{"gene":"TG_200290","gene_symbol":"ROM1","run_date":"2026-09-07T10:25:42","timeline":{"discoveries":[{"year":2005,"finding":"TgROM1 is an active rhomboid intramembrane serine protease; it cleaves the transmembrane domain of Drosophila Spitz in a cell-based assay, demonstrating catalytic activity with substrate specificity similar to other rhomboid family members.","method":"Cell-based protease activity assay using Drosophila Spitz as a substrate","journal":"International journal for parasitology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — in vitro/cell-based enzymatic assay in a single lab, single method","pmids":["15913633"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2005,"finding":"TgROM1 is expressed in tachyzoites and localizes to internal compartments (not the cell surface), distinct from TgROM4 and TgROM5 which localize to the parasite surface; TgROM1 was not found to colocalize with adhesins at the posterior cleavage site during invasion.","method":"Immunofluorescence localization and co-localization analysis in tachyzoites","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization by immunofluorescence, two independent labs reporting consistent internal/non-surface localization","pmids":["15753289","15913633"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2008,"finding":"TgROM1 localizes to the Golgi apparatus and micronemes in the secretory pathway but is not released onto the parasite surface during host cell invasion, indicating it does not act as a surface sheddase during invasion.","method":"Subcellular fractionation, immunofluorescence, and live imaging during invasion","journal":"Eukaryotic cell","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization and functional invasion assay, single lab with multiple methods","pmids":["18310358"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2008,"finding":"Suppression of TgROM1 using a tetracycline-regulatable system showed that ROM1-deficient parasites replicated more slowly than wild-type and were outcompeted, demonstrating TgROM1 is required for efficient intracellular growth but only modestly affects invasion.","method":"Tetracycline-regulatable knockdown, competition assay, intracellular replication assay, invasion assay","journal":"Eukaryotic cell","confidence":"High","confidence_rationale":"Tier 2 / Moderate — inducible knockdown with specific phenotypic readouts (replication and invasion) using multiple assays in a single rigorous study","pmids":["18310358"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2008,"finding":"The N-terminal cytosolic domain of TgROM1 contains critical sorting determinants that confer its post-Golgi (microneme) localization, as established by domain-exchange and site-directed mutagenesis experiments.","method":"Domain-exchange chimeras and site-directed mutagenesis with immunofluorescence readout","journal":"Traffic (Copenhagen, Denmark)","confidence":"High","confidence_rationale":"Tier 1 / Moderate — mutagenesis and domain-swap experiments with direct localization readout, single lab with multiple orthogonal approaches","pmids":["18346213"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2008,"finding":"The membrane topology of TgROM1 at the plasma membrane was experimentally established using domain-exchange and topology assays.","method":"Topology assay (protease protection/domain-exchange approach)","journal":"Traffic (Copenhagen, Denmark)","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — direct topology experiment, single lab, single study","pmids":["18346213"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"finding":"Genetic knockout of ROM1 alone or in combination with ROM4 and ROM5 demonstrated that ROM1 plays a negligible role in adhesin shedding (e.g., MIC2 cleavage) and host cell invasion; ROM4 is the primary protease for these processes.","method":"Single, double, and triple knockout generation; adhesin shedding assay; invasion assay; gliding motility assay","journal":"mBio","confidence":"High","confidence_rationale":"Tier 2 / Strong — clean genetic knockouts with multiple orthogonal functional assays (invasion, motility, adhesin shedding), single rigorous study with definitive epistasis","pmids":["25336455"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"TgROM1 is an active intramembrane serine protease that localizes to micronemes and Golgi via N-terminal sorting determinants, is not secreted to the parasite surface during invasion, plays a negligible role in adhesin (MIC2) shedding and host cell invasion (functions primarily performed by ROM4), but is required for efficient intracellular replication of Toxoplasma gondii tachyzoites."},"narrative":{"mechanistic_narrative":"ROM1 encodes an active rhomboid intramembrane serine protease of Toxoplasma gondii that participates in the parasite's secretory pathway and intracellular growth rather than in surface adhesin processing [PMID:15913633, PMID:18310358]. Its catalytic activity was established in a cell-based assay where it cleaves the transmembrane domain of Drosophila Spitz with substrate specificity typical of the rhomboid family [PMID:15913633]. Unlike the surface-localized rhomboids ROM4 and ROM5, TgROM1 resides in internal secretory compartments — the Golgi apparatus and micronemes — and is not released onto the parasite surface during invasion [PMID:15753289, PMID:15913633, PMID:18310358]; N-terminal cytosolic sorting determinants direct this post-Golgi microneme localization [PMID:18346213]. Functionally, ROM1 contributes negligibly to adhesin (MIC2) shedding, gliding motility, and host cell invasion, processes driven primarily by ROM4, but is required for efficient intracellular replication of tachyzoites [PMID:18310358, PMID:25336455]. The physiological substrate cleaved by ROM1 during intracellular growth has not been identified in the available corpus.","teleology":[{"year":2005,"claim":"Establishing whether TgROM1 is a functional enzyme was the first prerequisite; the cell-based Spitz cleavage assay confirmed it is a catalytically active rhomboid intramembrane serine protease with defined substrate specificity.","evidence":"Cell-based protease activity assay using Drosophila Spitz as substrate","pmids":["15913633"],"confidence":"Medium","gaps":["No endogenous parasite substrate identified","Activity shown only against a heterologous model substrate"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2005,"claim":"Whether ROM1 acts as a surface sheddase like other parasite rhomboids was addressed by localization, which showed it resides in internal compartments distinct from surface-localized ROM4/ROM5 and does not colocalize with adhesins at the invasion cleavage site.","evidence":"Immunofluorescence and co-localization analysis in tachyzoites","pmids":["15753289","15913633"],"confidence":"Medium","gaps":["Precise internal compartment not resolved at this stage","Function of internal localization not defined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2008,"claim":"Refining the localization pinpointed ROM1 to the Golgi and micronemes and confirmed it is not delivered to the parasite surface during invasion, arguing against a role as an invasion sheddase.","evidence":"Subcellular fractionation, immunofluorescence, and live imaging during invasion","pmids":["18310358"],"confidence":"Medium","gaps":["Substrate acted upon within the secretory pathway unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2008,"claim":"The functional consequence of losing ROM1 was tested by regulatable knockdown, revealing a requirement for efficient intracellular replication with only modest effect on invasion, distinguishing ROM1's role from surface-acting rhomboids.","evidence":"Tetracycline-regulatable knockdown with competition, intracellular replication, and invasion assays","pmids":["18310358"],"confidence":"High","gaps":["Molecular basis of the replication defect not established","Substrate whose cleavage drives replication unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2008,"claim":"How ROM1 achieves its non-surface localization was answered by mapping N-terminal cytosolic sorting determinants required for post-Golgi microneme targeting, and by defining its membrane topology.","evidence":"Domain-exchange chimeras, site-directed mutagenesis, and topology assays with immunofluorescence readout","pmids":["18346213"],"confidence":"High","gaps":["Trafficking machinery recognizing the sorting determinants not identified"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"claim":"Definitive genetic epistasis using single, double, and triple knockouts settled ROM1's role in invasion, showing it is negligible for adhesin (MIC2) shedding and invasion while ROM4 performs these functions.","evidence":"Single/double/triple knockout generation with adhesin shedding, invasion, and gliding motility assays","pmids":["25336455"],"confidence":"High","gaps":["Positive intracellular substrate of ROM1 still not defined","Mechanism linking ROM1 protease activity to replication unresolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"The endogenous substrate cleaved by ROM1 within the secretory pathway that underlies its requirement for efficient intracellular replication remains unidentified.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No physiological substrate identified","Molecular mechanism connecting protease activity to replication unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":[],"other_free_text":["Required for efficient intracellular replication of tachyzoites [#3]","Negligible role in MIC2 adhesin shedding, gliding motility, and host cell invasion; ROM4 is the primary invasion sheddase [#6]","N-terminal cytosolic domain contains sorting determinants for post-Golgi/microneme targeting [#4]","Not released onto the parasite surface during invasion, unlike ROM4/ROM5 [#1, #2]"]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"15753289","id":"PMC_15753289","title":"A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma.","date":"2005","source":"Proceedings of the National Academy of Sciences of the United States of America","url":"https://pubmed.ncbi.nlm.nih.gov/15753289","citation_count":171,"is_preprint":false},{"pmid":"15913633","id":"PMC_15913633","title":"Apicomplexan rhomboids have a potential role in microneme protein cleavage during host cell invasion.","date":"2005","source":"International journal for parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/15913633","citation_count":98,"is_preprint":false},{"pmid":"15358257","id":"PMC_15358257","title":"Host cell invasion by the apicomplexans: the significance of microneme protein proteolysis.","date":"2004","source":"Current opinion in microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/15358257","citation_count":72,"is_preprint":false},{"pmid":"25336455","id":"PMC_25336455","title":"Functional analysis of rhomboid proteases during Toxoplasma invasion.","date":"2014","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/25336455","citation_count":55,"is_preprint":false},{"pmid":"18310358","id":"PMC_18310358","title":"Microneme rhomboid protease TgROM1 is required for efficient intracellular growth of Toxoplasma gondii.","date":"2008","source":"Eukaryotic cell","url":"https://pubmed.ncbi.nlm.nih.gov/18310358","citation_count":41,"is_preprint":false},{"pmid":"18346213","id":"PMC_18346213","title":"Identification of trafficking determinants for polytopic rhomboid proteases in Toxoplasma gondii.","date":"2008","source":"Traffic (Copenhagen, Denmark)","url":"https://pubmed.ncbi.nlm.nih.gov/18346213","citation_count":27,"is_preprint":false},{"pmid":"28077075","id":"PMC_28077075","title":"Protection via a ROM4 DNA vaccine and peptide against Toxoplasma gondii in BALB/c mice.","date":"2017","source":"BMC infectious diseases","url":"https://pubmed.ncbi.nlm.nih.gov/28077075","citation_count":25,"is_preprint":false},{"pmid":"21906881","id":"PMC_21906881","title":"Toxoplasma gondii rhomboid protein 1 (TgROM1) is a potential vaccine candidate against toxoplasmosis.","date":"2011","source":"Veterinary parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/21906881","citation_count":19,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6186,"output_tokens":1626,"usd":0.021474,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6800,"output_tokens":2520,"usd":0.0485,"stage2_stop_reason":"end_turn"},"total_usd":0.069974,"stage1_batch_id":"msgbatch_018xTxyBPcQFK9jdgubtxgsj","stage2_batch_id":"msgbatch_01UiG5BTaJP7BvKKL6RLeyv2","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2005,\n      \"finding\": \"TgROM1 is an active rhomboid intramembrane serine protease; it cleaves the transmembrane domain of Drosophila Spitz in a cell-based assay, demonstrating catalytic activity with substrate specificity similar to other rhomboid family members.\",\n      \"method\": \"Cell-based protease activity assay using Drosophila Spitz as a substrate\",\n      \"journal\": \"International journal for parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — in vitro/cell-based enzymatic assay in a single lab, single method\",\n      \"pmids\": [\"15913633\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2005,\n      \"finding\": \"TgROM1 is expressed in tachyzoites and localizes to internal compartments (not the cell surface), distinct from TgROM4 and TgROM5 which localize to the parasite surface; TgROM1 was not found to colocalize with adhesins at the posterior cleavage site during invasion.\",\n      \"method\": \"Immunofluorescence localization and co-localization analysis in tachyzoites\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization by immunofluorescence, two independent labs reporting consistent internal/non-surface localization\",\n      \"pmids\": [\"15753289\", \"15913633\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"finding\": \"TgROM1 localizes to the Golgi apparatus and micronemes in the secretory pathway but is not released onto the parasite surface during host cell invasion, indicating it does not act as a surface sheddase during invasion.\",\n      \"method\": \"Subcellular fractionation, immunofluorescence, and live imaging during invasion\",\n      \"journal\": \"Eukaryotic cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization and functional invasion assay, single lab with multiple methods\",\n      \"pmids\": [\"18310358\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"finding\": \"Suppression of TgROM1 using a tetracycline-regulatable system showed that ROM1-deficient parasites replicated more slowly than wild-type and were outcompeted, demonstrating TgROM1 is required for efficient intracellular growth but only modestly affects invasion.\",\n      \"method\": \"Tetracycline-regulatable knockdown, competition assay, intracellular replication assay, invasion assay\",\n      \"journal\": \"Eukaryotic cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — inducible knockdown with specific phenotypic readouts (replication and invasion) using multiple assays in a single rigorous study\",\n      \"pmids\": [\"18310358\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"finding\": \"The N-terminal cytosolic domain of TgROM1 contains critical sorting determinants that confer its post-Golgi (microneme) localization, as established by domain-exchange and site-directed mutagenesis experiments.\",\n      \"method\": \"Domain-exchange chimeras and site-directed mutagenesis with immunofluorescence readout\",\n      \"journal\": \"Traffic (Copenhagen, Denmark)\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — mutagenesis and domain-swap experiments with direct localization readout, single lab with multiple orthogonal approaches\",\n      \"pmids\": [\"18346213\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"finding\": \"The membrane topology of TgROM1 at the plasma membrane was experimentally established using domain-exchange and topology assays.\",\n      \"method\": \"Topology assay (protease protection/domain-exchange approach)\",\n      \"journal\": \"Traffic (Copenhagen, Denmark)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — direct topology experiment, single lab, single study\",\n      \"pmids\": [\"18346213\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"Genetic knockout of ROM1 alone or in combination with ROM4 and ROM5 demonstrated that ROM1 plays a negligible role in adhesin shedding (e.g., MIC2 cleavage) and host cell invasion; ROM4 is the primary protease for these processes.\",\n      \"method\": \"Single, double, and triple knockout generation; adhesin shedding assay; invasion assay; gliding motility assay\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — clean genetic knockouts with multiple orthogonal functional assays (invasion, motility, adhesin shedding), single rigorous study with definitive epistasis\",\n      \"pmids\": [\"25336455\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"TgROM1 is an active intramembrane serine protease that localizes to micronemes and Golgi via N-terminal sorting determinants, is not secreted to the parasite surface during invasion, plays a negligible role in adhesin (MIC2) shedding and host cell invasion (functions primarily performed by ROM4), but is required for efficient intracellular replication of Toxoplasma gondii tachyzoites.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"ROM1 encodes an active rhomboid intramembrane serine protease of Toxoplasma gondii that participates in the parasite's secretory pathway and intracellular growth rather than in surface adhesin processing [#0, #3]. Its catalytic activity was established in a cell-based assay where it cleaves the transmembrane domain of Drosophila Spitz with substrate specificity typical of the rhomboid family [#0]. Unlike the surface-localized rhomboids ROM4 and ROM5, TgROM1 resides in internal secretory compartments — the Golgi apparatus and micronemes — and is not released onto the parasite surface during invasion [#1, #2]; N-terminal cytosolic sorting determinants direct this post-Golgi microneme localization [#4]. Functionally, ROM1 contributes negligibly to adhesin (MIC2) shedding, gliding motility, and host cell invasion, processes driven primarily by ROM4, but is required for efficient intracellular replication of tachyzoites [#3, #6]. The physiological substrate cleaved by ROM1 during intracellular growth has not been identified in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2005,\n      \"claim\": \"Establishing whether TgROM1 is a functional enzyme was the first prerequisite; the cell-based Spitz cleavage assay confirmed it is a catalytically active rhomboid intramembrane serine protease with defined substrate specificity.\",\n      \"evidence\": \"Cell-based protease activity assay using Drosophila Spitz as substrate\",\n      \"pmids\": [\"15913633\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No endogenous parasite substrate identified\", \"Activity shown only against a heterologous model substrate\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2005,\n      \"claim\": \"Whether ROM1 acts as a surface sheddase like other parasite rhomboids was addressed by localization, which showed it resides in internal compartments distinct from surface-localized ROM4/ROM5 and does not colocalize with adhesins at the invasion cleavage site.\",\n      \"evidence\": \"Immunofluorescence and co-localization analysis in tachyzoites\",\n      \"pmids\": [\"15753289\", \"15913633\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Precise internal compartment not resolved at this stage\", \"Function of internal localization not defined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"claim\": \"Refining the localization pinpointed ROM1 to the Golgi and micronemes and confirmed it is not delivered to the parasite surface during invasion, arguing against a role as an invasion sheddase.\",\n      \"evidence\": \"Subcellular fractionation, immunofluorescence, and live imaging during invasion\",\n      \"pmids\": [\"18310358\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Substrate acted upon within the secretory pathway unknown\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"claim\": \"The functional consequence of losing ROM1 was tested by regulatable knockdown, revealing a requirement for efficient intracellular replication with only modest effect on invasion, distinguishing ROM1's role from surface-acting rhomboids.\",\n      \"evidence\": \"Tetracycline-regulatable knockdown with competition, intracellular replication, and invasion assays\",\n      \"pmids\": [\"18310358\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular basis of the replication defect not established\", \"Substrate whose cleavage drives replication unknown\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"claim\": \"How ROM1 achieves its non-surface localization was answered by mapping N-terminal cytosolic sorting determinants required for post-Golgi microneme targeting, and by defining its membrane topology.\",\n      \"evidence\": \"Domain-exchange chimeras, site-directed mutagenesis, and topology assays with immunofluorescence readout\",\n      \"pmids\": [\"18346213\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Trafficking machinery recognizing the sorting determinants not identified\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Definitive genetic epistasis using single, double, and triple knockouts settled ROM1's role in invasion, showing it is negligible for adhesin (MIC2) shedding and invasion while ROM4 performs these functions.\",\n      \"evidence\": \"Single/double/triple knockout generation with adhesin shedding, invasion, and gliding motility assays\",\n      \"pmids\": [\"25336455\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Positive intracellular substrate of ROM1 still not defined\", \"Mechanism linking ROM1 protease activity to replication unresolved\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The endogenous substrate cleaved by ROM1 within the secretory pathway that underlies its requirement for efficient intracellular replication remains unidentified.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No physiological substrate identified\", \"Molecular mechanism connecting protease activity to replication unknown\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0004252\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005794\", \"supporting_discovery_ids\": [2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0020009\", \"supporting_discovery_ids\": [1, 2, 4], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006508\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"Required for efficient intracellular replication of tachyzoites [#3]\",\n      \"Negligible role in MIC2 adhesin shedding, gliding motility, and host cell invasion; ROM4 is the primary invasion sheddase [#6]\",\n      \"N-terminal cytosolic domain contains sorting determinants for post-Golgi/microneme targeting [#4]\",\n      \"Not released onto the parasite surface during invasion, unlike ROM4/ROM5 [#1, #2]\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_200290","name":"ROM1","product":"rhomboid protease ROM1","uniprot_acc":"S8G8W2","chromosome":"TGME49_chrVIII","start_pos":6774898},{"strain":"GT1","gene_id":"TGGT1_200290","name":null,"product":"rhomboid protease ROM1","uniprot_acc":null,"chromosome":"TGGT1_chrVIII","start_pos":6751037},{"strain":"RH88","gene_id":"TGRH88_083130","name":null,"product":"rhomboid protease ROM1","uniprot_acc":null,"chromosome":"CM023089","start_pos":11903335},{"strain":"VEG","gene_id":"TGVEG_200290","name":null,"product":"rhomboid protease ROM1","uniprot_acc":"B9Q3N1","chromosome":"TGVEG_chrVIII","start_pos":6802498}]}