{"gene":"GPHRB","run_date":"2026-06-10T01:55:21","timeline":{"discoveries":[{"year":2021,"finding":"GPR89B (GPHRB) physically interacts with nucleotide sugar transporters SLC35A2, SLC35A3, and SLC35A4, as demonstrated by co-immunoprecipitation and confirmed in vitro using the NanoBiT split-luciferase complementation assay, suggesting a role in regulating glycosylation through ion homeostasis.","method":"Co-immunoprecipitation pull-down followed by mass spectrometry; NanoBiT split-luciferase in vitro confirmation","journal":"Journal of proteomics","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — reciprocal interaction confirmed with two orthogonal methods (co-IP/MS and NanoBiT), single lab","pmids":["34242836"],"is_preprint":false},{"year":2020,"finding":"RABL3 strongly associates with and stabilizes GPR89 (GPHRB), and an ENU-induced mutation in Gpr89 (explorer allele) phenocopies Rabl3 knockout in lymphoid development, placing GPR89 as a downstream effector of RABL3 in lymphopoiesis.","method":"Genetic epistasis (ENU mutagenesis phenocopy), co-immunoprecipitation/association assay","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic epistasis combined with physical association assay, single lab, two orthogonal approaches","pmids":["32220963"],"is_preprint":false},{"year":2025,"finding":"GPR89B (GPHRB) overexpression in zebrafish larvae (via introduction of human GPR89B mRNA into zebrafish knockouts of the ortholog) results in dosage-mediated brain expansion, establishing a direct functional role for GPR89B in brain size regulation.","method":"Zebrafish CRISPR knockout of ortholog combined with humanization by mRNA injection; brain size phenotypic readout","journal":"Cell","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — clean loss-of-function with humanization rescue, defined cellular phenotype, single study","pmids":["40695280"],"is_preprint":false},{"year":2025,"finding":"Structural bioinformatic modeling places GPR89 (GPHRB) within the solute carrier (SLC) superfamily / LIMR protein superfamily, revealing a unique intracellular helix hairpin and a conserved transmembrane core compatible with transporter activity rather than GPCR signaling.","method":"Structural modeling (AlphaFold-based), phylogenetic reconstruction, genomic synteny analysis","journal":"Computational and structural biotechnology journal","confidence":"Low","confidence_rationale":"Tier 4 / Weak — computational/bioinformatic prediction only, no experimental validation of transport activity","pmids":["41282416"],"is_preprint":false},{"year":2014,"finding":"The Dictyostelium discoideum GPHR (GPR89) ortholog localizes to the endoplasmic reticulum and Golgi apparatus, and its loss results in developmental defects (abnormal slugs and fruiting bodies) and altered expression of development-specific markers, without detectable impairment of ER/Golgi membrane protein processing or glycosylation.","method":"Gene knockout (null mutant generation), immunofluorescence localization, developmental marker analysis, glycosylation assay","journal":"Eukaryotic cell","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization by immunofluorescence, clean KO with defined developmental phenotype, multiple assays in one study","pmids":["25380752"],"is_preprint":false}],"current_model":"GPHRB (GPR89B/GPHRB) is an orphan transmembrane protein that localizes to the endoplasmic reticulum and Golgi apparatus, where it interacts with nucleotide sugar transporters (SLC35A2/A3/A4) likely linking ion homeostasis to glycosylation regulation; it is stabilized by the small GTPase RABL3 and functions downstream of it in lymphoid development; structurally it belongs to the solute carrier/LIMR superfamily with a conserved transmembrane core compatible with transport activity; and in humans it contributes to dosage-mediated brain expansion as evidenced by zebrafish humanization experiments."},"narrative":{"mechanistic_narrative":"GPHRB (GPR89B) is an orphan multi-pass transmembrane protein that operates within the endomembrane system, where it links nucleotide-sugar transport machinery to organelle development and cell-size regulation [PMID:34242836, PMID:25380752]. In mammalian cells it physically associates with the nucleotide sugar transporters SLC35A2, SLC35A3, and SLC35A4, an interaction confirmed by co-immunoprecipitation and split-luciferase complementation, positioning GPHRB in the regulation of glycosylation through ion homeostasis [PMID:34242836]. Its stability and function are governed by the small GTPase RABL3: RABL3 binds and stabilizes GPHRB, and a loss-of-function Gpr89 allele phenocopies Rabl3 disruption in lymphoid development, establishing GPHRB as a downstream effector in lymphopoiesis [PMID:32220963]. In the Dictyostelium ortholog, the protein localizes to the endoplasmic reticulum and Golgi, and its loss causes developmental defects without measurable impairment of membrane-protein processing or glycosylation [PMID:25380752]. Humanization of zebrafish ortholog knockouts with human GPR89B mRNA produces dosage-dependent brain expansion, assigning GPHRB a direct role in brain-size regulation [PMID:40695280]. Beyond these findings, the molecular transport activity of GPHRB has not been directly demonstrated in the available corpus.","teleology":[{"year":2014,"claim":"Established the subcellular compartment in which GPHRB acts and tested whether it is required for canonical secretory-pathway functions, by characterizing the Dictyostelium ortholog.","evidence":"Gene knockout, immunofluorescence localization, and glycosylation assays in Dictyostelium discoideum","pmids":["25380752"],"confidence":"Medium","gaps":["No molecular transport substrate identified","Developmental phenotype mechanism not linked to a biochemical activity","Glycosylation unaffected, leaving the functional output undefined"]},{"year":2020,"claim":"Placed GPHRB in a defined regulatory hierarchy by showing it is stabilized by and acts downstream of the GTPase RABL3 in lymphoid development.","evidence":"ENU mutagenesis genetic epistasis (phenocopy) combined with co-immunoprecipitation/association assay in mouse","pmids":["32220963"],"confidence":"Medium","gaps":["Biochemical consequence of RABL3 binding on GPHRB activity unknown","Mechanism connecting GPHRB to lymphopoiesis not resolved","Single lab"]},{"year":2021,"claim":"Identified direct physical partners, connecting GPHRB to nucleotide-sugar transport and a candidate role in glycosylation/ion homeostasis.","evidence":"Co-IP/mass spectrometry with NanoBiT split-luciferase confirmation of SLC35A2/A3/A4 interactions","pmids":["34242836"],"confidence":"Medium","gaps":["Functional consequence of SLC35 binding not demonstrated","Ion homeostasis role inferred, not measured","Single lab"]},{"year":2025,"claim":"Provided direct functional evidence that human GPHRB dosage regulates brain size, via cross-species humanization.","evidence":"Zebrafish CRISPR ortholog knockout rescued with human GPR89B mRNA, scored by brain size","pmids":["40695280"],"confidence":"Medium","gaps":["Molecular pathway linking GPHRB to brain expansion unknown","Cell-type responsible not defined","Single study"]},{"year":2025,"claim":"Reassigned GPHRB structurally from a GPCR to a solute-carrier-like transporter, reframing its likely molecular activity.","evidence":"AlphaFold-based structural modeling, phylogenetics, and genomic synteny analysis","pmids":["41282416"],"confidence":"Low","gaps":["Computational prediction only, transport activity not experimentally validated","No identified transported solute","No experimental structure"]},{"year":null,"claim":"The biochemical activity of GPHRB and the substrate it transports or regulates remain undefined, leaving its molecular function unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No direct demonstration of transport activity","No mechanistic link between SLC35 binding, RABL3 regulation, and the brain-size/developmental phenotypes"]}],"mechanism_profile":{"molecular_activity":[],"localization":[{"term_id":"GO:0005783","term_label":"endoplasmic reticulum","supporting_discovery_ids":[4]},{"term_id":"GO:0005794","term_label":"Golgi apparatus","supporting_discovery_ids":[4]}],"pathway":[],"complexes":[],"partners":["RABL3","SLC35A2","SLC35A3","SLC35A4"],"other_free_text":[]}},"prefetch_data":{"uniprot":{},"depmap":{"release":"DepMap","has_data":false,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/GPHRB"},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/GPHRB","total_profiled":1310},"omim":[],"hpa":{"profiled":true,"resolved_as":"GPR89B","reliability":"Approved","locations":[{"location":"Endoplasmic reticulum","reliability":"Approved"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/GPR89B"},"hgnc":{"alias_symbol":["GPHRB","SH120"],"prev_symbol":["GPR89","GPR89C","LINC02804","GPR89B"]},"alphafold":{},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=GPHRB","jax_strain_url":"https://www.jax.org/strain/search?query=GPHRB"},"sequence":{}},"corpus_meta":[{"pmid":"30503212","id":"PMC_30503212","title":"Oligopeptide Signaling through TbGPR89 Drives Trypanosome Quorum Sensing.","date":"2018","source":"Cell","url":"https://pubmed.ncbi.nlm.nih.gov/30503212","citation_count":96,"is_preprint":false},{"pmid":"32554864","id":"PMC_32554864","title":"Serum exosomal long noncoding RNAs lnc-FAM72D-3 and lnc-EPC1-4 as diagnostic biomarkers for hepatocellular carcinoma.","date":"2020","source":"Aging","url":"https://pubmed.ncbi.nlm.nih.gov/32554864","citation_count":52,"is_preprint":false},{"pmid":"26282200","id":"PMC_26282200","title":"Different roles of GPR120 and GPR40 in the acquisition of malignant properties in pancreatic cancer cells.","date":"2015","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/26282200","citation_count":38,"is_preprint":false},{"pmid":"7869107","id":"PMC_7869107","title":"Functional expression of Shaker K+ channels in cultured Drosophila \"giant\" neurons derived from Sh cDNA transformants: distinct properties, distribution, and turnover.","date":"1995","source":"The Journal of neuroscience : the official journal of the Society for Neuroscience","url":"https://pubmed.ncbi.nlm.nih.gov/7869107","citation_count":34,"is_preprint":false},{"pmid":"32220963","id":"PMC_32220963","title":"Genetic and structural studies of RABL3 reveal an essential role in lymphoid development and function.","date":"2020","source":"Proceedings of the National Academy of Sciences of the United States of America","url":"https://pubmed.ncbi.nlm.nih.gov/32220963","citation_count":13,"is_preprint":false},{"pmid":"34242836","id":"PMC_34242836","title":"Identification of novel potential interaction partners of UDP-galactose (SLC35A2), UDP-N-acetylglucosamine (SLC35A3) and an orphan (SLC35A4) nucleotide sugar transporters.","date":"2021","source":"Journal of proteomics","url":"https://pubmed.ncbi.nlm.nih.gov/34242836","citation_count":13,"is_preprint":false},{"pmid":"40695280","id":"PMC_40695280","title":"Human-specific gene expansions contribute to brain evolution.","date":"2025","source":"Cell","url":"https://pubmed.ncbi.nlm.nih.gov/40695280","citation_count":12,"is_preprint":false},{"pmid":"25380752","id":"PMC_25380752","title":"The Dictyostelium discoideum GPHR ortholog is an endoplasmic reticulum and Golgi protein with roles during development.","date":"2014","source":"Eukaryotic cell","url":"https://pubmed.ncbi.nlm.nih.gov/25380752","citation_count":11,"is_preprint":false},{"pmid":"31759543","id":"PMC_31759543","title":"Detection of a familial 1q21.1 microdeletion and concomitant CHD1L mutation in a fetus with oligohydramnios and bilateral renal dysplasia on prenatal ultrasound.","date":"2019","source":"Taiwanese journal of obstetrics & gynecology","url":"https://pubmed.ncbi.nlm.nih.gov/31759543","citation_count":8,"is_preprint":false},{"pmid":"30342663","id":"PMC_30342663","title":"Prenatal diagnosis of a familial 1q21.1-q21.2 microdeletion in a fetus with polydactyly of left foot on prenatal ultrasound.","date":"2018","source":"Taiwanese journal of obstetrics & gynecology","url":"https://pubmed.ncbi.nlm.nih.gov/30342663","citation_count":8,"is_preprint":false},{"pmid":"35574218","id":"PMC_35574218","title":"Proteomic analysis reveals dual requirement for Grb2 and PLCγ1 interactions for BCR-FGFR1-Driven 8p11 cell proliferation.","date":"2022","source":"Oncotarget","url":"https://pubmed.ncbi.nlm.nih.gov/35574218","citation_count":5,"is_preprint":false},{"pmid":"30322321","id":"PMC_30322321","title":"Inter-relationships among physical dimensions, distal-proximal rank orders, and basal GCaMP fluorescence levels in Ca2+ imaging of functionally distinct synaptic boutons at Drosophila neuromuscular junctions.","date":"2018","source":"Journal of neurogenetics","url":"https://pubmed.ncbi.nlm.nih.gov/30322321","citation_count":5,"is_preprint":false},{"pmid":"39386494","id":"PMC_39386494","title":"Human-specific gene expansions contribute to brain evolution.","date":"2025","source":"bioRxiv : the preprint server for biology","url":"https://pubmed.ncbi.nlm.nih.gov/39386494","citation_count":3,"is_preprint":false},{"pmid":"41282416","id":"PMC_41282416","title":"Evolutionary and structural bioinformatics identifies GPR89 as a conserved member of the LIMR protein superfamily.","date":"2025","source":"Computational and structural biotechnology journal","url":"https://pubmed.ncbi.nlm.nih.gov/41282416","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2025.08.04.668498","title":"Evolutionary and Structural Bioinformatics Reveal GPR89 as a Conserved Solute Carrier Transporter","date":"2025-08-06","source":"bioRxiv","url":"https://doi.org/10.1101/2025.08.04.668498","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":9573,"output_tokens":1250,"usd":0.023734,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7887,"output_tokens":1868,"usd":0.043068,"stage2_stop_reason":"end_turn"},"total_usd":0.066802,"stage1_batch_id":"msgbatch_01DUPACZi7AAWwuZiUjseQF4","stage2_batch_id":"msgbatch_018yt7chE3f48PEFtDwtj6AE","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2021,\n      \"finding\": \"GPR89B (GPHRB) physically interacts with nucleotide sugar transporters SLC35A2, SLC35A3, and SLC35A4, as demonstrated by co-immunoprecipitation and confirmed in vitro using the NanoBiT split-luciferase complementation assay, suggesting a role in regulating glycosylation through ion homeostasis.\",\n      \"method\": \"Co-immunoprecipitation pull-down followed by mass spectrometry; NanoBiT split-luciferase in vitro confirmation\",\n      \"journal\": \"Journal of proteomics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — reciprocal interaction confirmed with two orthogonal methods (co-IP/MS and NanoBiT), single lab\",\n      \"pmids\": [\"34242836\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"RABL3 strongly associates with and stabilizes GPR89 (GPHRB), and an ENU-induced mutation in Gpr89 (explorer allele) phenocopies Rabl3 knockout in lymphoid development, placing GPR89 as a downstream effector of RABL3 in lymphopoiesis.\",\n      \"method\": \"Genetic epistasis (ENU mutagenesis phenocopy), co-immunoprecipitation/association assay\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic epistasis combined with physical association assay, single lab, two orthogonal approaches\",\n      \"pmids\": [\"32220963\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"GPR89B (GPHRB) overexpression in zebrafish larvae (via introduction of human GPR89B mRNA into zebrafish knockouts of the ortholog) results in dosage-mediated brain expansion, establishing a direct functional role for GPR89B in brain size regulation.\",\n      \"method\": \"Zebrafish CRISPR knockout of ortholog combined with humanization by mRNA injection; brain size phenotypic readout\",\n      \"journal\": \"Cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — clean loss-of-function with humanization rescue, defined cellular phenotype, single study\",\n      \"pmids\": [\"40695280\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Structural bioinformatic modeling places GPR89 (GPHRB) within the solute carrier (SLC) superfamily / LIMR protein superfamily, revealing a unique intracellular helix hairpin and a conserved transmembrane core compatible with transporter activity rather than GPCR signaling.\",\n      \"method\": \"Structural modeling (AlphaFold-based), phylogenetic reconstruction, genomic synteny analysis\",\n      \"journal\": \"Computational and structural biotechnology journal\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 4 / Weak — computational/bioinformatic prediction only, no experimental validation of transport activity\",\n      \"pmids\": [\"41282416\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"The Dictyostelium discoideum GPHR (GPR89) ortholog localizes to the endoplasmic reticulum and Golgi apparatus, and its loss results in developmental defects (abnormal slugs and fruiting bodies) and altered expression of development-specific markers, without detectable impairment of ER/Golgi membrane protein processing or glycosylation.\",\n      \"method\": \"Gene knockout (null mutant generation), immunofluorescence localization, developmental marker analysis, glycosylation assay\",\n      \"journal\": \"Eukaryotic cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization by immunofluorescence, clean KO with defined developmental phenotype, multiple assays in one study\",\n      \"pmids\": [\"25380752\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"GPHRB (GPR89B/GPHRB) is an orphan transmembrane protein that localizes to the endoplasmic reticulum and Golgi apparatus, where it interacts with nucleotide sugar transporters (SLC35A2/A3/A4) likely linking ion homeostasis to glycosylation regulation; it is stabilized by the small GTPase RABL3 and functions downstream of it in lymphoid development; structurally it belongs to the solute carrier/LIMR superfamily with a conserved transmembrane core compatible with transport activity; and in humans it contributes to dosage-mediated brain expansion as evidenced by zebrafish humanization experiments.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"GPHRB (GPR89B) is an orphan multi-pass transmembrane protein that operates within the endomembrane system, where it links nucleotide-sugar transport machinery to organelle development and cell-size regulation [#0, #4]. In mammalian cells it physically associates with the nucleotide sugar transporters SLC35A2, SLC35A3, and SLC35A4, an interaction confirmed by co-immunoprecipitation and split-luciferase complementation, positioning GPHRB in the regulation of glycosylation through ion homeostasis [#0]. Its stability and function are governed by the small GTPase RABL3: RABL3 binds and stabilizes GPHRB, and a loss-of-function Gpr89 allele phenocopies Rabl3 disruption in lymphoid development, establishing GPHRB as a downstream effector in lymphopoiesis [#1]. In the Dictyostelium ortholog, the protein localizes to the endoplasmic reticulum and Golgi, and its loss causes developmental defects without measurable impairment of membrane-protein processing or glycosylation [#4]. Humanization of zebrafish ortholog knockouts with human GPR89B mRNA produces dosage-dependent brain expansion, assigning GPHRB a direct role in brain-size regulation [#2]. Beyond these findings, the molecular transport activity of GPHRB has not been directly demonstrated in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Established the subcellular compartment in which GPHRB acts and tested whether it is required for canonical secretory-pathway functions, by characterizing the Dictyostelium ortholog.\",\n      \"evidence\": \"Gene knockout, immunofluorescence localization, and glycosylation assays in Dictyostelium discoideum\",\n      \"pmids\": [\"25380752\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No molecular transport substrate identified\", \"Developmental phenotype mechanism not linked to a biochemical activity\", \"Glycosylation unaffected, leaving the functional output undefined\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Placed GPHRB in a defined regulatory hierarchy by showing it is stabilized by and acts downstream of the GTPase RABL3 in lymphoid development.\",\n      \"evidence\": \"ENU mutagenesis genetic epistasis (phenocopy) combined with co-immunoprecipitation/association assay in mouse\",\n      \"pmids\": [\"32220963\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Biochemical consequence of RABL3 binding on GPHRB activity unknown\", \"Mechanism connecting GPHRB to lymphopoiesis not resolved\", \"Single lab\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Identified direct physical partners, connecting GPHRB to nucleotide-sugar transport and a candidate role in glycosylation/ion homeostasis.\",\n      \"evidence\": \"Co-IP/mass spectrometry with NanoBiT split-luciferase confirmation of SLC35A2/A3/A4 interactions\",\n      \"pmids\": [\"34242836\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Functional consequence of SLC35 binding not demonstrated\", \"Ion homeostasis role inferred, not measured\", \"Single lab\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Provided direct functional evidence that human GPHRB dosage regulates brain size, via cross-species humanization.\",\n      \"evidence\": \"Zebrafish CRISPR ortholog knockout rescued with human GPR89B mRNA, scored by brain size\",\n      \"pmids\": [\"40695280\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Molecular pathway linking GPHRB to brain expansion unknown\", \"Cell-type responsible not defined\", \"Single study\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Reassigned GPHRB structurally from a GPCR to a solute-carrier-like transporter, reframing its likely molecular activity.\",\n      \"evidence\": \"AlphaFold-based structural modeling, phylogenetics, and genomic synteny analysis\",\n      \"pmids\": [\"41282416\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Computational prediction only, transport activity not experimentally validated\", \"No identified transported solute\", \"No experimental structure\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The biochemical activity of GPHRB and the substrate it transports or regulates remain undefined, leaving its molecular function unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No direct demonstration of transport activity\", \"No mechanistic link between SLC35 binding, RABL3 regulation, and the brain-size/developmental phenotypes\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [],\n    \"localization\": [\n      {\"term_id\": \"GO:0005783\", \"supporting_discovery_ids\": [4]},\n      {\"term_id\": \"GO:0005794\", \"supporting_discovery_ids\": [4]}\n    ],\n    \"pathway\": [],\n    \"complexes\": [],\n    \"partners\": [\"RABL3\", \"SLC35A2\", \"SLC35A3\", \"SLC35A4\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"faith_supported":5,"faith_total":5,"faith_pct":100.0}}