{"gene":"TG_234570","gene_symbol":"SCP2","run_date":"2026-09-08T12:58:24","timeline":{"discoveries":[{"year":2008,"finding":"Toxoplasma expresses a unique d-bifunctional protein (TgHAD-2SCP-2) consisting of one N-terminal d-3-hydroxyacyl-CoA dehydrogenase domain fused to two tandem SCP-2 domains; this protein undergoes multiple cleavage steps to release free SCP-2, and the most C-terminal SCP-2 carries a PTS1 signal that directs it to vesicles before processing — abrogation of PTS1 results in SCP-2 accumulation in the cytoplasm.","method":"Molecular characterization, transfection with PTS1-abrogated constructs, subcellular localization imaging","journal":"Molecular biology of the cell","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization experiment with functional consequence (PTS1 mutation shifts compartment), single lab, multiple methods including mutagenesis and imaging","pmids":["19005217"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2008,"finding":"Parasite SCP-2 binds cholesterol in vitro, but with ~10-fold lower affinity than phosphatidylcholine, demonstrating lipid-binding selectivity.","method":"In vitro lipid-binding assay","journal":"Molecular biology of the cell","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — in vitro binding assay establishing substrate preference, single lab, single method","pmids":["19005217"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2008,"finding":"Overexpression of TgHAD-2SCP-2 in Toxoplasma promotes inter-organelle circulation of various lipids, enhances uptake of cholesterol and oleate (incorporated into neutral lipids at the basal end of the parasite), and results in faster intracellular replication.","method":"Transfection/overexpression, fluorescent lipid trafficking assays, replication assays","journal":"Molecular biology of the cell","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — gain-of-function with defined lipid-trafficking and growth phenotype, single lab, multiple orthogonal readouts","pmids":["19005217"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2018,"finding":"TgSCP2 functions as a cytosolic acyl-CoA transporter; its acyl-CoA binding activity was confirmed by fluorometric binding assay and yeast complementation. Disruption of TgSCP2 alone caused no obvious phenotype, but double disruption with TgACBP1 resulted in defects in intracellular growth, reduced virulence in mice, decreased fatty acid elongation (C18:1, C22:1, C24:1), and serious defects in glyceride and phospholipid production, demonstrating synergistic roles with TgACBP1 in lipid metabolism.","method":"Fluorometric binding assay, yeast complementation, gene disruption (single and double KO), GC-MS lipidomics, 13C labelling + GC-MS, HPLC-HRMS lipidomics, mouse virulence assay","journal":"Cellular microbiology","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (biochemical binding, yeast complementation, genetic KO, isotope labelling, lipidomics) in a single rigorous study establishing acyl-CoA transport activity and pathway position","pmids":["30362657"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2018,"finding":"The PTS1 sequence of Toxoplasma SCP2 interacts in vitro with the PTS1-binding domain of Toxoplasma Pex5, indicating SCP2 is a cargo of the peroxisomal import receptor Pex5.","method":"In vitro protein–protein interaction assay (PTS1-binding domain of Pex5 vs. SCP2 PTS1 ligand)","journal":"Genes","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single in vitro interaction assay, single lab, no functional follow-up for SCP2 specifically","pmids":["30158461"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"Toxoplasma SCP2 is a cytosolic acyl-CoA and lipid-transfer protein derived from cleavage of an ancestral d-bifunctional protein (TgHAD-2SCP-2); it binds acyl-CoAs and cholesterol, traffics lipids between organelles via a PTS1-directed pathway (interacting with the peroxisomal import receptor Pex5), and acts synergistically with TgACBP1 to sustain fatty acid elongation and phospholipid synthesis required for intracellular parasite growth and virulence."},"narrative":{"mechanistic_narrative":"Toxoplasma gondii SCP2 is a lipid-transfer and acyl-CoA-binding protein that supports the parasite's acquisition and inter-organelle trafficking of lipids required for intracellular replication [PMID:19005217, PMID:30362657]. It originates as the two tandem C-terminal SCP-2 domains of an unusual d-bifunctional protein (TgHAD-2SCP-2), whose proteolytic processing releases free SCP-2; the most C-terminal SCP-2 domain carries a PTS1 signal that directs the protein to vesicles, and mutation of this signal causes cytoplasmic accumulation [PMID:19005217]. Biochemically, the protein binds cholesterol in vitro—though with lower affinity than phosphatidylcholine—and functions as a cytosolic acyl-CoA transporter confirmed by fluorometric binding and yeast complementation [PMID:19005217, PMID:30362657]. Overexpression of TgHAD-2SCP-2 enhances circulation of lipids between organelles, boosts cholesterol and oleate uptake, and accelerates replication [PMID:19005217]. Genetically, SCP2 is dispensable alone, but its combined disruption with TgACBP1 impairs intracellular growth, reduces virulence in mice, and causes defects in fatty acid elongation, glyceride, and phospholipid synthesis, establishing a synergistic role with TgACBP1 in parasite lipid metabolism [PMID:30362657].","teleology":[{"year":2008,"claim":"Established the origin, processing, and targeting logic of parasite SCP-2, showing it is liberated from a fused d-bifunctional protein and routed by a PTS1 signal — defining where the transfer protein acts in the cell.","evidence":"Molecular characterization with PTS1-abrogated transfection constructs and subcellular imaging in T. gondii","pmids":["19005217"],"confidence":"Medium","gaps":["Exact protease(s) and processing sequence releasing free SCP-2 not defined","Vesicular identity of the PTS1-targeted compartment not fully resolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2008,"claim":"Determined the lipid-binding selectivity of the protein, showing it binds cholesterol but favors phosphatidylcholine ~10-fold, indicating it is a selective lipid-transfer protein.","evidence":"In vitro lipid-binding assay","pmids":["19005217"],"confidence":"Medium","gaps":["Binding measured in vitro without structural basis for selectivity","Full spectrum of physiological lipid ligands not defined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2008,"claim":"Linked SCP-2 function to a cellular phenotype by showing overexpression promotes inter-organelle lipid circulation, enhances cholesterol/oleate uptake, and accelerates replication — connecting lipid transfer to parasite growth.","evidence":"Overexpression with fluorescent lipid trafficking and replication assays in T. gondii","pmids":["19005217"],"confidence":"Medium","gaps":["Gain-of-function readout; loss-of-function contribution of native SCP-2 not addressed here","Mechanistic step at which SCP-2 acts in trafficking not resolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2018,"claim":"Defined SCP2 as a cytosolic acyl-CoA transporter and placed it in a lipid-metabolic pathway acting synergistically with TgACBP1, explaining why the single knockout is silent while the double knockout cripples fatty acid elongation, phospholipid synthesis, growth, and virulence.","evidence":"Fluorometric binding, yeast complementation, single and double gene disruption, GC-MS/13C lipidomics, HPLC-HRMS, and mouse virulence assay","pmids":["30362657"],"confidence":"High","gaps":["Molecular basis of the functional redundancy with TgACBP1 not resolved","Directionality and organellar endpoints of acyl-CoA transport in vivo not established"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2018,"claim":"Provided the molecular basis for SCP2 targeting by showing its PTS1 sequence binds the PTS1-binding domain of Pex5, identifying SCP2 as cargo of the peroxisomal import receptor.","evidence":"In vitro protein–protein interaction assay between Pex5 PTS1-binding domain and SCP2 PTS1 ligand","pmids":["30158461"],"confidence":"Low","gaps":["Single in vitro interaction assay without functional follow-up for SCP2","Whether SCP2 is genuinely imported into a peroxisome-like compartment in vivo not demonstrated"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"How SCP2-mediated lipid and acyl-CoA transfer is spatially organized between organelles and coordinated with TgACBP1 at the biochemical level remains unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No structural model of SCP2 lipid/acyl-CoA binding","In vivo trafficking route and organellar acceptor sites undefined","Mechanism of functional redundancy with TgACBP1 unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["TGACBP1 (SYNERGISTIC PARTNER IN LIPID METABOLISM) [#3]","TGPEX5 (PEROXISOMAL PTS1 IMPORT RECEPTOR; BINDS SCP2 PTS1) [#4]"],"other_free_text":["SCP2 is derived from proteolytic cleavage of the d-bifunctional protein TgHAD-2SCP-2, which comprises an N-terminal d-3-hydroxyacyl-CoA dehydrogenase domain fused to two tandem SCP-2 domains [#0].","The most C-terminal SCP-2 domain carries a PTS1 signal directing it to vesicles; PTS1 abrogation causes cytoplasmic accumulation [#0].","Single knockout of TgSCP2 has no obvious phenotype; the double knockout with TgACBP1 impairs intracellular growth, virulence, fatty acid elongation (C18:1, C22:1, C24:1), and glyceride/phospholipid production [#3]."]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"19005217","id":"PMC_19005217","title":"Role of an ancestral d-bifunctional protein containing two sterol-carrier protein-2 domains in lipid uptake and trafficking in Toxoplasma.","date":"2008","source":"Molecular biology of the cell","url":"https://pubmed.ncbi.nlm.nih.gov/19005217","citation_count":23,"is_preprint":false},{"pmid":"30362657","id":"PMC_30362657","title":"Synergistic roles of acyl-CoA binding protein (ACBP1) and sterol carrier protein 2 (SCP2) in Toxoplasma lipid metabolism.","date":"2018","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/30362657","citation_count":13,"is_preprint":false},{"pmid":"30158461","id":"PMC_30158461","title":"Functional Analyses of a Putative, Membrane-Bound, Peroxisomal Protein Import Mechanism from the Apicomplexan Protozoan Toxoplasma gondii.","date":"2018","source":"Genes","url":"https://pubmed.ncbi.nlm.nih.gov/30158461","citation_count":2,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4124,"output_tokens":1463,"usd":0.017159,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6539,"output_tokens":3029,"usd":0.05421,"stage2_stop_reason":"end_turn"},"total_usd":0.071369,"stage1_batch_id":"msgbatch_01TEPNZ4MCzJ7xtsNwosiDRk","stage2_batch_id":"msgbatch_01FQShM7n1sfCr4pWTDShmki","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2008,\n      \"finding\": \"Toxoplasma expresses a unique d-bifunctional protein (TgHAD-2SCP-2) consisting of one N-terminal d-3-hydroxyacyl-CoA dehydrogenase domain fused to two tandem SCP-2 domains; this protein undergoes multiple cleavage steps to release free SCP-2, and the most C-terminal SCP-2 carries a PTS1 signal that directs it to vesicles before processing — abrogation of PTS1 results in SCP-2 accumulation in the cytoplasm.\",\n      \"method\": \"Molecular characterization, transfection with PTS1-abrogated constructs, subcellular localization imaging\",\n      \"journal\": \"Molecular biology of the cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization experiment with functional consequence (PTS1 mutation shifts compartment), single lab, multiple methods including mutagenesis and imaging\",\n      \"pmids\": [\"19005217\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"finding\": \"Parasite SCP-2 binds cholesterol in vitro, but with ~10-fold lower affinity than phosphatidylcholine, demonstrating lipid-binding selectivity.\",\n      \"method\": \"In vitro lipid-binding assay\",\n      \"journal\": \"Molecular biology of the cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — in vitro binding assay establishing substrate preference, single lab, single method\",\n      \"pmids\": [\"19005217\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"finding\": \"Overexpression of TgHAD-2SCP-2 in Toxoplasma promotes inter-organelle circulation of various lipids, enhances uptake of cholesterol and oleate (incorporated into neutral lipids at the basal end of the parasite), and results in faster intracellular replication.\",\n      \"method\": \"Transfection/overexpression, fluorescent lipid trafficking assays, replication assays\",\n      \"journal\": \"Molecular biology of the cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — gain-of-function with defined lipid-trafficking and growth phenotype, single lab, multiple orthogonal readouts\",\n      \"pmids\": [\"19005217\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"TgSCP2 functions as a cytosolic acyl-CoA transporter; its acyl-CoA binding activity was confirmed by fluorometric binding assay and yeast complementation. Disruption of TgSCP2 alone caused no obvious phenotype, but double disruption with TgACBP1 resulted in defects in intracellular growth, reduced virulence in mice, decreased fatty acid elongation (C18:1, C22:1, C24:1), and serious defects in glyceride and phospholipid production, demonstrating synergistic roles with TgACBP1 in lipid metabolism.\",\n      \"method\": \"Fluorometric binding assay, yeast complementation, gene disruption (single and double KO), GC-MS lipidomics, 13C labelling + GC-MS, HPLC-HRMS lipidomics, mouse virulence assay\",\n      \"journal\": \"Cellular microbiology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (biochemical binding, yeast complementation, genetic KO, isotope labelling, lipidomics) in a single rigorous study establishing acyl-CoA transport activity and pathway position\",\n      \"pmids\": [\"30362657\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"The PTS1 sequence of Toxoplasma SCP2 interacts in vitro with the PTS1-binding domain of Toxoplasma Pex5, indicating SCP2 is a cargo of the peroxisomal import receptor Pex5.\",\n      \"method\": \"In vitro protein–protein interaction assay (PTS1-binding domain of Pex5 vs. SCP2 PTS1 ligand)\",\n      \"journal\": \"Genes\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single in vitro interaction assay, single lab, no functional follow-up for SCP2 specifically\",\n      \"pmids\": [\"30158461\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"Toxoplasma SCP2 is a cytosolic acyl-CoA and lipid-transfer protein derived from cleavage of an ancestral d-bifunctional protein (TgHAD-2SCP-2); it binds acyl-CoAs and cholesterol, traffics lipids between organelles via a PTS1-directed pathway (interacting with the peroxisomal import receptor Pex5), and acts synergistically with TgACBP1 to sustain fatty acid elongation and phospholipid synthesis required for intracellular parasite growth and virulence.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"Toxoplasma gondii SCP2 is a lipid-transfer and acyl-CoA-binding protein that supports the parasite's acquisition and inter-organelle trafficking of lipids required for intracellular replication [#0, #2, #3]. It originates as the two tandem C-terminal SCP-2 domains of an unusual d-bifunctional protein (TgHAD-2SCP-2), whose proteolytic processing releases free SCP-2; the most C-terminal SCP-2 domain carries a PTS1 signal that directs the protein to vesicles, and mutation of this signal causes cytoplasmic accumulation [#0]. Biochemically, the protein binds cholesterol in vitro—though with lower affinity than phosphatidylcholine—and functions as a cytosolic acyl-CoA transporter confirmed by fluorometric binding and yeast complementation [#1, #3]. Overexpression of TgHAD-2SCP-2 enhances circulation of lipids between organelles, boosts cholesterol and oleate uptake, and accelerates replication [#2]. Genetically, SCP2 is dispensable alone, but its combined disruption with TgACBP1 impairs intracellular growth, reduces virulence in mice, and causes defects in fatty acid elongation, glyceride, and phospholipid synthesis, establishing a synergistic role with TgACBP1 in parasite lipid metabolism [#3].\",\n  \"teleology\": [\n    {\n      \"year\": 2008,\n      \"claim\": \"Established the origin, processing, and targeting logic of parasite SCP-2, showing it is liberated from a fused d-bifunctional protein and routed by a PTS1 signal — defining where the transfer protein acts in the cell.\",\n      \"evidence\": \"Molecular characterization with PTS1-abrogated transfection constructs and subcellular imaging in T. gondii\",\n      \"pmids\": [\"19005217\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Exact protease(s) and processing sequence releasing free SCP-2 not defined\", \"Vesicular identity of the PTS1-targeted compartment not fully resolved\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"claim\": \"Determined the lipid-binding selectivity of the protein, showing it binds cholesterol but favors phosphatidylcholine ~10-fold, indicating it is a selective lipid-transfer protein.\",\n      \"evidence\": \"In vitro lipid-binding assay\",\n      \"pmids\": [\"19005217\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Binding measured in vitro without structural basis for selectivity\", \"Full spectrum of physiological lipid ligands not defined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"claim\": \"Linked SCP-2 function to a cellular phenotype by showing overexpression promotes inter-organelle lipid circulation, enhances cholesterol/oleate uptake, and accelerates replication — connecting lipid transfer to parasite growth.\",\n      \"evidence\": \"Overexpression with fluorescent lipid trafficking and replication assays in T. gondii\",\n      \"pmids\": [\"19005217\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Gain-of-function readout; loss-of-function contribution of native SCP-2 not addressed here\", \"Mechanistic step at which SCP-2 acts in trafficking not resolved\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Defined SCP2 as a cytosolic acyl-CoA transporter and placed it in a lipid-metabolic pathway acting synergistically with TgACBP1, explaining why the single knockout is silent while the double knockout cripples fatty acid elongation, phospholipid synthesis, growth, and virulence.\",\n      \"evidence\": \"Fluorometric binding, yeast complementation, single and double gene disruption, GC-MS/13C lipidomics, HPLC-HRMS, and mouse virulence assay\",\n      \"pmids\": [\"30362657\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular basis of the functional redundancy with TgACBP1 not resolved\", \"Directionality and organellar endpoints of acyl-CoA transport in vivo not established\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Provided the molecular basis for SCP2 targeting by showing its PTS1 sequence binds the PTS1-binding domain of Pex5, identifying SCP2 as cargo of the peroxisomal import receptor.\",\n      \"evidence\": \"In vitro protein–protein interaction assay between Pex5 PTS1-binding domain and SCP2 PTS1 ligand\",\n      \"pmids\": [\"30158461\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Single in vitro interaction assay without functional follow-up for SCP2\", \"Whether SCP2 is genuinely imported into a peroxisome-like compartment in vivo not demonstrated\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How SCP2-mediated lipid and acyl-CoA transfer is spatially organized between organelles and coordinated with TgACBP1 at the biochemical level remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No structural model of SCP2 lipid/acyl-CoA binding\", \"In vivo trafficking route and organellar acceptor sites undefined\", \"Mechanism of functional redundancy with TgACBP1 unknown\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0000062\", \"supporting_discovery_ids\": [3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0015485\", \"supporting_discovery_ids\": [1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0120019\", \"supporting_discovery_ids\": [1, 2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [0, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0031410\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006629\", \"supporting_discovery_ids\": [2, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0030497\", \"supporting_discovery_ids\": [3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0008654\", \"supporting_discovery_ids\": [3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\n      \"TgACBP1 (synergistic partner in lipid metabolism) [#3]\",\n      \"TgPex5 (peroxisomal PTS1 import receptor; binds SCP2 PTS1) [#4]\"\n    ],\n    \"other_free_text\": [\n      \"SCP2 is derived from proteolytic cleavage of the d-bifunctional protein TgHAD-2SCP-2, which comprises an N-terminal d-3-hydroxyacyl-CoA dehydrogenase domain fused to two tandem SCP-2 domains [#0].\",\n      \"The most C-terminal SCP-2 domain carries a PTS1 signal directing it to vesicles; PTS1 abrogation causes cytoplasmic accumulation [#0].\",\n      \"Single knockout of TgSCP2 has no obvious phenotype; the double knockout with TgACBP1 impairs intracellular growth, virulence, fatty acid elongation (C18:1, C22:1, C24:1), and glyceride/phospholipid production [#3].\"\n    ]\n  },\n  \"strain_conflicts\": []\n}\n```","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_234570","name":"SCP2","product":"sterol carrier protein-2 HAD-2SCP-2","uniprot_acc":"A0A125YZ46","chromosome":"TGME49_chrX","start_pos":4467643},{"strain":"GT1","gene_id":"TGGT1_234570","name":null,"product":"sterol carrier protein-2 HAD-2SCP-2","uniprot_acc":null,"chromosome":"TGGT1_chrX","start_pos":4363733},{"strain":"RH88","gene_id":"TGRH88_042370","name":null,"product":"sterol carrier protein-2 HAD-2SCP-2","uniprot_acc":null,"chromosome":"CM023091","start_pos":3069026},{"strain":"VEG","gene_id":"TGVEG_234570","name":null,"product":"sterol carrier protein-2 HAD-2SCP-2","uniprot_acc":"B6KM24","chromosome":"TGVEG_chrX","start_pos":4379384}]}