{"gene":"TG_289120","gene_symbol":"ULP1","run_date":"2026-09-08T14:08:30","timeline":{"discoveries":[{"year":2024,"finding":"T. gondii ULP1 localizes to the Golgi apparatus and is structurally similar to the eukaryotic trafficking factor p115/Uso1. Conditional depletion of ULP1 causes defects in microneme secretion, invasion, replication, and egress, demonstrating an essential role in the secretory pathway.","method":"Conditional knockdown, live/fixed imaging for Golgi localization, plaque/invasion/egress assays, microneme secretion assay","journal":"mBio","confidence":"High","confidence_rationale":"Tier 2 / Strong — conditional knockdown with multiple defined phenotypic readouts (microneme secretion, invasion, replication, egress) and structural characterization, replicated across preprint and peer-reviewed publication by the same lab with orthogonal methods","pmids":["39345210","38352341"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"finding":"ULP1 physically interacts with the T. gondii conserved oligomeric Golgi (COG) complex, as identified by TurboID proximity labeling and immunoprecipitation.","method":"TurboID proximity labeling, immunoprecipitation/mass spectrometry","journal":"mBio","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal proximity labeling and co-IP in a single lab, two orthogonal methods (TurboID + IP)","pmids":["39345210","38352341"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2018,"finding":"Recombinant TgUlp1 functions as an active SUMO protease, capable of removing SUMO from a sumoylated substrate in vitro, and can rescue the growth-deficient phenotype of a yeast Ulp1 knockout, establishing it as the key enzyme in T. gondii sumoylation/desumoylation pathways.","method":"In vitro desumoylation assay with recombinant protein; functional complementation in yeast Ulp1 knockout","journal":"International journal for parasitology","confidence":"High","confidence_rationale":"Tier 1 / Moderate — direct in vitro enzymatic assay plus cross-species functional complementation in a single rigorous study with two orthogonal methods","pmids":["30005881"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""},{"species":"Saccharomyces cerevisiae","strain":""}]},{"year":2018,"finding":"Expression and enzymatic activity of TgUlp1 is post-transcriptionally regulated by Tg-miR-60 (a T. gondii microRNA); inhibition of Tg-miR-60 increases TgUlp1 expression and its SUMO protease activity, which in turn affects parasite growth fitness.","method":"Transgenic epitope-tagged strain, miR-60 inhibitor transfection, enzymatic activity assay, growth assay","journal":"International journal for parasitology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — miRNA inhibitor experiment with matched enzymatic activity and growth readouts in a single lab, two orthogonal functional methods","pmids":["30005881"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2020,"finding":"A natural antisense transcript (TgUlp1-NAT1) from the TgUlp1 locus down-regulates TgUlp1 mRNA expression via the RNA interference pathway (requiring TgDicer), as shown by reporter assays and a TgDicer-knockout strain; TgUlp1-NAT1 promoter activity resides within the 3'-region of the TgUlp1 coding sequence.","method":"Dual luciferase reporter assay, in vitro RNase III processing, TgDicer knockout strain analysis, reporter knockdown assay","journal":"Molecular and biochemical parasitology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic (Dicer-KO epistasis) plus reporter assay in single lab, two orthogonal methods; this concerns the non-coding regulatory product, but the functional consequence directly affects TgUlp1 protein levels","pmids":["33011210"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"T. gondii ULP1 is a Golgi-localized SUMO protease (structurally related to p115/Uso1) that is essential for microneme secretion, host cell invasion, intracellular replication, and egress; it interacts with the conserved oligomeric Golgi (COG) complex and its expression is post-transcriptionally controlled by the microRNA Tg-miR-60 and a natural antisense transcript (TgUlp1-NAT1) acting through the RNAi pathway."},"narrative":{"mechanistic_narrative":"Toxoplasma gondii ULP1 is an active SUMO protease that couples desumoylation activity to the parasite's secretory pathway and lytic cycle [PMID:39345210, PMID:38352341, PMID:30005881]. Recombinant TgUlp1 removes SUMO from a sumoylated substrate in vitro and functionally complements a yeast Ulp1 knockout, establishing it as a key enzyme in T. gondii sumoylation/desumoylation [PMID:30005881]. The protein localizes to the Golgi apparatus, is structurally similar to the trafficking factor p115/Uso1, and physically associates with the conserved oligomeric Golgi (COG) complex [PMID:39345210, PMID:38352341]; conditional depletion impairs microneme secretion, host cell invasion, intracellular replication, and egress, defining an essential role in the secretory pathway [PMID:39345210, PMID:38352341]. TgUlp1 abundance and protease activity are set post-transcriptionally: the microRNA Tg-miR-60 restrains its expression and activity [PMID:30005881], and a natural antisense transcript, TgUlp1-NAT1, down-regulates TgUlp1 mRNA through the RNAi pathway in a TgDicer-dependent manner [PMID:33011210].","teleology":[{"year":2018,"claim":"Whether TgUlp1 is a functional SUMO protease was unknown; demonstrating in vitro desumoylation and yeast complementation established it as the enzyme driving T. gondii desumoylation.","evidence":"In vitro desumoylation assay with recombinant protein and functional complementation of a yeast Ulp1 knockout","pmids":["30005881"],"confidence":"High","gaps":["Endogenous SUMO substrates in T. gondii not identified","Subcellular site of desumoylation not linked to enzymatic activity in this study"],"attribution":[{"species":"Toxoplasma gondii","strain":""},{"species":"Saccharomyces cerevisiae","strain":""}]},{"year":2018,"claim":"How TgUlp1 levels are controlled was unknown; showing that Tg-miR-60 inhibition raises TgUlp1 expression, protease activity, and growth fitness established post-transcriptional regulation by a parasite microRNA.","evidence":"Transgenic epitope-tagged strain with miR-60 inhibitor transfection, enzymatic activity and growth assays","pmids":["30005881"],"confidence":"Medium","gaps":["Direct binding of Tg-miR-60 to the TgUlp1 transcript not demonstrated","Physiological conditions triggering miR-60 regulation unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2020,"claim":"A second layer of TgUlp1 control was defined by identifying a natural antisense transcript (TgUlp1-NAT1) that lowers TgUlp1 mRNA through the RNAi pathway, revealing Dicer-dependent locus-encoded regulation.","evidence":"Dual luciferase reporter assay, in vitro RNase III processing, and TgDicer-knockout strain analysis","pmids":["33011210"],"confidence":"Medium","gaps":["Quantitative contribution of NAT1 to endogenous TgUlp1 protein levels not established","Interplay between NAT1 and Tg-miR-60 regulation unresolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"claim":"The cellular role of TgUlp1 was undefined; Golgi localization, structural similarity to p115/Uso1, COG-complex interaction, and conditional depletion phenotypes established it as essential for the secretory pathway and the lytic cycle.","evidence":"Conditional knockdown with imaging, plaque/invasion/egress and microneme secretion assays, plus TurboID proximity labeling and co-IP/MS","pmids":["39345210","38352341"],"confidence":"High","gaps":["Mechanistic link between SUMO protease activity and Golgi trafficking not established","Whether COG-complex components are desumoylation substrates unknown","How ULP1 depletion mechanistically blocks microneme secretion unresolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"It remains unknown how TgUlp1's catalytic SUMO protease activity is mechanistically integrated with its Golgi/COG-associated trafficking function and its endogenous substrates.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No endogenous SUMO substrate identified at the Golgi","No structural model connecting protease and trafficking roles","Catalytic-dead depletion complementation to separate the two functions not reported"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Conserved oligomeric Golgi (COG) complex (interaction partner)"],"partners":["COG COMPLEX COMPONENTS (TURBOID/CO-IP)","SUMO (SUBSTRATE)","TG-MIR-60 (POST-TRANSCRIPTIONAL REGULATOR)","TGULP1-NAT1 NATURAL ANTISENSE TRANSCRIPT (REGULATOR)","TGDICER (RNAI PATHWAY COMPONENT ACTING ON NAT1)"],"other_free_text":["Structurally similar to the eukaryotic trafficking factor p115/Uso1 [#0]","Essential for microneme secretion, host cell invasion, intracellular replication, and egress [#0]","Expression controlled by two post-transcriptional mechanisms: Tg-miR-60 and a Dicer-dependent natural antisense transcript [#3, #4]"]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"39345210","id":"PMC_39345210","title":"Characterization and functional analysis of Toxoplasma Golgi-associated proteins identified by proximity labeling.","date":"2024","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/39345210","citation_count":8,"is_preprint":false},{"pmid":"30005881","id":"PMC_30005881","title":"Toxoplasma ubiquitin-like protease 1, a key enzyme in sumoylation and desumoylation pathways, is under the control of non-coding RNAs.","date":"2018","source":"International journal for parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/30005881","citation_count":8,"is_preprint":false},{"pmid":"33011210","id":"PMC_33011210","title":"Characterization of natural antisense transcripts arisen from the locus encoding Toxoplasma gondii ubiquitin-like protease.","date":"2020","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/33011210","citation_count":2,"is_preprint":false},{"pmid":"38352341","id":"PMC_38352341","title":"Characterization and functional analysis of Toxoplasma Golgi-associated proteins identified by proximity labelling.","date":"2024","source":"bioRxiv : the preprint server for biology","url":"https://pubmed.ncbi.nlm.nih.gov/38352341","citation_count":1,"is_preprint":false},{"pmid":"40086715","id":"PMC_40086715","title":"Involvement of Toxoplasma gondii natural antisense transcripts in cellular stress responses.","date":"2025","source":"Experimental parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/40086715","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5398,"output_tokens":1475,"usd":0.019159,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6507,"output_tokens":2501,"usd":0.04753,"stage2_stop_reason":"end_turn"},"total_usd":0.066689,"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\": 2024,\n      \"finding\": \"T. gondii ULP1 localizes to the Golgi apparatus and is structurally similar to the eukaryotic trafficking factor p115/Uso1. Conditional depletion of ULP1 causes defects in microneme secretion, invasion, replication, and egress, demonstrating an essential role in the secretory pathway.\",\n      \"method\": \"Conditional knockdown, live/fixed imaging for Golgi localization, plaque/invasion/egress assays, microneme secretion assay\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — conditional knockdown with multiple defined phenotypic readouts (microneme secretion, invasion, replication, egress) and structural characterization, replicated across preprint and peer-reviewed publication by the same lab with orthogonal methods\",\n      \"pmids\": [\"39345210\", \"38352341\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"ULP1 physically interacts with the T. gondii conserved oligomeric Golgi (COG) complex, as identified by TurboID proximity labeling and immunoprecipitation.\",\n      \"method\": \"TurboID proximity labeling, immunoprecipitation/mass spectrometry\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal proximity labeling and co-IP in a single lab, two orthogonal methods (TurboID + IP)\",\n      \"pmids\": [\"39345210\", \"38352341\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Recombinant TgUlp1 functions as an active SUMO protease, capable of removing SUMO from a sumoylated substrate in vitro, and can rescue the growth-deficient phenotype of a yeast Ulp1 knockout, establishing it as the key enzyme in T. gondii sumoylation/desumoylation pathways.\",\n      \"method\": \"In vitro desumoylation assay with recombinant protein; functional complementation in yeast Ulp1 knockout\",\n      \"journal\": \"International journal for parasitology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — direct in vitro enzymatic assay plus cross-species functional complementation in a single rigorous study with two orthogonal methods\",\n      \"pmids\": [\"30005881\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"},\n        {\"species\": \"Saccharomyces cerevisiae\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Expression and enzymatic activity of TgUlp1 is post-transcriptionally regulated by Tg-miR-60 (a T. gondii microRNA); inhibition of Tg-miR-60 increases TgUlp1 expression and its SUMO protease activity, which in turn affects parasite growth fitness.\",\n      \"method\": \"Transgenic epitope-tagged strain, miR-60 inhibitor transfection, enzymatic activity assay, growth assay\",\n      \"journal\": \"International journal for parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — miRNA inhibitor experiment with matched enzymatic activity and growth readouts in a single lab, two orthogonal functional methods\",\n      \"pmids\": [\"30005881\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"A natural antisense transcript (TgUlp1-NAT1) from the TgUlp1 locus down-regulates TgUlp1 mRNA expression via the RNA interference pathway (requiring TgDicer), as shown by reporter assays and a TgDicer-knockout strain; TgUlp1-NAT1 promoter activity resides within the 3'-region of the TgUlp1 coding sequence.\",\n      \"method\": \"Dual luciferase reporter assay, in vitro RNase III processing, TgDicer knockout strain analysis, reporter knockdown assay\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic (Dicer-KO epistasis) plus reporter assay in single lab, two orthogonal methods; this concerns the non-coding regulatory product, but the functional consequence directly affects TgUlp1 protein levels\",\n      \"pmids\": [\"33011210\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"T. gondii ULP1 is a Golgi-localized SUMO protease (structurally related to p115/Uso1) that is essential for microneme secretion, host cell invasion, intracellular replication, and egress; it interacts with the conserved oligomeric Golgi (COG) complex and its expression is post-transcriptionally controlled by the microRNA Tg-miR-60 and a natural antisense transcript (TgUlp1-NAT1) acting through the RNAi pathway.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"Toxoplasma gondii ULP1 is an active SUMO protease that couples desumoylation activity to the parasite's secretory pathway and lytic cycle [#0, #2]. Recombinant TgUlp1 removes SUMO from a sumoylated substrate in vitro and functionally complements a yeast Ulp1 knockout, establishing it as a key enzyme in T. gondii sumoylation/desumoylation [#2]. The protein localizes to the Golgi apparatus, is structurally similar to the trafficking factor p115/Uso1, and physically associates with the conserved oligomeric Golgi (COG) complex [#0, #1]; conditional depletion impairs microneme secretion, host cell invasion, intracellular replication, and egress, defining an essential role in the secretory pathway [#0]. TgUlp1 abundance and protease activity are set post-transcriptionally: the microRNA Tg-miR-60 restrains its expression and activity [#3], and a natural antisense transcript, TgUlp1-NAT1, down-regulates TgUlp1 mRNA through the RNAi pathway in a TgDicer-dependent manner [#4].\",\n  \"teleology\": [\n    {\n      \"year\": 2018,\n      \"claim\": \"Whether TgUlp1 is a functional SUMO protease was unknown; demonstrating in vitro desumoylation and yeast complementation established it as the enzyme driving T. gondii desumoylation.\",\n      \"evidence\": \"In vitro desumoylation assay with recombinant protein and functional complementation of a yeast Ulp1 knockout\",\n      \"pmids\": [\"30005881\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Endogenous SUMO substrates in T. gondii not identified\",\n        \"Subcellular site of desumoylation not linked to enzymatic activity in this study\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"},\n        {\"species\": \"Saccharomyces cerevisiae\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"How TgUlp1 levels are controlled was unknown; showing that Tg-miR-60 inhibition raises TgUlp1 expression, protease activity, and growth fitness established post-transcriptional regulation by a parasite microRNA.\",\n      \"evidence\": \"Transgenic epitope-tagged strain with miR-60 inhibitor transfection, enzymatic activity and growth assays\",\n      \"pmids\": [\"30005881\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Direct binding of Tg-miR-60 to the TgUlp1 transcript not demonstrated\",\n        \"Physiological conditions triggering miR-60 regulation unknown\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"A second layer of TgUlp1 control was defined by identifying a natural antisense transcript (TgUlp1-NAT1) that lowers TgUlp1 mRNA through the RNAi pathway, revealing Dicer-dependent locus-encoded regulation.\",\n      \"evidence\": \"Dual luciferase reporter assay, in vitro RNase III processing, and TgDicer-knockout strain analysis\",\n      \"pmids\": [\"33011210\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Quantitative contribution of NAT1 to endogenous TgUlp1 protein levels not established\",\n        \"Interplay between NAT1 and Tg-miR-60 regulation unresolved\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"The cellular role of TgUlp1 was undefined; Golgi localization, structural similarity to p115/Uso1, COG-complex interaction, and conditional depletion phenotypes established it as essential for the secretory pathway and the lytic cycle.\",\n      \"evidence\": \"Conditional knockdown with imaging, plaque/invasion/egress and microneme secretion assays, plus TurboID proximity labeling and co-IP/MS\",\n      \"pmids\": [\"39345210\", \"38352341\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Mechanistic link between SUMO protease activity and Golgi trafficking not established\",\n        \"Whether COG-complex components are desumoylation substrates unknown\",\n        \"How ULP1 depletion mechanistically blocks microneme secretion unresolved\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unknown how TgUlp1's catalytic SUMO protease activity is mechanistically integrated with its Golgi/COG-associated trafficking function and its endogenous substrates.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No endogenous SUMO substrate identified at the Golgi\",\n        \"No structural model connecting protease and trafficking roles\",\n        \"Catalytic-dead depletion complementation to separate the two functions not reported\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0016929\", \"supporting_discovery_ids\": [2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}, {\"species\": \"Saccharomyces cerevisiae\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005794\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0046903\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0016925\", \"supporting_discovery_ids\": [2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [\n      \"Conserved oligomeric Golgi (COG) complex (interaction partner)\"\n    ],\n    \"partners\": [\n      \"COG complex components (TurboID/co-IP)\",\n      \"SUMO (substrate)\",\n      \"Tg-miR-60 (post-transcriptional regulator)\",\n      \"TgUlp1-NAT1 natural antisense transcript (regulator)\",\n      \"TgDicer (RNAi pathway component acting on NAT1)\"\n    ],\n    \"other_free_text\": [\n      \"Structurally similar to the eukaryotic trafficking factor p115/Uso1 [#0]\",\n      \"Essential for microneme secretion, host cell invasion, intracellular replication, and egress [#0]\",\n      \"Expression controlled by two post-transcriptional mechanisms: Tg-miR-60 and a Dicer-dependent natural antisense transcript [#3, #4]\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_289120","name":"ULP1","product":"Uso1-like protein ULP1","uniprot_acc":"S8F360","chromosome":"TGME49_chrIX","start_pos":3001559},{"strain":"GT1","gene_id":"TGGT1_289120","name":null,"product":"hypothetical protein","uniprot_acc":null,"chromosome":"TGGT1_chrIX","start_pos":2810023},{"strain":"RH88","gene_id":"TGRH88_013940","name":null,"product":"unspecified product","uniprot_acc":null,"chromosome":"CM023090","start_pos":3065603},{"strain":"VEG","gene_id":"TGVEG_289120","name":null,"product":"putative glutamic acid-rich protein","uniprot_acc":"V4ZNF6","chromosome":"TGVEG_chrIX","start_pos":3036155}]}