cell host & microbe","confidence":"High","confidence_rationale":"Tier 2 / Strong — clean genetic KO with defined metabolic phenotype, domain dissection, and phosphoproteomic substrate identification, all in a single rigorous study replicated in mouse model","pmids":["26651943"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2015,"finding":"CDPK2 deficiency in bradyzoite stages causes massive amylopectin granule accumulation leading to gross morphological defects and complete ablation of cyst formation in a mouse model, demonstrating CDPK2 is essential for viable cyst development.","method":"Genetic knockout, mouse infection model, electron microscopy/morphological analysis","journal":"Cell host & microbe","confidence":"High","confidence_rationale":"Tier 2 / Strong — clean genetic KO with defined in vivo phenotype (complete loss of cyst formation) using multiple readouts","pmids":["26651943"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2017,"finding":"CDPK2 regulates glycogen phosphorylase (TgGP) activity through phosphorylation of Ser25; the phosphorylation-mimetic TgGP S25E mutant (which bypasses CDPK2-mediated activation) rescues amylopectin accumulation in Δcdpk2 parasites, placing CDPK2 upstream of TgGP in the amylopectin degradation pathway.","method":"Genetic epistasis: CDPK2 knockout combined with phosphorylation-null (S25A), phosphorylation-mimetic (S25E), and stop-codon (S25stop) TgGP mutants; amylopectin accumulation assay; mouse brain cyst counts","journal":"mBio","confidence":"High","confidence_rationale":"Tier 2 / Strong — genetic epistasis with reciprocal phosphomutants and rescue experiments clearly place CDPK2 upstream of TgGP in amylopectin catabolism","pmids":["28851850"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":"Pru"}]},{"year":2021,"finding":"Deleting the starch synthase (SS) gene in a Δcdpk2 background completely abolishes amylopectin accumulation and restores cyst formation and virulence in mice, demonstrating that the lethal phenotype of CDPK2 deficiency is entirely dependent on amylopectin overproduction and that CDPK2 acts downstream of SS-driven amylopectin synthesis.","method":"Double genetic knockout (ΔSS/Δcdpk2), mouse infection model, cyst formation assay, virulence assessment","journal":"Open biology","confidence":"High","confidence_rationale":"Tier 2 / Strong — clean double KO with in vivo rescue of cyst formation and virulence, mechanistically linking CDPK2 phenotype to amylopectin synthesis","pmids":["34129780"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"TgCDPK2 is a Ca2+-dependent protein kinase that localizes to amylopectin granules via its CBM20 domain and, upon Ca2+-mediated activation through its EF-hands, phosphorylates enzymes of amylopectin catabolism (including glycogen phosphorylase TgGP at Ser25) to promote amylopectin degradation; loss of CDPK2 causes amylopectin hyperaccumulation that is lethal to bradyzoites and abolishes tissue cyst formation."},"narrative":{"mechanistic_narrative":"TgCDPK2 is a Ca2+-dependent protein kinase that serves as a critical regulator of amylopectin metabolism in Toxoplasma gondii and is essential for viable tissue cyst development [PMID:26651943]. It localizes to amylopectin stores through a carbohydrate-binding module 20 (CBM20), and its catalytic activity is switched on by Ca2+ acting through its EF-hands, coupling calcium signaling to storage-carbohydrate turnover [PMID:26651943]. Once activated, CDPK2 phosphorylates enzymes of amylopectin catabolism, including glycogen phosphorylase (TgGP) at Ser25; the phosphomimetic TgGP S25E bypasses CDPK2 and rescues amylopectin accumulation in Δcdpk2 parasites, placing CDPK2 directly upstream of TgGP-driven degradation [PMID:28851850]. Loss of CDPK2 causes massive amylopectin hyperaccumulation from both increased synthesis and lost degradation, producing gross morphological defects and complete ablation of cyst formation in mice; this lethality is entirely attributable to amylopectin overproduction, as deleting starch synthase in a Δcdpk2 background abolishes the accumulation and restores cyst formation and virulence [PMID:26651943, PMID:34129780]. Although its mRNA is expressed in tachyzoites, TgCDPK2 protein is not detectably present there and does not account for the KT5926-sensitive kinase controlling tachyzoite motility [PMID:11154702].","teleology":[{"year":2001,"claim":"Established that TgCDPK2, despite tachyzoite mRNA expression, is not the kinase governing tachyzoite motility, distinguishing it from TgCDPK1 and redirecting attention away from a motility role.","evidence":"RT-PCR for mRNA plus immunodetection/protein fractionation in Toxoplasma tachyzoites","pmids":["11154702"],"confidence":"Medium","gaps":["Did not identify the stage or condition where TgCDPK2 protein is expressed","Left the actual cellular function of CDPK2 unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2015,"claim":"Defined CDPK2 as a Ca2+-regulated kinase targeted to amylopectin via a CBM20 domain and required to restrain amylopectin levels, revealing its true role in storage-carbohydrate metabolism.","evidence":"Genetic knockout, CBM20/EF-hand domain dissection, phosphoproteomics, and carbohydrate analysis in Toxoplasma","pmids":["26651943"],"confidence":"High","gaps":["Direct catabolic substrates were not individually validated at this stage","How EF-hand Ca2+ binding mechanistically activates the kinase not resolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2015,"claim":"Demonstrated that CDPK2 is essential specifically for bradyzoite viability, since its loss drives amylopectin granule accumulation that abolishes cyst formation in vivo.","evidence":"Genetic knockout with mouse infection model and electron microscopy/morphological analysis","pmids":["26651943"],"confidence":"High","gaps":["Did not establish which specific catabolic enzyme(s) mediate the phenotype"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2017,"claim":"Placed CDPK2 mechanistically upstream of glycogen phosphorylase by showing that Ser25 phosphorylation of TgGP activates degradation, with the phosphomimetic S25E rescuing amylopectin accumulation in Δcdpk2.","evidence":"Genetic epistasis with S25A/S25E/S25stop TgGP mutants, amylopectin assays, and mouse brain cyst counts in the Pru strain","pmids":["28851850"],"confidence":"High","gaps":["Whether TgGP is the sole relevant substrate not established","Direct in vitro demonstration of CDPK2 phosphorylating TgGP Ser25 not detailed"],"attribution":[{"species":"Toxoplasma gondii","strain":"Pru"}]},{"year":2021,"claim":"Proved that the lethality of CDPK2 loss stems entirely from amylopectin overproduction, since ablating starch synthase in Δcdpk2 removes the accumulation and restores cyst formation and virulence.","evidence":"Double genetic knockout (ΔSS/Δcdpk2) with mouse infection, cyst formation, and virulence assays","pmids":["34129780"],"confidence":"High","gaps":["Does not resolve upstream signals that trigger Ca2+-dependent CDPK2 activation in bradyzoites","Full set of catabolic enzymes controlled by CDPK2 remains incompletely defined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"The upstream Ca2+ signal that activates CDPK2 during bradyzoite differentiation and the complete complement of its amylopectin-catabolic substrates remain to be defined.","evidence":"","pmids":[],"confidence":"High","gaps":["Trigger for Ca2+-dependent activation in cysts unknown","Substrates beyond TgGP not fully enumerated"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["TGGP (GLYCOGEN PHOSPHORYLASE; PHOSPHORYLATED AT SER25 BY CDPK2)","STARCH SYNTHASE (SS; GENETICALLY EPISTATIC, ACTS UPSTREAM OF CDPK2 IN AMYLOPECTIN SYNTHESIS)"],"other_free_text":["CDPK2 protein is not detectably expressed in tachyzoites despite mRNA presence, and is not the KT5926-sensitive motility kinase [#0].","CDPK2 is essential for bradyzoite viability and tissue cyst formation; its loss causes lethal amylopectin hyperaccumulation [#2].","The lethal phenotype of CDPK2 deficiency is entirely dependent on amylopectin overproduction, since ΔSS/Δcdpk2 double mutants restore cyst formation and virulence [#4]."]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"11154702","id":"PMC_11154702","title":"Toxoplasma gondii attachment to host cells is regulated by a calmodulin-like domain protein kinase.","date":"2001","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/11154702","citation_count":126,"is_preprint":false},{"pmid":"26651943","id":"PMC_26651943","title":"Regulation of Starch Stores by a Ca(2+)-Dependent Protein Kinase Is Essential for Viable Cyst Development in Toxoplasma gondii.","date":"2015","source":"Cell host & microbe","url":"https://pubmed.ncbi.nlm.nih.gov/26651943","citation_count":69,"is_preprint":false},{"pmid":"28851850","id":"PMC_28851850","title":"Toxoplasma gondii Requires Glycogen Phosphorylase for Balancing Amylopectin Storage and for Efficient Production of Brain Cysts.","date":"2017","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/28851850","citation_count":50,"is_preprint":false},{"pmid":"29669003","id":"PMC_29669003","title":"Live Attenuated Pru:Δcdpk2 Strain of Toxoplasma gondii Protects Against Acute, Chronic, and Congenital Toxoplasmosis.","date":"2018","source":"The Journal of infectious diseases","url":"https://pubmed.ncbi.nlm.nih.gov/29669003","citation_count":43,"is_preprint":false},{"pmid":"29119944","id":"PMC_29119944","title":"Immune responses and protection after DNA vaccination against Toxoplasma gondii calcium-dependent protein kinase 2 (TgCDPK2).","date":"2017","source":"Parasite (Paris, France)","url":"https://pubmed.ncbi.nlm.nih.gov/29119944","citation_count":22,"is_preprint":false},{"pmid":"34129780","id":"PMC_34129780","title":"Role of amylopectin synthesis in Toxoplasma gondii and its implication in vaccine development against toxoplasmosis.","date":"2021","source":"Open biology","url":"https://pubmed.ncbi.nlm.nih.gov/34129780","citation_count":17,"is_preprint":false},{"pmid":"38752002","id":"PMC_38752002","title":"Immunoinformatics studies and design of a novel multi-epitope peptide vaccine against Toxoplasma gondii based on calcium-dependent protein kinases antigens through an in-silico analysis.","date":"2024","source":"Clinical and experimental vaccine research","url":"https://pubmed.ncbi.nlm.nih.gov/38752002","citation_count":5,"is_preprint":false},{"pmid":"25966270","id":"PMC_25966270","title":"Low-level sequence variation in Toxoplasma gondii calcium-dependent protein kinases among different genotypes.","date":"2015","source":"Genetics and molecular research : GMR","url":"https://pubmed.ncbi.nlm.nih.gov/25966270","citation_count":1,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6623,"output_tokens":1513,"usd":0.021282,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6600,"output_tokens":2834,"usd":0.051925,"stage2_stop_reason":"end_turn"},"total_usd":0.073207,"stage1_batch_id":"msgbatch_01WokvBYTB6JLnYrpD4rXnyV","stage2_batch_id":"msgbatch_01M7hsQDvz6AqVC9DLVjQzzc","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2001,\n      \"finding\": \"TgCDPK2 mRNA is expressed in tachyzoites but no TgCDPK2 protein was detected, indicating TgCDPK2 is not the KT5926-sensitive kinase responsible for regulating Toxoplasma motility and host cell attachment in tachyzoites (that role belongs to TgCDPK1).\",\n      \"method\": \"Immunodetection / protein fractionation; RT-PCR for mRNA detection\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — direct protein detection experiment in a single study; negative result for protein expression is mechanistically informative\",\n      \"pmids\": [\"11154702\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"CDPK2 is a Ca2+-dependent protein kinase that localizes to amylopectin stores via a carbohydrate-binding module 20 (CBM20), and its kinase activity is regulated by EF-hands in response to Ca2+; loss of CDPK2 causes hyperaccumulation of amylopectin due to increased synthesis and loss of degradation, identifying CDPK2 as a critical regulator of amylopectin metabolism.\",\n      \"method\": \"Genetic knockout (CDPK2-deficient parasites), domain function analysis (CBM20 targeting, EF-hand regulation), phosphoproteomics to identify substrates whose phosphorylation is CDPK2-dependent, carbohydrate analysis\",\n      \"journal\": \"Cell host & microbe\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — clean genetic KO with defined metabolic phenotype, domain dissection, and phosphoproteomic substrate identification, all in a single rigorous study replicated in mouse model\",\n      \"pmids\": [\"26651943\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"CDPK2 deficiency in bradyzoite stages causes massive amylopectin granule accumulation leading to gross morphological defects and complete ablation of cyst formation in a mouse model, demonstrating CDPK2 is essential for viable cyst development.\",\n      \"method\": \"Genetic knockout, mouse infection model, electron microscopy/morphological analysis\",\n      \"journal\": \"Cell host & microbe\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — clean genetic KO with defined in vivo phenotype (complete loss of cyst formation) using multiple readouts\",\n      \"pmids\": [\"26651943\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"CDPK2 regulates glycogen phosphorylase (TgGP) activity through phosphorylation of Ser25; the phosphorylation-mimetic TgGP S25E mutant (which bypasses CDPK2-mediated activation) rescues amylopectin accumulation in Δcdpk2 parasites, placing CDPK2 upstream of TgGP in the amylopectin degradation pathway.\",\n      \"method\": \"Genetic epistasis: CDPK2 knockout combined with phosphorylation-null (S25A), phosphorylation-mimetic (S25E), and stop-codon (S25stop) TgGP mutants; amylopectin accumulation assay; mouse brain cyst counts\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — genetic epistasis with reciprocal phosphomutants and rescue experiments clearly place CDPK2 upstream of TgGP in amylopectin catabolism\",\n      \"pmids\": [\"28851850\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"Pru\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Deleting the starch synthase (SS) gene in a Δcdpk2 background completely abolishes amylopectin accumulation and restores cyst formation and virulence in mice, demonstrating that the lethal phenotype of CDPK2 deficiency is entirely dependent on amylopectin overproduction and that CDPK2 acts downstream of SS-driven amylopectin synthesis.\",\n      \"method\": \"Double genetic knockout (ΔSS/Δcdpk2), mouse infection model, cyst formation assay, virulence assessment\",\n      \"journal\": \"Open biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — clean double KO with in vivo rescue of cyst formation and virulence, mechanistically linking CDPK2 phenotype to amylopectin synthesis\",\n      \"pmids\": [\"34129780\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"TgCDPK2 is a Ca2+-dependent protein kinase that localizes to amylopectin granules via its CBM20 domain and, upon Ca2+-mediated activation through its EF-hands, phosphorylates enzymes of amylopectin catabolism (including glycogen phosphorylase TgGP at Ser25) to promote amylopectin degradation; loss of CDPK2 causes amylopectin hyperaccumulation that is lethal to bradyzoites and abolishes tissue cyst formation.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"TgCDPK2 is a Ca2+-dependent protein kinase that serves as a critical regulator of amylopectin metabolism in Toxoplasma gondii and is essential for viable tissue cyst development [#1, #2]. It localizes to amylopectin stores through a carbohydrate-binding module 20 (CBM20), and its catalytic activity is switched on by Ca2+ acting through its EF-hands, coupling calcium signaling to storage-carbohydrate turnover [#1]. Once activated, CDPK2 phosphorylates enzymes of amylopectin catabolism, including glycogen phosphorylase (TgGP) at Ser25; the phosphomimetic TgGP S25E bypasses CDPK2 and rescues amylopectin accumulation in Δcdpk2 parasites, placing CDPK2 directly upstream of TgGP-driven degradation [#3]. Loss of CDPK2 causes massive amylopectin hyperaccumulation from both increased synthesis and lost degradation, producing gross morphological defects and complete ablation of cyst formation in mice; this lethality is entirely attributable to amylopectin overproduction, as deleting starch synthase in a Δcdpk2 background abolishes the accumulation and restores cyst formation and virulence [#2, #4]. Although its mRNA is expressed in tachyzoites, TgCDPK2 protein is not detectably present there and does not account for the KT5926-sensitive kinase controlling tachyzoite motility [#0].\",\n  \"teleology\": [\n    {\n      \"year\": 2001,\n      \"claim\": \"Established that TgCDPK2, despite tachyzoite mRNA expression, is not the kinase governing tachyzoite motility, distinguishing it from TgCDPK1 and redirecting attention away from a motility role.\",\n      \"evidence\": \"RT-PCR for mRNA plus immunodetection/protein fractionation in Toxoplasma tachyzoites\",\n      \"pmids\": [\"11154702\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Did not identify the stage or condition where TgCDPK2 protein is expressed\", \"Left the actual cellular function of CDPK2 unknown\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Defined CDPK2 as a Ca2+-regulated kinase targeted to amylopectin via a CBM20 domain and required to restrain amylopectin levels, revealing its true role in storage-carbohydrate metabolism.\",\n      \"evidence\": \"Genetic knockout, CBM20/EF-hand domain dissection, phosphoproteomics, and carbohydrate analysis in Toxoplasma\",\n      \"pmids\": [\"26651943\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Direct catabolic substrates were not individually validated at this stage\", \"How EF-hand Ca2+ binding mechanistically activates the kinase not resolved\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Demonstrated that CDPK2 is essential specifically for bradyzoite viability, since its loss drives amylopectin granule accumulation that abolishes cyst formation in vivo.\",\n      \"evidence\": \"Genetic knockout with mouse infection model and electron microscopy/morphological analysis\",\n      \"pmids\": [\"26651943\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Did not establish which specific catabolic enzyme(s) mediate the phenotype\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Placed CDPK2 mechanistically upstream of glycogen phosphorylase by showing that Ser25 phosphorylation of TgGP activates degradation, with the phosphomimetic S25E rescuing amylopectin accumulation in Δcdpk2.\",\n      \"evidence\": \"Genetic epistasis with S25A/S25E/S25stop TgGP mutants, amylopectin assays, and mouse brain cyst counts in the Pru strain\",\n      \"pmids\": [\"28851850\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether TgGP is the sole relevant substrate not established\", \"Direct in vitro demonstration of CDPK2 phosphorylating TgGP Ser25 not detailed\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"Pru\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Proved that the lethality of CDPK2 loss stems entirely from amylopectin overproduction, since ablating starch synthase in Δcdpk2 removes the accumulation and restores cyst formation and virulence.\",\n      \"evidence\": \"Double genetic knockout (ΔSS/Δcdpk2) with mouse infection, cyst formation, and virulence assays\",\n      \"pmids\": [\"34129780\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not resolve upstream signals that trigger Ca2+-dependent CDPK2 activation in bradyzoites\", \"Full set of catabolic enzymes controlled by CDPK2 remains incompletely defined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The upstream Ca2+ signal that activates CDPK2 during bradyzoite differentiation and the complete complement of its amylopectin-catabolic substrates remain to be defined.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Trigger for Ca2+-dependent activation in cysts unknown\", \"Substrates beyond TgGP not fully enumerated\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0004683\", \"supporting_discovery_ids\": [1, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0005509\", \"supporting_discovery_ids\": [1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:2001070\", \"supporting_discovery_ids\": [1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0009011\", \"supporting_discovery_ids\": [1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0005983\", \"supporting_discovery_ids\": [1, 3, 4], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0006112\", \"supporting_discovery_ids\": [1, 4], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\n      \"TgGP (glycogen phosphorylase; phosphorylated at Ser25 by CDPK2)\",\n      \"Starch synthase (SS; genetically epistatic, acts upstream of CDPK2 in amylopectin synthesis)\"\n    ],\n    \"other_free_text\": [\n      \"CDPK2 protein is not detectably expressed in tachyzoites despite mRNA presence, and is not the KT5926-sensitive motility kinase [#0].\",\n      \"CDPK2 is essential for bradyzoite viability and tissue cyst formation; its loss causes lethal amylopectin hyperaccumulation [#2].\",\n      \"The lethal phenotype of CDPK2 deficiency is entirely dependent on amylopectin overproduction, since ΔSS/Δcdpk2 double mutants restore cyst formation and virulence [#4].\"\n    ]\n  },\n  \"strain_conflicts\": []\n}\n```","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_225490","name":"CDPK2","product":"calcium-dependent protein kinase CDPK2","uniprot_acc":"S8EXE8","chromosome":"TGME49_chrX","start_pos":2208246},{"strain":"GT1","gene_id":"TGGT1_225490","name":null,"product":"calcium-dependent protein kinase CDPK2","uniprot_acc":null,"chromosome":"TGGT1_chrX","start_pos":2118577},{"strain":"RH88","gene_id":"TGRH88_045220","name":null,"product":"calcium-dependent protein kinase CDPK2","uniprot_acc":null,"chromosome":"CM023091","start_pos":5357434},{"strain":"VEG","gene_id":"TGVEG_225490","name":null,"product":"calcium-dependent protein kinase CDPK2","uniprot_acc":"B9Q7T5","chromosome":"TGVEG_chrX","start_pos":2109516}]}