{"gene":"TG_294690","gene_symbol":"ROM5","run_date":"2026-09-08T14:08:30","timeline":{"discoveries":[{"year":2005,"finding":"TgROM5 is an active intramembrane serine protease localized primarily at the posterior pole of the tachyzoite surface; upon microneme secretion, the MIC2 adhesin translocates to the posterior and colocalizes exclusively with TgROM5, and only TgROM5 (not TgROM4) was able to cleave MIC adhesins in a cell-based cleavage assay.","method":"Cloning and characterization of T. gondii rhomboids; cell-based protease activity assay; immunofluorescence co-localization of MIC2 and TgROM5 during invasion","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"High","confidence_rationale":"Tier 2 / Moderate — cell-based substrate cleavage assay combined with direct co-localization during invasion, single lab but multiple orthogonal methods","pmids":["15753289"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2005,"finding":"TgROM5 is an active rhomboid-family intramembrane serine protease that cleaves the transmembrane domain of Drosophila Spitz, an established rhomboid substrate, demonstrating bona fide protease activity.","method":"Cell-based heterologous substrate cleavage assay using Drosophila Spitz as substrate","journal":"International journal for parasitology","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — functional cell-based cleavage assay, single lab, single method","pmids":["15913633"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"finding":"Genetic knockouts of ROM5 (single, double, and triple with ROM1/ROM4) demonstrated that ROM5 plays a negligible role in adhesin processing and host cell invasion; ROM4, not ROM5, is the primary rhomboid protease responsible for adhesin shedding in tachyzoites.","method":"Single, double, and triple knockout generation; adhesin shedding assay (MIC2 surface accumulation); gliding motility assay; invasion efficiency assay; moving junction formation assay","journal":"mBio","confidence":"High","confidence_rationale":"Tier 2 / Strong — clean genetic knockouts with multiple orthogonal phenotypic readouts, directly tests ROM5 function in vivo","pmids":["25336455"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2015,"finding":"ROM5 knockout parasites show no alteration in MIC2 or MIC6 shedding or invasion efficiency; however, ROM5 is responsible for residual intramembrane cleavage of AMA1 (and other AMA family members) in the absence of ROM4, and exhibits a detectable contribution to invasion specifically in the absence of ROM4.","method":"CRISPR-Cas9 knockout of ROM5; Cre-recombinase knockout of ROM4; MIC2, MIC6, and AMA1 shedding assays; invasion assays in single and double knockout parasites","journal":"Molecular microbiology","confidence":"High","confidence_rationale":"Tier 2 / Strong — CRISPR-based knockouts combined with biochemical shedding assays and invasion assays, multiple substrates tested, independent from Sibley lab","pmids":["25846828"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2008,"finding":"TgROM4 and TgROM5 are both localized to the pellicle (plasma membrane) of T. gondii; domain-exchange and site-directed mutagenesis experiments identified critical sorting determinants in the N-terminal cytosolic domains of TgROM1 and TgROM2, but the specific determinants for TgROM4/5 pellicle targeting were not resolved in this study.","method":"Immunofluorescence localization; domain-exchange chimeras; site-directed mutagenesis of N-terminal cytosolic domains","journal":"Traffic (Copenhagen, Denmark)","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — direct localization by immunofluorescence confirmed pellicle targeting of ROM5, but trafficking determinants for ROM5 specifically were not experimentally resolved","pmids":["18346213"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"TgROM5 is an active intramembrane serine protease constitutively localized at the posterior pole of the Toxoplasma gondii tachyzoite pellicle; although early studies suggested it was the primary sheddase for MIC adhesins based on co-localization with translocated MIC2 and cell-based cleavage activity, genetic knockout studies established that ROM4 is the dominant adhesin-processing rhomboid during invasion, while ROM5 plays a negligible role in MIC2/MIC6 shedding but contributes residual intramembrane cleavage of AMA1 and related family members, becoming detectably important for invasion only in the absence of ROM4."},"narrative":{"mechanistic_narrative":"TgROM5 is an active rhomboid-family intramembrane serine protease of Toxoplasma gondii that acts at the parasite pellicle to cleave the transmembrane domains of surface adhesins during host cell invasion [PMID:15753289, PMID:15913633]. It is a bona fide protease, cleaving the transmembrane domain of the heterologous rhomboid substrate Drosophila Spitz [PMID:15913633], and localizes to the pellicle, concentrating at the posterior pole where the translocated MIC2 adhesin accumulates and colocalizes with it during invasion [PMID:15753289, PMID:18346213]. Although early cell-based cleavage and co-localization data implicated ROM5 as the principal MIC-adhesin sheddase [PMID:15753289], genetic knockout studies overturned this: single, double, and triple knockouts showed ROM5 plays a negligible role in MIC2/MIC6 shedding and invasion, with ROM4 serving as the dominant adhesin-processing rhomboid [PMID:25336455, PMID:25846828]. ROM5's residual physiological role is intramembrane cleavage of AMA1 (and other AMA family members), which becomes detectable only in the absence of ROM4 [PMID:25846828]. The sorting determinants directing ROM5 specifically to the pellicle have not been resolved in the available corpus [PMID:18346213].","teleology":[{"year":2005,"claim":"Establishing whether a Toxoplasma rhomboid could cleave the microneme adhesins that must be shed for invasion identified ROM5 as an active intramembrane protease colocalizing with translocated MIC2 at the posterior pole.","evidence":"Cloning and characterization of T. gondii rhomboids with cell-based cleavage assay and IF co-localization of MIC2 during invasion","pmids":["15753289"],"confidence":"High","gaps":["Cell-based cleavage and co-localization do not establish that ROM5 is the sheddase responsible in vivo","No genetic loss-of-function test of ROM5 function"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2005,"claim":"Confirming ROM5 was a genuine protease rather than merely a rhomboid homolog, it cleaved the transmembrane domain of the canonical rhomboid substrate Spitz.","evidence":"Cell-based heterologous cleavage assay using Drosophila Spitz","pmids":["15913633"],"confidence":"Medium","gaps":["Heterologous substrate does not define physiological substrates","Single method, single lab"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2008,"claim":"Determining where ROM5 acts, it was confirmed to reside at the pellicle, though the trafficking determinants specifying this localization were not resolved for ROM5.","evidence":"Immunofluorescence localization plus domain-exchange chimeras and site-directed mutagenesis of N-terminal cytosolic domains","pmids":["18346213"],"confidence":"Medium","gaps":["ROM4/ROM5-specific pellicle sorting determinants remain unidentified","Localization does not establish substrate access or function"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"claim":"Directly testing ROM5's in vivo requirement via knockouts overturned its assumed role as the primary adhesin sheddase, revealing ROM4 as the dominant adhesin-processing rhomboid and ROM5 as negligible for invasion.","evidence":"Single, double, and triple knockouts with adhesin shedding, gliding, invasion, and moving-junction assays","pmids":["25336455"],"confidence":"High","gaps":["Did not identify a distinct physiological substrate for ROM5","Possible functional redundancy masking ROM5 role not fully dissected"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2015,"claim":"Resolving what residual function ROM5 retains, ROM5/ROM4 double-knockout analysis showed ROM5 mediates residual intramembrane cleavage of AMA1 and contributes to invasion only when ROM4 is absent.","evidence":"CRISPR-Cas9 ROM5 knockout and Cre-recombinase ROM4 knockout with MIC2, MIC6, and AMA1 shedding assays and invasion assays","pmids":["25846828"],"confidence":"High","gaps":["Full physiological substrate repertoire of ROM5 not defined","Molecular basis of ROM4/ROM5 substrate discrimination unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"The determinants that restrict ROM5 to the posterior pole and the basis for its substrate preference for AMA-family adhesins over ROM4-preferred substrates remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["ROM5-specific pellicle/posterior-pole sorting determinants unidentified","Structural or biochemical basis of ROM5 versus ROM4 substrate selectivity unknown","No structural model of ROM5"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":[],"other_free_text":["Cleaves the transmembrane domains of adhesins; residual physiological substrate is AMA1 and other AMA-family members, detectable only in the absence of ROM4 [#3].","Cleaves the heterologous rhomboid substrate Drosophila Spitz, confirming bona fide intramembrane protease activity [#1].","Concentrates at the posterior pole of the tachyzoite pellicle, colocalizing with translocated MIC2 during invasion [#0].","ROM4, not ROM5, is the dominant adhesin-processing rhomboid during tachyzoite invasion [#2, #3]."]},"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":"11927542","id":"PMC_11927542","title":"Intramembrane cleavage of microneme proteins at the surface of the apicomplexan parasite Toxoplasma gondii.","date":"2002","source":"The EMBO journal","url":"https://pubmed.ncbi.nlm.nih.gov/11927542","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":"26111968","id":"PMC_26111968","title":"Protective efficacy of two novel DNA vaccines expressing Toxoplasma gondii rhomboid 4 and rhomboid 5 proteins against acute and chronic toxoplasmosis in mice.","date":"2015","source":"Expert review of vaccines","url":"https://pubmed.ncbi.nlm.nih.gov/26111968","citation_count":41,"is_preprint":false},{"pmid":"25846828","id":"PMC_25846828","title":"Distinct contribution of Toxoplasma gondii rhomboid proteases 4 and 5 to micronemal protein protease 1 activity during invasion.","date":"2015","source":"Molecular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/25846828","citation_count":39,"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}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5978,"output_tokens":1489,"usd":0.020134,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6575,"output_tokens":2494,"usd":0.047613,"stage2_stop_reason":"end_turn"},"total_usd":0.067747,"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\": 2005,\n      \"finding\": \"TgROM5 is an active intramembrane serine protease localized primarily at the posterior pole of the tachyzoite surface; upon microneme secretion, the MIC2 adhesin translocates to the posterior and colocalizes exclusively with TgROM5, and only TgROM5 (not TgROM4) was able to cleave MIC adhesins in a cell-based cleavage assay.\",\n      \"method\": \"Cloning and characterization of T. gondii rhomboids; cell-based protease activity assay; immunofluorescence co-localization of MIC2 and TgROM5 during invasion\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — cell-based substrate cleavage assay combined with direct co-localization during invasion, single lab but multiple orthogonal methods\",\n      \"pmids\": [\"15753289\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2005,\n      \"finding\": \"TgROM5 is an active rhomboid-family intramembrane serine protease that cleaves the transmembrane domain of Drosophila Spitz, an established rhomboid substrate, demonstrating bona fide protease activity.\",\n      \"method\": \"Cell-based heterologous substrate cleavage assay using Drosophila Spitz as substrate\",\n      \"journal\": \"International journal for parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — functional cell-based cleavage assay, single lab, single method\",\n      \"pmids\": [\"15913633\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"Genetic knockouts of ROM5 (single, double, and triple with ROM1/ROM4) demonstrated that ROM5 plays a negligible role in adhesin processing and host cell invasion; ROM4, not ROM5, is the primary rhomboid protease responsible for adhesin shedding in tachyzoites.\",\n      \"method\": \"Single, double, and triple knockout generation; adhesin shedding assay (MIC2 surface accumulation); gliding motility assay; invasion efficiency assay; moving junction formation assay\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — clean genetic knockouts with multiple orthogonal phenotypic readouts, directly tests ROM5 function in vivo\",\n      \"pmids\": [\"25336455\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"ROM5 knockout parasites show no alteration in MIC2 or MIC6 shedding or invasion efficiency; however, ROM5 is responsible for residual intramembrane cleavage of AMA1 (and other AMA family members) in the absence of ROM4, and exhibits a detectable contribution to invasion specifically in the absence of ROM4.\",\n      \"method\": \"CRISPR-Cas9 knockout of ROM5; Cre-recombinase knockout of ROM4; MIC2, MIC6, and AMA1 shedding assays; invasion assays in single and double knockout parasites\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — CRISPR-based knockouts combined with biochemical shedding assays and invasion assays, multiple substrates tested, independent from Sibley lab\",\n      \"pmids\": [\"25846828\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"finding\": \"TgROM4 and TgROM5 are both localized to the pellicle (plasma membrane) of T. gondii; domain-exchange and site-directed mutagenesis experiments identified critical sorting determinants in the N-terminal cytosolic domains of TgROM1 and TgROM2, but the specific determinants for TgROM4/5 pellicle targeting were not resolved in this study.\",\n      \"method\": \"Immunofluorescence localization; domain-exchange chimeras; site-directed mutagenesis of N-terminal cytosolic domains\",\n      \"journal\": \"Traffic (Copenhagen, Denmark)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — direct localization by immunofluorescence confirmed pellicle targeting of ROM5, but trafficking determinants for ROM5 specifically were not experimentally resolved\",\n      \"pmids\": [\"18346213\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"TgROM5 is an active intramembrane serine protease constitutively localized at the posterior pole of the Toxoplasma gondii tachyzoite pellicle; although early studies suggested it was the primary sheddase for MIC adhesins based on co-localization with translocated MIC2 and cell-based cleavage activity, genetic knockout studies established that ROM4 is the dominant adhesin-processing rhomboid during invasion, while ROM5 plays a negligible role in MIC2/MIC6 shedding but contributes residual intramembrane cleavage of AMA1 and related family members, becoming detectably important for invasion only in the absence of ROM4.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"TgROM5 is an active rhomboid-family intramembrane serine protease of Toxoplasma gondii that acts at the parasite pellicle to cleave the transmembrane domains of surface adhesins during host cell invasion [#0, #1]. It is a bona fide protease, cleaving the transmembrane domain of the heterologous rhomboid substrate Drosophila Spitz [#1], and localizes to the pellicle, concentrating at the posterior pole where the translocated MIC2 adhesin accumulates and colocalizes with it during invasion [#0, #4]. Although early cell-based cleavage and co-localization data implicated ROM5 as the principal MIC-adhesin sheddase [#0], genetic knockout studies overturned this: single, double, and triple knockouts showed ROM5 plays a negligible role in MIC2/MIC6 shedding and invasion, with ROM4 serving as the dominant adhesin-processing rhomboid [#2, #3]. ROM5's residual physiological role is intramembrane cleavage of AMA1 (and other AMA family members), which becomes detectable only in the absence of ROM4 [#3]. The sorting determinants directing ROM5 specifically to the pellicle have not been resolved in the available corpus [#4].\",\n  \"teleology\": [\n    {\n      \"year\": 2005,\n      \"claim\": \"Establishing whether a Toxoplasma rhomboid could cleave the microneme adhesins that must be shed for invasion identified ROM5 as an active intramembrane protease colocalizing with translocated MIC2 at the posterior pole.\",\n      \"evidence\": \"Cloning and characterization of T. gondii rhomboids with cell-based cleavage assay and IF co-localization of MIC2 during invasion\",\n      \"pmids\": [\"15753289\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Cell-based cleavage and co-localization do not establish that ROM5 is the sheddase responsible in vivo\", \"No genetic loss-of-function test of ROM5 function\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2005,\n      \"claim\": \"Confirming ROM5 was a genuine protease rather than merely a rhomboid homolog, it cleaved the transmembrane domain of the canonical rhomboid substrate Spitz.\",\n      \"evidence\": \"Cell-based heterologous cleavage assay using Drosophila Spitz\",\n      \"pmids\": [\"15913633\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Heterologous substrate does not define physiological substrates\", \"Single method, single lab\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2008,\n      \"claim\": \"Determining where ROM5 acts, it was confirmed to reside at the pellicle, though the trafficking determinants specifying this localization were not resolved for ROM5.\",\n      \"evidence\": \"Immunofluorescence localization plus domain-exchange chimeras and site-directed mutagenesis of N-terminal cytosolic domains\",\n      \"pmids\": [\"18346213\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"ROM4/ROM5-specific pellicle sorting determinants remain unidentified\", \"Localization does not establish substrate access or function\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Directly testing ROM5's in vivo requirement via knockouts overturned its assumed role as the primary adhesin sheddase, revealing ROM4 as the dominant adhesin-processing rhomboid and ROM5 as negligible for invasion.\",\n      \"evidence\": \"Single, double, and triple knockouts with adhesin shedding, gliding, invasion, and moving-junction assays\",\n      \"pmids\": [\"25336455\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Did not identify a distinct physiological substrate for ROM5\", \"Possible functional redundancy masking ROM5 role not fully dissected\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Resolving what residual function ROM5 retains, ROM5/ROM4 double-knockout analysis showed ROM5 mediates residual intramembrane cleavage of AMA1 and contributes to invasion only when ROM4 is absent.\",\n      \"evidence\": \"CRISPR-Cas9 ROM5 knockout and Cre-recombinase ROM4 knockout with MIC2, MIC6, and AMA1 shedding assays and invasion assays\",\n      \"pmids\": [\"25846828\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Full physiological substrate repertoire of ROM5 not defined\", \"Molecular basis of ROM4/ROM5 substrate discrimination unknown\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The determinants that restrict ROM5 to the posterior pole and the basis for its substrate preference for AMA-family adhesins over ROM4-preferred substrates remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"ROM5-specific pellicle/posterior-pole sorting determinants unidentified\", \"Structural or biochemical basis of ROM5 versus ROM4 substrate selectivity unknown\", \"No structural model of ROM5\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0004252\", \"supporting_discovery_ids\": [0, 1, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005886\", \"supporting_discovery_ids\": [0, 4], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0044409\", \"supporting_discovery_ids\": [0, 2, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"Cleaves the transmembrane domains of adhesins; residual physiological substrate is AMA1 and other AMA-family members, detectable only in the absence of ROM4 [#3].\",\n      \"Cleaves the heterologous rhomboid substrate Drosophila Spitz, confirming bona fide intramembrane protease activity [#1].\",\n      \"Concentrates at the posterior pole of the tachyzoite pellicle, colocalizing with translocated MIC2 during invasion [#0].\",\n      \"ROM4, not ROM5, is the dominant adhesin-processing rhomboid during tachyzoite invasion [#2, #3].\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_294690","name":"ROM5","product":"rhomboid protease ROM5","uniprot_acc":"A0A125YG69","chromosome":"TGME49_chrIa","start_pos":1060612},{"strain":"GT1","gene_id":"TGGT1_294690","name":null,"product":"rhomboid protease ROM5","uniprot_acc":null,"chromosome":"TGGT1_chrIa","start_pos":1047083},{"strain":"RH88","gene_id":"TGRH88_019690","name":null,"product":"rhomboid protease ROM5","uniprot_acc":null,"chromosome":"CM023081","start_pos":1067445},{"strain":"VEG","gene_id":"TGVEG_294690","name":null,"product":"rhomboid protease ROM5","uniprot_acc":"A0A0F7UNN4","chromosome":"TGVEG_chrIa","start_pos":1070757}]}