{"gene":"EMC7","run_date":"2026-06-09T23:54:43","timeline":{"discoveries":[{"year":2020,"finding":"Cryo-EM structure of the yeast ER membrane complex (EMC) revealed that Emc7 is one of eight subunits (Emc1-6, Emc7, Emc10) forming the complex, with a large lumenal region, smaller cytosolic region, and a transmembrane region. The complex contains a five-TMH fold centered around Emc3 resembling the prokaryotic YidC insertase, delineating a hydrophilic client protein pocket required for TMH insertion into the ER membrane.","method":"Cryo-electron microscopy structure determination with mutational studies validating functional requirements (Emc4 flexibility and hydrophilicity of client pocket)","journal":"Nature","confidence":"High","confidence_rationale":"Tier 1 / Strong — cryo-EM structure with functional mutagenesis validation, published in high-impact journal","pmids":["32494008"],"is_preprint":false},{"year":2020,"finding":"EMC7 (together with EMC4) functions as a molecular tether connecting late endosomes (LE) to the ER by engaging LE-associated Rab7, thereby promoting LE-to-ER targeting of SV40 polyomavirus during viral entry. EMC7 also binds the ER-resident fusion machinery component syntaxin18, which is required for SV40 arrival at the ER.","method":"Functional knockdown experiments with SV40 infection assays, co-immunoprecipitation of EMC7 with Rab7 and syntaxin18, organelle transport assays","journal":"Nature Communications","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — co-IP binding partners identified and KD phenotype established, single lab but multiple orthogonal approaches","pmids":["32111841"],"is_preprint":false},{"year":2011,"finding":"C15orf24 (EMC7) protein localizes to the murine postsynaptic sarcolemma of the neuromuscular junction, as demonstrated by antibody staining of murine NMJ sections.","method":"Antibody generation against C15orf24 and immunolocalization at murine neuromuscular junction","journal":"Marine genomics","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single localization experiment with no functional consequence established, single lab, single method","pmids":["21429463"],"is_preprint":false},{"year":2013,"finding":"UPF0480 protein C15orf24 (EMC7) was identified as a binding partner of the Na+/Mg2+ exchanger SLC41A1 in a split-ubiquitin yeast two-hybrid assay, suggesting a transient interaction in the ER context.","method":"Split-ubiquitin yeast two-hybrid assay","journal":"Magnesium research","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single method (yeast two-hybrid), not confirmed by mass spectrometry, interaction described as transient","pmids":["23823179"],"is_preprint":false}],"current_model":"EMC7 is a subunit of the conserved ER membrane complex (EMC), which functions as a transmembrane-domain insertase structurally resembling the prokaryotic YidC insertase; additionally, EMC7 acts as a molecular tether at LE-ER membrane contact sites by binding Rab7 and syntaxin18 to facilitate inter-organelle cargo transport."},"narrative":{"mechanistic_narrative":"EMC7 is a constitutive subunit of the conserved ER membrane complex (EMC), an eight-subunit transmembrane-domain insertase of the endoplasmic reticulum [PMID:32494008]. Within the complex, EMC7 contributes to an assembly centered on a five-TMH fold resembling the prokaryotic YidC insertase that forms a hydrophilic client pocket for inserting transmembrane helices into the ER membrane [PMID:32494008]. Beyond its structural role in the EMC, EMC7 acts as a molecular tether at late endosome–ER membrane contact sites: it engages LE-associated Rab7 and binds the ER-resident fusion machinery component syntaxin18, thereby promoting LE-to-ER cargo targeting, as demonstrated for the entry of SV40 polyomavirus [PMID:32111841]. Beyond these roles, the broader functional repertoire of EMC7 has not been characterized in the available corpus.","teleology":[{"year":2011,"claim":"An early question was where the uncharacterized C15orf24 (EMC7) protein resides in tissue; immunolocalization placed it at the postsynaptic sarcolemma of the neuromuscular junction, giving a first anatomical foothold.","evidence":"Antibody generation and immunolocalization at murine neuromuscular junction sections","pmids":["21429463"],"confidence":"Low","gaps":["Single localization experiment with no functional consequence established","No molecular activity or interaction partner defined","Does not connect the protein to any pathway"]},{"year":2013,"claim":"To find candidate interactors, a split-ubiquitin screen identified the Na+/Mg2+ exchanger SLC41A1 as a transient ER-context binding partner of EMC7, hinting at an ER membrane role.","evidence":"Split-ubiquitin yeast two-hybrid assay","pmids":["23823179"],"confidence":"Low","gaps":["Single method (yeast two-hybrid) not confirmed by mass spectrometry or reciprocal co-IP","Interaction described as transient, functional significance unclear","Does not establish whether the interaction reflects EMC client handling"]},{"year":2020,"claim":"The molecular function of EMC7 was resolved by placing it within the EMC: cryo-EM showed it is one of eight subunits of a transmembrane-domain insertase whose YidC-like fold creates a hydrophilic pocket for TMH insertion into the ER membrane.","evidence":"Cryo-EM structure of the yeast EMC with mutational validation of client-pocket hydrophilicity and Emc4 flexibility","pmids":["32494008"],"confidence":"High","gaps":["Structure does not define the specific contribution of EMC7 to client insertion","Substrate repertoire handled with EMC7 participation not enumerated","Human EMC7 inferred from yeast complex architecture"]},{"year":2020,"claim":"A distinct, EMC-independent role emerged when EMC7 was shown to tether late endosomes to the ER by binding Rab7 and syntaxin18, enabling LE-to-ER cargo transport exploited during SV40 entry.","evidence":"Knockdown with SV40 infection assays, co-immunoprecipitation of EMC7 with Rab7 and syntaxin18, and organelle transport assays","pmids":["32111841"],"confidence":"Medium","gaps":["Co-IP partners identified in a single lab without reciprocal structural validation of the tether","Whether tethering activity is separable from EMC subunit function is unresolved","Generality beyond SV40 cargo not established"]},{"year":null,"claim":"How the EMC insertase activity of EMC7 relates mechanistically to its endosome-ER tethering role, and whether both functions operate simultaneously in the same cells, remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of the EMC7-Rab7-syntaxin18 tether","Native client substrates of the human EMC requiring EMC7 not defined","Functional significance of NMJ localization and SLC41A1 interaction unintegrated"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140096","term_label":"catalytic activity, acting on a protein","supporting_discovery_ids":[0]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[1]}],"localization":[{"term_id":"GO:0005783","term_label":"endoplasmic reticulum","supporting_discovery_ids":[0,1]},{"term_id":"GO:0005768","term_label":"endosome","supporting_discovery_ids":[1]}],"pathway":[{"term_id":"R-HSA-392499","term_label":"Metabolism of proteins","supporting_discovery_ids":[0]},{"term_id":"R-HSA-5653656","term_label":"Vesicle-mediated transport","supporting_discovery_ids":[1]}],"complexes":["ER membrane complex (EMC)"],"partners":["EMC4","RAB7","STX18","SLC41A1"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q9NPA0","full_name":"Endoplasmic reticulum membrane protein complex subunit 7","aliases":["ER membrane protein complex subunit 7"],"length_aa":242,"mass_kda":26.5,"function":"Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:29242231, PubMed:29809151, PubMed:30415835, PubMed:32439656, PubMed:32459176). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:29242231, PubMed:29809151, PubMed:30415835). Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:29809151, PubMed:30415835). It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes (PubMed:29242231, PubMed:29809151). By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors (PubMed:30415835). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable)","subcellular_location":"Endoplasmic reticulum membrane","url":"https://www.uniprot.org/uniprotkb/Q9NPA0/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/EMC7","classification":"Common Essential","n_dependent_lines":892,"n_total_lines":1208,"dependency_fraction":0.7384105960264901},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000134153","cell_line_id":"CID001792","localizations":[{"compartment":"er","grade":3}],"interactors":[{"gene":"EMC1","stoichiometry":10.0},{"gene":"EMC2","stoichiometry":10.0},{"gene":"EMC3","stoichiometry":10.0},{"gene":"EMC4","stoichiometry":10.0},{"gene":"EMC8","stoichiometry":10.0},{"gene":"CCDC47","stoichiometry":10.0},{"gene":"EMC9","stoichiometry":10.0},{"gene":"CANX","stoichiometry":0.2},{"gene":"EMC10","stoichiometry":0.2},{"gene":"GNA12","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/target/CID001792","total_profiled":1310},"omim":[{"mim_id":"620631","title":"ENDOPLASMIC RETICULUM MEMBRANE PROTEIN COMPLEX, SUBUNIT 7; EMC7","url":"https://www.omim.org/entry/620631"},{"mim_id":"620273","title":"ENDOPLASMIC RETICULUM MEMBRANE PROTEIN COMPLEX, SUBUNIT 3; EMC3","url":"https://www.omim.org/entry/620273"},{"mim_id":"620261","title":"ENDOPLASMIC RETICULUM MEMBRANE PROTEIN COMPLEX, SUBUNIT 6; EMC6","url":"https://www.omim.org/entry/620261"},{"mim_id":"616245","title":"ENDOPLASMIC RETICULUM MEMBRANE PROTEIN COMPLEX, SUBUNIT 4; EMC4","url":"https://www.omim.org/entry/616245"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"","locations":[],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/EMC7"},"hgnc":{"alias_symbol":["C11orf3"],"prev_symbol":["C15orf24"]},"alphafold":{"accession":"Q9NPA0","domains":[{"cath_id":"2.60.40","chopping":"44-143","consensus_level":"high","plddt":90.9809,"start":44,"end":143},{"cath_id":"4.10.220","chopping":"152-201","consensus_level":"medium","plddt":75.9596,"start":152,"end":201}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9NPA0","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9NPA0-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9NPA0-F1-predicted_aligned_error_v6.png","plddt_mean":72.94},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=EMC7","jax_strain_url":"https://www.jax.org/strain/search?query=EMC7"},"sequence":{"accession":"Q9NPA0","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9NPA0.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9NPA0/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9NPA0"}},"corpus_meta":[{"pmid":"32494008","id":"PMC_32494008","title":"Structure of the ER membrane complex, a transmembrane-domain insertase.","date":"2020","source":"Nature","url":"https://pubmed.ncbi.nlm.nih.gov/32494008","citation_count":110,"is_preprint":false},{"pmid":"26512320","id":"PMC_26512320","title":"The ubiquitous and ancient ER membrane protein complex (EMC): tether or not?","date":"2015","source":"F1000Research","url":"https://pubmed.ncbi.nlm.nih.gov/26512320","citation_count":76,"is_preprint":false},{"pmid":"33739783","id":"PMC_33739783","title":"NUT Is a Specific Immunohistochemical Marker for the Diagnosis of YAP1-NUTM1-rearranged Cutaneous Poroid Neoplasms.","date":"2021","source":"The American journal of surgical pathology","url":"https://pubmed.ncbi.nlm.nih.gov/33739783","citation_count":60,"is_preprint":false},{"pmid":"32111841","id":"PMC_32111841","title":"Selective EMC subunits act as molecular tethers of intracellular organelles exploited during viral entry.","date":"2020","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/32111841","citation_count":22,"is_preprint":false},{"pmid":"26536597","id":"PMC_26536597","title":"The Orthology Clause in the Next Generation Sequencing Era: Novel Reference Genes Identified by RNA-seq in Humans Improve Normalization of Neonatal Equine Ovary RT-qPCR Data.","date":"2015","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/26536597","citation_count":18,"is_preprint":false},{"pmid":"23823179","id":"PMC_23823179","title":"Nature of SLC41A1 complexes: report on the split-ubiquitin yeast two hybrid assay.","date":"2013","source":"Magnesium research","url":"https://pubmed.ncbi.nlm.nih.gov/23823179","citation_count":8,"is_preprint":false},{"pmid":"38308464","id":"PMC_38308464","title":"Licochalcone A induces endoplasmic reticulum stress-mediated apoptosis of endometrial cancer cells via upregulation of GRP78 expression.","date":"2024","source":"Environmental toxicology","url":"https://pubmed.ncbi.nlm.nih.gov/38308464","citation_count":8,"is_preprint":false},{"pmid":"21429463","id":"PMC_21429463","title":"Evolution and comparative genomics of subcellular specializations: EST sequencing of Torpedo electric organ.","date":"2011","source":"Marine genomics","url":"https://pubmed.ncbi.nlm.nih.gov/21429463","citation_count":5,"is_preprint":false},{"pmid":"39209956","id":"PMC_39209956","title":"Identification of genetic variants associated with clinical features of sickle cell disease.","date":"2024","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/39209956","citation_count":4,"is_preprint":false},{"pmid":"39955304","id":"PMC_39955304","title":"Leclercia barmai sp. nov., isolated from worm castings of Eisenia fetida, is a urease-positive, 3-nitropropionic acid and glycerol-consuming bacterium.","date":"2025","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/39955304","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":7267,"output_tokens":985,"usd":0.018288,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7455,"output_tokens":1913,"usd":0.04255,"stage2_stop_reason":"end_turn"},"total_usd":0.060838,"stage1_batch_id":"msgbatch_01AsR7g8dGTEiEw9U83bJeWn","stage2_batch_id":"msgbatch_01YV5ZyxtFNUZEjxRcpd9jzb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2020,\n      \"finding\": \"Cryo-EM structure of the yeast ER membrane complex (EMC) revealed that Emc7 is one of eight subunits (Emc1-6, Emc7, Emc10) forming the complex, with a large lumenal region, smaller cytosolic region, and a transmembrane region. The complex contains a five-TMH fold centered around Emc3 resembling the prokaryotic YidC insertase, delineating a hydrophilic client protein pocket required for TMH insertion into the ER membrane.\",\n      \"method\": \"Cryo-electron microscopy structure determination with mutational studies validating functional requirements (Emc4 flexibility and hydrophilicity of client pocket)\",\n      \"journal\": \"Nature\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — cryo-EM structure with functional mutagenesis validation, published in high-impact journal\",\n      \"pmids\": [\"32494008\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"EMC7 (together with EMC4) functions as a molecular tether connecting late endosomes (LE) to the ER by engaging LE-associated Rab7, thereby promoting LE-to-ER targeting of SV40 polyomavirus during viral entry. EMC7 also binds the ER-resident fusion machinery component syntaxin18, which is required for SV40 arrival at the ER.\",\n      \"method\": \"Functional knockdown experiments with SV40 infection assays, co-immunoprecipitation of EMC7 with Rab7 and syntaxin18, organelle transport assays\",\n      \"journal\": \"Nature Communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — co-IP binding partners identified and KD phenotype established, single lab but multiple orthogonal approaches\",\n      \"pmids\": [\"32111841\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"C15orf24 (EMC7) protein localizes to the murine postsynaptic sarcolemma of the neuromuscular junction, as demonstrated by antibody staining of murine NMJ sections.\",\n      \"method\": \"Antibody generation against C15orf24 and immunolocalization at murine neuromuscular junction\",\n      \"journal\": \"Marine genomics\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single localization experiment with no functional consequence established, single lab, single method\",\n      \"pmids\": [\"21429463\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"UPF0480 protein C15orf24 (EMC7) was identified as a binding partner of the Na+/Mg2+ exchanger SLC41A1 in a split-ubiquitin yeast two-hybrid assay, suggesting a transient interaction in the ER context.\",\n      \"method\": \"Split-ubiquitin yeast two-hybrid assay\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single method (yeast two-hybrid), not confirmed by mass spectrometry, interaction described as transient\",\n      \"confidence\": \"Low\",\n      \"journal\": \"Magnesium research\",\n      \"pmids\": [\"23823179\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"EMC7 is a subunit of the conserved ER membrane complex (EMC), which functions as a transmembrane-domain insertase structurally resembling the prokaryotic YidC insertase; additionally, EMC7 acts as a molecular tether at LE-ER membrane contact sites by binding Rab7 and syntaxin18 to facilitate inter-organelle cargo transport.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"EMC7 is a constitutive subunit of the conserved ER membrane complex (EMC), an eight-subunit transmembrane-domain insertase of the endoplasmic reticulum [#0]. Within the complex, EMC7 contributes to an assembly centered on a five-TMH fold resembling the prokaryotic YidC insertase that forms a hydrophilic client pocket for inserting transmembrane helices into the ER membrane [#0]. Beyond its structural role in the EMC, EMC7 acts as a molecular tether at late endosome–ER membrane contact sites: it engages LE-associated Rab7 and binds the ER-resident fusion machinery component syntaxin18, thereby promoting LE-to-ER cargo targeting, as demonstrated for the entry of SV40 polyomavirus [#1]. Beyond these roles, the broader functional repertoire of EMC7 has not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2011,\n      \"claim\": \"An early question was where the uncharacterized C15orf24 (EMC7) protein resides in tissue; immunolocalization placed it at the postsynaptic sarcolemma of the neuromuscular junction, giving a first anatomical foothold.\",\n      \"evidence\": \"Antibody generation and immunolocalization at murine neuromuscular junction sections\",\n      \"pmids\": [\"21429463\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Single localization experiment with no functional consequence established\",\n        \"No molecular activity or interaction partner defined\",\n        \"Does not connect the protein to any pathway\"\n      ]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"To find candidate interactors, a split-ubiquitin screen identified the Na+/Mg2+ exchanger SLC41A1 as a transient ER-context binding partner of EMC7, hinting at an ER membrane role.\",\n      \"evidence\": \"Split-ubiquitin yeast two-hybrid assay\",\n      \"pmids\": [\"23823179\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Single method (yeast two-hybrid) not confirmed by mass spectrometry or reciprocal co-IP\",\n        \"Interaction described as transient, functional significance unclear\",\n        \"Does not establish whether the interaction reflects EMC client handling\"\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"The molecular function of EMC7 was resolved by placing it within the EMC: cryo-EM showed it is one of eight subunits of a transmembrane-domain insertase whose YidC-like fold creates a hydrophilic pocket for TMH insertion into the ER membrane.\",\n      \"evidence\": \"Cryo-EM structure of the yeast EMC with mutational validation of client-pocket hydrophilicity and Emc4 flexibility\",\n      \"pmids\": [\"32494008\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structure does not define the specific contribution of EMC7 to client insertion\",\n        \"Substrate repertoire handled with EMC7 participation not enumerated\",\n        \"Human EMC7 inferred from yeast complex architecture\"\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"A distinct, EMC-independent role emerged when EMC7 was shown to tether late endosomes to the ER by binding Rab7 and syntaxin18, enabling LE-to-ER cargo transport exploited during SV40 entry.\",\n      \"evidence\": \"Knockdown with SV40 infection assays, co-immunoprecipitation of EMC7 with Rab7 and syntaxin18, and organelle transport assays\",\n      \"pmids\": [\"32111841\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Co-IP partners identified in a single lab without reciprocal structural validation of the tether\",\n        \"Whether tethering activity is separable from EMC subunit function is unresolved\",\n        \"Generality beyond SV40 cargo not established\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How the EMC insertase activity of EMC7 relates mechanistically to its endosome-ER tethering role, and whether both functions operate simultaneously in the same cells, remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No structural model of the EMC7-Rab7-syntaxin18 tether\",\n        \"Native client substrates of the human EMC requiring EMC7 not defined\",\n        \"Functional significance of NMJ localization and SLC41A1 interaction unintegrated\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140096\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005783\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0005768\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-392499\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"R-HSA-5653656\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"complexes\": [\"ER membrane complex (EMC)\"],\n    \"partners\": [\"EMC4\", \"RAB7\", \"STX18\", \"SLC41A1\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":3,"faith_total":3,"faith_pct":100.0}}