{"gene":"TG_293000","gene_symbol":"PDE2","run_date":"2026-09-08T14:08:30","timeline":{"discoveries":[{"year":2022,"finding":"TgPDE2 is a cAMP-specific phosphodiesterase (not dual-specific), with a Km of 14 μM for cAMP, establishing its substrate selectivity biochemically.","method":"Biochemical analysis of TgPDE2 purified from Toxoplasma lysates; enzyme kinetics (Km determination)","journal":"mSphere / Computational and structural biotechnology journal","confidence":"High","confidence_rationale":"Tier 1 / Strong — in vitro enzymatic assay with substrate specificity determination replicated independently in two separate studies (PMID:35107337 and PMID:36382189)","pmids":["35107337","36382189"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"finding":"TgPDE2 is required for host cell invasion, parasite replication, host cell egress, and extracellular motility in tachyzoites, as demonstrated by knockdown causing severe growth defects across these lytic cycle stages.","method":"Conditional knockdown (TgPDE2 depletion) with phenotypic readouts: invasion, replication, egress, and motility assays","journal":"mSphere","confidence":"High","confidence_rationale":"Tier 2 / Strong — clean conditional KO with multiple defined cellular phenotypes replicated across two independent studies (PMID:35107337 and PMID:36382189)","pmids":["35107337","36382189"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"finding":"TgPDE2 displays an endoplasmic reticulum/cytomembranous distribution, as well as subcellular localizations including the inner membrane complex, apical pole, plasma membrane, cytosol, dense granule, and rhoptry, indicating spatial control of cAMP signaling.","method":"Subcellular localization by standard microscopy (mSphere) and immuno-electron microscopy (PMID:36382189)","journal":"mSphere / Computational and structural biotechnology journal","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — localization established by two orthogonal imaging methods across two independent studies, but functional link to specific compartments not directly tested","pmids":["35107337","36382189"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"finding":"TgPDE2 regulates calcium (Ca2+)-induced egress in a CDPK3-independent manner, placing it in the cAMP branch of the positive feedback loop linking calcium and cyclic nucleotide signaling during egress.","method":"Biochemical phosphoproteomics and conditional knockout analysis in WT and CDPK3 KO parasites; Ca2+ ionophore-induced egress assays","journal":"PLoS pathogens","confidence":"High","confidence_rationale":"Tier 2 / Strong — genetic epistasis using conditional KO combined with phosphoproteomics and functional egress assays in a single rigorous study with multiple orthogonal methods","pmids":["36265000"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"finding":"TgPDE2 does not physically interact with TgPDE1 or other TgPDEs, but its interactome includes kinases and phosphatases that may regulate its enzymatic activity.","method":"Interactome/co-immunoprecipitation studies of TgPDE2 purified from Toxoplasma lysates","journal":"mSphere / Computational and structural biotechnology journal","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — interactome data from two independent studies, but regulatory mechanism of kinase/phosphatase interaction not directly validated functionally","pmids":["35107337","36382189"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"finding":"Combined loss of TgPDE1 and TgPDE2 is lethal to the parasite, whereas individual loss causes severe but non-lethal growth defects, indicating functional cooperation between these two PDEs in maintaining cyclic nucleotide homeostasis.","method":"Double conditional knockout (TgPDE1 + TgPDE2) lethality assay; individual knockdowns with growth assays","journal":"Computational and structural biotechnology journal","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic epistasis via double KO in a single study; lethality is a strong phenotypic readout but single lab","pmids":["36382189"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"TgPDE2 is a cAMP-specific phosphodiesterase (Km ~14 μM) localized to the endoplasmic reticulum, inner membrane complex, and other subcellular compartments, where it regulates intracellular cAMP levels to control tachyzoite invasion, replication, egress, and motility, and acts downstream of calcium signaling in a CDPK3-independent manner within a positive feedback loop linking calcium and cyclic nucleotide signaling during egress; its activity is potentially regulated by associated kinases and phosphatases, and it cooperates with TgPDE1 such that their combined loss is lethal."},"narrative":{"mechanistic_narrative":"TgPDE2 is a cAMP-specific phosphodiesterase in Toxoplasma gondii that governs the tachyzoite lytic cycle by controlling intracellular cAMP levels [PMID:35107337, PMID:36382189]. Biochemically it is selective for cAMP (Km ~14 μM) rather than dual-specific [PMID:35107337, PMID:36382189], and its depletion produces severe defects in host cell invasion, replication, egress, and extracellular motility, establishing it as a central regulator of cyclic nucleotide signaling across the lytic cycle [PMID:35107337, PMID:36382189]. During egress it acts in the cAMP branch of a positive feedback loop that links calcium and cyclic nucleotide signaling, functioning in a CDPK3-independent manner downstream of calcium signaling [PMID:36265000]. Spatial control of cAMP is reflected in its broad subcellular distribution, prominently the endoplasmic reticulum/cytomembranous system and inner membrane complex, with additional signal at the apical pole, plasma membrane, cytosol, dense granule, and rhoptry [PMID:35107337, PMID:36382189]. TgPDE2 does not physically associate with TgPDE1 or other TgPDEs, yet its combined loss with TgPDE1 is lethal, indicating functional cooperation between the two enzymes in maintaining cyclic nucleotide homeostasis [PMID:35107337, PMID:36382189]. Its interactome includes kinases and phosphatases that may modulate its activity [PMID:35107337, PMID:36382189].","teleology":[{"year":2022,"claim":"Establishing the substrate specificity of TgPDE2 defined which cyclic nucleotide pool it controls, distinguishing a cAMP-specific from a dual-specific enzyme.","evidence":"Enzyme kinetics (Km determination) on TgPDE2 purified from Toxoplasma lysates","pmids":["35107337","36382189"],"confidence":"High","gaps":["No structural basis for cAMP selectivity resolved","Regulation of catalytic activity in vivo not defined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"claim":"Conditional depletion demonstrated that TgPDE2 is required across the entire tachyzoite lytic cycle, converting a biochemical activity into a defined biological function.","evidence":"Conditional knockdown with invasion, replication, egress, and motility assays","pmids":["35107337","36382189"],"confidence":"High","gaps":["Whether each phenotype reflects the same or distinct cAMP pools not resolved","Downstream effectors of cAMP in each stage not identified"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"claim":"Subcellular localization mapping showed TgPDE2 is distributed across ER, IMC, and multiple compartments, implying spatially compartmentalized cAMP regulation.","evidence":"Standard microscopy and immuno-electron microscopy across two studies","pmids":["35107337","36382189"],"confidence":"Medium","gaps":["Functional link between specific compartments and phenotypes not tested","Mechanism of targeting to these compartments unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"claim":"Genetic epistasis placed TgPDE2 in the cAMP branch of the calcium/cyclic-nucleotide feedback loop controlling egress, acting independently of CDPK3.","evidence":"Conditional KO in WT and CDPK3 KO parasites with phosphoproteomics and Ca2+ ionophore-induced egress assays","pmids":["36265000"],"confidence":"High","gaps":["Direct molecular link between calcium and TgPDE2 activity not defined","Identity of the feedback loop's cAMP effectors not established"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"claim":"Interactome and double-knockout analyses showed TgPDE2 cooperates functionally, but not physically, with TgPDE1 and associates with candidate regulatory kinases/phosphatases.","evidence":"Co-immunoprecipitation interactome and double conditional knockout lethality assay","pmids":["35107337","36382189"],"confidence":"Medium","gaps":["Regulatory role of interacting kinases/phosphatases not functionally validated","Basis of functional redundancy with TgPDE1 despite no physical interaction unresolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"The downstream cAMP effectors and the mechanism by which compartment-specific TgPDE2 activity is regulated during each lytic-cycle stage remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No direct demonstration of which kinase/phosphatase partners regulate activity","No mapping of cAMP effector pathways to specific phenotypes"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["TGPDE1 (FUNCTIONAL COOPERATION, NO PHYSICAL INTERACTION)","ASSOCIATED KINASES AND PHOSPHATASES (INTERACTOME)"],"other_free_text":["cAMP-specific phosphodiesterase, Km ~14 μM for cAMP","Required for tachyzoite invasion, replication, egress, and motility","Acts downstream of calcium signaling in a CDPK3-independent manner during egress","Combined loss with TgPDE1 is lethal; individual loss is severe but non-lethal"]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"36265000","id":"PMC_36265000","title":"A positive feedback loop mediates crosstalk between calcium, cyclic nucleotide and lipid signalling in calcium-induced Toxoplasma gondii egress.","date":"2022","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/36265000","citation_count":19,"is_preprint":false},{"pmid":"35107337","id":"PMC_35107337","title":"Functional Analysis of the Expanded Phosphodiesterase Gene Family in Toxoplasma gondii Tachyzoites.","date":"2022","source":"mSphere","url":"https://pubmed.ncbi.nlm.nih.gov/35107337","citation_count":19,"is_preprint":false},{"pmid":"36382189","id":"PMC_36382189","title":"Plasticity and therapeutic potential of cAMP and cGMP-specific phosphodiesterases in Toxoplasma gondii.","date":"2022","source":"Computational and structural biotechnology journal","url":"https://pubmed.ncbi.nlm.nih.gov/36382189","citation_count":6,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4381,"output_tokens":1607,"usd":0.018624,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6743,"output_tokens":2419,"usd":0.047095,"stage2_stop_reason":"end_turn"},"total_usd":0.065719,"stage1_batch_id":"msgbatch_015xmQKDRqnTh9anE4m7LiD6","stage2_batch_id":"msgbatch_01JLpkFTVhoQBNgqHCKFrVVU","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2022,\n      \"finding\": \"TgPDE2 is a cAMP-specific phosphodiesterase (not dual-specific), with a Km of 14 μM for cAMP, establishing its substrate selectivity biochemically.\",\n      \"method\": \"Biochemical analysis of TgPDE2 purified from Toxoplasma lysates; enzyme kinetics (Km determination)\",\n      \"journal\": \"mSphere / Computational and structural biotechnology journal\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — in vitro enzymatic assay with substrate specificity determination replicated independently in two separate studies (PMID:35107337 and PMID:36382189)\",\n      \"pmids\": [\"35107337\", \"36382189\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"TgPDE2 is required for host cell invasion, parasite replication, host cell egress, and extracellular motility in tachyzoites, as demonstrated by knockdown causing severe growth defects across these lytic cycle stages.\",\n      \"method\": \"Conditional knockdown (TgPDE2 depletion) with phenotypic readouts: invasion, replication, egress, and motility assays\",\n      \"journal\": \"mSphere\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — clean conditional KO with multiple defined cellular phenotypes replicated across two independent studies (PMID:35107337 and PMID:36382189)\",\n      \"pmids\": [\"35107337\", \"36382189\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"TgPDE2 displays an endoplasmic reticulum/cytomembranous distribution, as well as subcellular localizations including the inner membrane complex, apical pole, plasma membrane, cytosol, dense granule, and rhoptry, indicating spatial control of cAMP signaling.\",\n      \"method\": \"Subcellular localization by standard microscopy (mSphere) and immuno-electron microscopy (PMID:36382189)\",\n      \"journal\": \"mSphere / Computational and structural biotechnology journal\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — localization established by two orthogonal imaging methods across two independent studies, but functional link to specific compartments not directly tested\",\n      \"pmids\": [\"35107337\", \"36382189\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"TgPDE2 regulates calcium (Ca2+)-induced egress in a CDPK3-independent manner, placing it in the cAMP branch of the positive feedback loop linking calcium and cyclic nucleotide signaling during egress.\",\n      \"method\": \"Biochemical phosphoproteomics and conditional knockout analysis in WT and CDPK3 KO parasites; Ca2+ ionophore-induced egress assays\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — genetic epistasis using conditional KO combined with phosphoproteomics and functional egress assays in a single rigorous study with multiple orthogonal methods\",\n      \"pmids\": [\"36265000\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"TgPDE2 does not physically interact with TgPDE1 or other TgPDEs, but its interactome includes kinases and phosphatases that may regulate its enzymatic activity.\",\n      \"method\": \"Interactome/co-immunoprecipitation studies of TgPDE2 purified from Toxoplasma lysates\",\n      \"journal\": \"mSphere / Computational and structural biotechnology journal\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — interactome data from two independent studies, but regulatory mechanism of kinase/phosphatase interaction not directly validated functionally\",\n      \"pmids\": [\"35107337\", \"36382189\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"Combined loss of TgPDE1 and TgPDE2 is lethal to the parasite, whereas individual loss causes severe but non-lethal growth defects, indicating functional cooperation between these two PDEs in maintaining cyclic nucleotide homeostasis.\",\n      \"method\": \"Double conditional knockout (TgPDE1 + TgPDE2) lethality assay; individual knockdowns with growth assays\",\n      \"journal\": \"Computational and structural biotechnology journal\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic epistasis via double KO in a single study; lethality is a strong phenotypic readout but single lab\",\n      \"pmids\": [\"36382189\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"TgPDE2 is a cAMP-specific phosphodiesterase (Km ~14 μM) localized to the endoplasmic reticulum, inner membrane complex, and other subcellular compartments, where it regulates intracellular cAMP levels to control tachyzoite invasion, replication, egress, and motility, and acts downstream of calcium signaling in a CDPK3-independent manner within a positive feedback loop linking calcium and cyclic nucleotide signaling during egress; its activity is potentially regulated by associated kinases and phosphatases, and it cooperates with TgPDE1 such that their combined loss is lethal.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"TgPDE2 is a cAMP-specific phosphodiesterase in Toxoplasma gondii that governs the tachyzoite lytic cycle by controlling intracellular cAMP levels [#0, #1]. Biochemically it is selective for cAMP (Km ~14 μM) rather than dual-specific [#0], and its depletion produces severe defects in host cell invasion, replication, egress, and extracellular motility, establishing it as a central regulator of cyclic nucleotide signaling across the lytic cycle [#1]. During egress it acts in the cAMP branch of a positive feedback loop that links calcium and cyclic nucleotide signaling, functioning in a CDPK3-independent manner downstream of calcium signaling [#3]. Spatial control of cAMP is reflected in its broad subcellular distribution, prominently the endoplasmic reticulum/cytomembranous system and inner membrane complex, with additional signal at the apical pole, plasma membrane, cytosol, dense granule, and rhoptry [#2]. TgPDE2 does not physically associate with TgPDE1 or other TgPDEs, yet its combined loss with TgPDE1 is lethal, indicating functional cooperation between the two enzymes in maintaining cyclic nucleotide homeostasis [#4, #5]. Its interactome includes kinases and phosphatases that may modulate its activity [#4].\",\n  \"teleology\": [\n    {\n      \"year\": 2022,\n      \"claim\": \"Establishing the substrate specificity of TgPDE2 defined which cyclic nucleotide pool it controls, distinguishing a cAMP-specific from a dual-specific enzyme.\",\n      \"evidence\": \"Enzyme kinetics (Km determination) on TgPDE2 purified from Toxoplasma lysates\",\n      \"pmids\": [\"35107337\", \"36382189\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No structural basis for cAMP selectivity resolved\", \"Regulation of catalytic activity in vivo not defined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Conditional depletion demonstrated that TgPDE2 is required across the entire tachyzoite lytic cycle, converting a biochemical activity into a defined biological function.\",\n      \"evidence\": \"Conditional knockdown with invasion, replication, egress, and motility assays\",\n      \"pmids\": [\"35107337\", \"36382189\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether each phenotype reflects the same or distinct cAMP pools not resolved\", \"Downstream effectors of cAMP in each stage not identified\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Subcellular localization mapping showed TgPDE2 is distributed across ER, IMC, and multiple compartments, implying spatially compartmentalized cAMP regulation.\",\n      \"evidence\": \"Standard microscopy and immuno-electron microscopy across two studies\",\n      \"pmids\": [\"35107337\", \"36382189\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Functional link between specific compartments and phenotypes not tested\", \"Mechanism of targeting to these compartments unknown\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Genetic epistasis placed TgPDE2 in the cAMP branch of the calcium/cyclic-nucleotide feedback loop controlling egress, acting independently of CDPK3.\",\n      \"evidence\": \"Conditional KO in WT and CDPK3 KO parasites with phosphoproteomics and Ca2+ ionophore-induced egress assays\",\n      \"pmids\": [\"36265000\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Direct molecular link between calcium and TgPDE2 activity not defined\", \"Identity of the feedback loop's cAMP effectors not established\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Interactome and double-knockout analyses showed TgPDE2 cooperates functionally, but not physically, with TgPDE1 and associates with candidate regulatory kinases/phosphatases.\",\n      \"evidence\": \"Co-immunoprecipitation interactome and double conditional knockout lethality assay\",\n      \"pmids\": [\"35107337\", \"36382189\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Regulatory role of interacting kinases/phosphatases not functionally validated\", \"Basis of functional redundancy with TgPDE1 despite no physical interaction unresolved\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The downstream cAMP effectors and the mechanism by which compartment-specific TgPDE2 activity is regulated during each lytic-cycle stage remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No direct demonstration of which kinase/phosphatase partners regulate activity\", \"No mapping of cAMP effector pathways to specific phenotypes\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0004115\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005783\", \"supporting_discovery_ids\": [2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0070258\", \"supporting_discovery_ids\": [2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0019933\", \"supporting_discovery_ids\": [0, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"TgPDE1 (functional cooperation, no physical interaction)\", \"associated kinases and phosphatases (interactome)\"],\n    \"other_free_text\": [\n      \"cAMP-specific phosphodiesterase, Km ~14 μM for cAMP\",\n      \"Required for tachyzoite invasion, replication, egress, and motility\",\n      \"Acts downstream of calcium signaling in a CDPK3-independent manner during egress\",\n      \"Combined loss with TgPDE1 is lethal; individual loss is severe but non-lethal\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_293000","name":"PDE2","product":"3'5'-cyclic nucleotide phosphodiesterase PDE2","uniprot_acc":"A0A125YIU9","chromosome":"TGME49_chrIa","start_pos":72463},{"strain":"GT1","gene_id":"TGGT1_293000","name":null,"product":"3'5'-cyclic nucleotide phosphodiesterase domain-containing protein","uniprot_acc":null,"chromosome":"TGGT1_chrIa","start_pos":58977},{"strain":"RH88","gene_id":"TGRH88_018390","name":null,"product":"3'5'-cyclic nucleotide phosphodiesterase domain-containing protein","uniprot_acc":null,"chromosome":"CM023081","start_pos":79170},{"strain":"VEG","gene_id":"TGVEG_293000","name":null,"product":"3'5'-cyclic nucleotide phosphodiesterase domain-containing protein","uniprot_acc":"A0A125YIV1","chromosome":"TGVEG_chrIa","start_pos":82248}]}