{"gene":"SLC37A3","run_date":"2026-06-10T07:46:33","timeline":{"discoveries":[{"year":2018,"finding":"SLC37A3 forms a complex with ATRAID (all-trans retinoic acid-induced differentiation factor) and both proteins localize to lysosomes. SLC37A3 is required for releasing nitrogen-containing bisphosphonates (N-BPs) that have trafficked to lysosomes via fluid-phase endocytosis into the cytosol, thereby enabling N-BPs to reach their cytosolic target (the mevalonate pathway).","method":"CRISPRi genome-wide screen, co-localization, complex identification, functional rescue assays","journal":"eLife","confidence":"High","confidence_rationale":"Tier 2 / Strong — genome-wide CRISPRi screen identified SLC37A3, validated by complex formation with ATRAID, lysosomal localization, and functional N-BP transport assays; multiple orthogonal methods in a single rigorous study","pmids":["29745899"],"is_preprint":false},{"year":2014,"finding":"SLC37A3 is an endoplasmic reticulum-associated protein belonging to the sugar-phosphate/phosphate exchanger family (SLC37); its transport activity (substrate specificity) remains unknown, unlike the other three family members (SLC37A1, A2, A4) which are Pi-linked glucose-6-phosphate antiporters.","method":"Sequence homology analysis and functional comparison across SLC37 family members; review of biochemical characterization data","journal":"Current topics in membranes","confidence":"Medium","confidence_rationale":"Tier 3 / Strong — conclusion about unknown transport activity is based on absence of functional data replicated across multiple independent reviews; ER localization inferred from family membership","pmids":["24745989"],"is_preprint":false},{"year":2022,"finding":"Homozygous null variants in SLC37A3 cause autosomal recessive retinitis pigmentosa (ARRP); two of the identified variants cause exon skipping, establishing loss-of-function as the pathogenic mechanism.","method":"Exome sequencing of IRD patient cohort, transcript analysis (exon skipping demonstrated), protein expression analysis in fibroblast cell lines and retinal sections","journal":"Genetics in medicine","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — human genetics with molecular validation (transcript/protein analysis), multiple families, but mechanism of retinal degeneration not fully elucidated","pmids":["35486108"],"is_preprint":false},{"year":2025,"finding":"In CLL cells, lncRNA TUSC7 acts as a sponge for miR-211-5p, which targets SLC37A3; silencing SLC37A3 or upregulating miR-211-5p reverses the anti-proliferative and pro-apoptotic effects of TUSC7 overexpression, placing SLC37A3 downstream of the TUSC7/miR-211-5p axis in regulation of CLL cell proliferation.","method":"RT-qPCR, gain-of-function (TUSC7 overexpression), RNA pulldown/interaction assays, siRNA silencing of SLC37A3, rescue experiments measuring cell proliferation and apoptosis","journal":"The Kaohsiung journal of medical sciences","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, rescue experiments establish pathway placement but molecular mechanism of SLC37A3 action in CLL is not defined","pmids":["40056063"],"is_preprint":false}],"current_model":"SLC37A3 is a lysosome-localized transporter that forms a complex with ATRAID and is required for the release of nitrogen-containing bisphosphonates from lysosomes into the cytosol; it belongs to the ER-associated SLC37 sugar-phosphate/phosphate exchanger family but its intrinsic transport substrate remains uncharacterized, and loss-of-function variants cause autosomal recessive retinitis pigmentosa."},"narrative":{"mechanistic_narrative":"SLC37A3 is a membrane transporter of the SLC37 sugar-phosphate/phosphate exchanger family whose principal characterized role is in lysosomal export of nitrogen-containing bisphosphonates (N-BPs) [PMID:29745899, PMID:24745989]. At the lysosome, SLC37A3 forms a complex with ATRAID and is required to release N-BPs that have entered cells via fluid-phase endocytosis from the lysosome into the cytosol, enabling these drugs to reach their cytosolic target in the mevalonate pathway [PMID:29745899]. While the other three SLC37 family members are Pi-linked glucose-6-phosphate antiporters, the intrinsic physiological transport substrate of SLC37A3 has not been defined in the available corpus [PMID:24745989]. Homozygous loss-of-function variants in SLC37A3, including variants that cause exon skipping, cause autosomal recessive retinitis pigmentosa [PMID:35486108]. Beyond these findings, the molecular basis of SLC37A3 transport activity and its role in retinal degeneration have not been characterized in the available corpus.","teleology":[{"year":2014,"claim":"Establishing where SLC37A3 sits among transporters set the initial expectation that it is a sugar-phosphate/phosphate exchanger, while flagging that its substrate was uniquely undefined within the family.","evidence":"Sequence homology and functional comparison across SLC37 family members","pmids":["24745989"],"confidence":"Medium","gaps":["No direct transport assay identifying a substrate","ER localization inferred from family membership rather than measured for SLC37A3","Does not address physiological cargo or directionality"]},{"year":2018,"claim":"A genome-wide screen for N-BP sensitivity revealed an unexpected functional role: SLC37A3 partners with ATRAID at the lysosome to export endocytosed N-BPs into the cytosol, answering how these drugs escape the lysosome to reach their target.","evidence":"CRISPRi genome-wide screen with co-localization, complex identification, and functional N-BP rescue assays in human cells","pmids":["29745899"],"confidence":"High","gaps":["Whether N-BP export reflects the native physiological substrate or an opportunistic activity is unresolved","Stoichiometry and transport mechanism of the SLC37A3-ATRAID complex not defined","Reconciliation with the earlier ER-localization assignment not addressed"]},{"year":2022,"claim":"Human genetics tied SLC37A3 to disease, showing that complete loss of function causes autosomal recessive retinitis pigmentosa and establishing the gene as essential for retinal health.","evidence":"Exome sequencing of an inherited retinal disease cohort with transcript (exon skipping) and protein expression analysis across multiple families","pmids":["35486108"],"confidence":"Medium","gaps":["Mechanism linking SLC37A3 loss to photoreceptor degeneration not elucidated","Whether the retinal phenotype involves a transport substrate distinct from N-BPs is unknown","No animal model establishing causality"]},{"year":2025,"claim":"A regulatory context was added by placing SLC37A3 downstream of a lncRNA/miRNA axis controlling chronic lymphocytic leukemia cell proliferation.","evidence":"RT-qPCR, TUSC7 overexpression, RNA pulldown, siRNA silencing, and rescue assays measuring proliferation/apoptosis in CLL cells","pmids":["40056063"],"confidence":"Low","gaps":["Single-lab study; molecular mechanism of SLC37A3 action in CLL not defined","Whether transport activity underlies the proliferative phenotype unknown","No independent confirmation of the TUSC7/miR-211-5p/SLC37A3 axis"]},{"year":null,"claim":"The intrinsic physiological transport substrate of SLC37A3 and the mechanism connecting its loss to retinal degeneration remain unknown.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No direct biochemical identification of a native substrate","No structural model of the transporter or the SLC37A3-ATRAID complex","Causal mechanism in retinitis pigmentosa undefined"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0005215","term_label":"transporter activity","supporting_discovery_ids":[0,1]}],"localization":[{"term_id":"GO:0005764","term_label":"lysosome","supporting_discovery_ids":[0]}],"pathway":[],"complexes":["SLC37A3-ATRAID complex"],"partners":["ATRAID"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q8NCC5","full_name":"Sugar phosphate exchanger 3","aliases":["Solute carrier family 37 member 3"],"length_aa":494,"mass_kda":54.5,"function":"Unlike the other SLC37 members, lacks glucose-6-phosphate antiporter activity (PubMed:21949678). In osteoclasts, forms a transporter complex with ATRAID for nitrogen-containing-bisphophonates (N-BPs) required for releasing N-BP molecules that have trafficked to lysosomes through fluid-phase endocytosis into the cytosol (PubMed:29745899)","subcellular_location":"Endoplasmic reticulum membrane; Lysosome membrane","url":"https://www.uniprot.org/uniprotkb/Q8NCC5/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/SLC37A3","classification":"Not Classified","n_dependent_lines":3,"n_total_lines":1208,"dependency_fraction":0.0024834437086092716},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000157800","cell_line_id":"CID001346","localizations":[{"compartment":"vesicles","grade":3}],"interactors":[],"url":"https://opencell.sf.czbiohub.org/target/CID001346","total_profiled":1310},"omim":[{"mim_id":"619682","title":"ALL-TRANS RETINOIC ACID-INDUCED DIFFERENTIATION FACTOR; ATRAID","url":"https://www.omim.org/entry/619682"},{"mim_id":"619137","title":"SOLUTE CARRIER FAMILY 37, MEMBER A3; SLC37A3","url":"https://www.omim.org/entry/619137"}],"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/SLC37A3"},"hgnc":{"alias_symbol":["DKFZp761N0624","SPX3"],"prev_symbol":[]},"alphafold":{"accession":"Q8NCC5","domains":[{"cath_id":"1.20.1250.20","chopping":"17-54_72-228_281-492","consensus_level":"medium","plddt":92.0267,"start":17,"end":492}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8NCC5","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q8NCC5-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q8NCC5-F1-predicted_aligned_error_v6.png","plddt_mean":84.38},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=SLC37A3","jax_strain_url":"https://www.jax.org/strain/search?query=SLC37A3"},"sequence":{"accession":"Q8NCC5","fasta_url":"https://rest.uniprot.org/uniprotkb/Q8NCC5.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q8NCC5/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8NCC5"}},"corpus_meta":[{"pmid":"25651499","id":"PMC_25651499","title":"An analysis of DNA methylation in human adipose tissue reveals differential modification of obesity genes before and after gastric bypass and weight loss.","date":"2015","source":"Genome biology","url":"https://pubmed.ncbi.nlm.nih.gov/25651499","citation_count":200,"is_preprint":false},{"pmid":"24219008","id":"PMC_24219008","title":"Dynamically regulated miRNA-mRNA networks revealed by exercise.","date":"2013","source":"BMC physiology","url":"https://pubmed.ncbi.nlm.nih.gov/24219008","citation_count":99,"is_preprint":false},{"pmid":"24368504","id":"PMC_24368504","title":"The paralogous SPX3 and SPX5 genes redundantly modulate Pi homeostasis in rice.","date":"2013","source":"Journal of experimental botany","url":"https://pubmed.ncbi.nlm.nih.gov/24368504","citation_count":76,"is_preprint":false},{"pmid":"34469578","id":"PMC_34469578","title":"Medicago SPX1 and SPX3 regulate phosphate homeostasis, mycorrhizal colonization, and arbuscule degradation.","date":"2021","source":"The Plant cell","url":"https://pubmed.ncbi.nlm.nih.gov/34469578","citation_count":66,"is_preprint":false},{"pmid":"24745989","id":"PMC_24745989","title":"The SLC37 family of sugar-phosphate/phosphate exchangers.","date":"2014","source":"Current topics in membranes","url":"https://pubmed.ncbi.nlm.nih.gov/24745989","citation_count":49,"is_preprint":false},{"pmid":"29745899","id":"PMC_29745899","title":"Identification of a transporter complex responsible for the cytosolic entry of nitrogen-containing bisphosphonates.","date":"2018","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/29745899","citation_count":43,"is_preprint":false},{"pmid":"27181950","id":"PMC_27181950","title":"Soybean SPX1 is an important component of the response to phosphate deficiency for phosphorus homeostasis.","date":"2016","source":"Plant science : an international journal of experimental plant biology","url":"https://pubmed.ncbi.nlm.nih.gov/27181950","citation_count":40,"is_preprint":false},{"pmid":"29719821","id":"PMC_29719821","title":"The Physiopathological Role of the Exchangers Belonging to the SLC37 Family.","date":"2018","source":"Frontiers in chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/29719821","citation_count":34,"is_preprint":false},{"pmid":"12811562","id":"PMC_12811562","title":"The human sugar-phosphate/phosphate exchanger family SLC37.","date":"2003","source":"Pflugers Archiv : European journal of physiology","url":"https://pubmed.ncbi.nlm.nih.gov/12811562","citation_count":26,"is_preprint":false},{"pmid":"35486108","id":"PMC_35486108","title":"Identification of autosomal recessive novel genes and retinal phenotypes in members of the solute carrier (SLC) superfamily.","date":"2022","source":"Genetics in medicine : official journal of the American College of Medical Genetics","url":"https://pubmed.ncbi.nlm.nih.gov/35486108","citation_count":14,"is_preprint":false},{"pmid":"32614576","id":"PMC_32614576","title":"Boron and Phosphorus Act Synergistically to Modulate Absorption and Distribution of Phosphorus and Growth of Brassica napus.","date":"2020","source":"Journal of agricultural and food chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/32614576","citation_count":11,"is_preprint":false},{"pmid":"38540416","id":"PMC_38540416","title":"Whole-Exome Sequencing (WES) Reveals Novel Sex-Specific Gene Variants in Non-Alcoholic Steatohepatitis (MASH).","date":"2024","source":"Genes","url":"https://pubmed.ncbi.nlm.nih.gov/38540416","citation_count":5,"is_preprint":false},{"pmid":"38444759","id":"PMC_38444759","title":"Cold exposure impacts DNA methylation patterns in cattle sperm.","date":"2024","source":"Frontiers in genetics","url":"https://pubmed.ncbi.nlm.nih.gov/38444759","citation_count":4,"is_preprint":false},{"pmid":"36476775","id":"PMC_36476775","title":"Identification of perturbed pathways rendering susceptibility to tuberculosis in type 2 diabetes mellitus patients using BioNSi simulation of integrated networks of implicated human genes.","date":"2022","source":"Journal of biosciences","url":"https://pubmed.ncbi.nlm.nih.gov/36476775","citation_count":2,"is_preprint":false},{"pmid":"41496451","id":"PMC_41496451","title":"The Medicago SPX1/3-PHR2 network relays phosphate signaling to orchestrate root nodulation-dependent nitrogen acquisition by controlling flavonoid biosynthesis.","date":"2026","source":"Plant communications","url":"https://pubmed.ncbi.nlm.nih.gov/41496451","citation_count":1,"is_preprint":false},{"pmid":"40069519","id":"PMC_40069519","title":"SLC37A3-associated retinitis pigmentosa: a case report of clinical features and three-year follow up.","date":"2025","source":"Documenta ophthalmologica. Advances in ophthalmology","url":"https://pubmed.ncbi.nlm.nih.gov/40069519","citation_count":0,"is_preprint":false},{"pmid":"40056063","id":"PMC_40056063","title":"LncRNA TUSC7 Inhibits Cell Proliferation in Chronic Lymphocytic Leukemia by Modulating the miR-211-5p/SLC37A3 Axis.","date":"2025","source":"The Kaohsiung journal of medical sciences","url":"https://pubmed.ncbi.nlm.nih.gov/40056063","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":10952,"output_tokens":1098,"usd":0.024663,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7663,"output_tokens":1810,"usd":0.041783,"stage2_stop_reason":"end_turn"},"total_usd":0.066446,"stage1_batch_id":"msgbatch_013LWZZT6MWaqB9qyTSeQBmU","stage2_batch_id":"msgbatch_0194ZzQaTGNpruoNJBbEMbt3","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2018,\n      \"finding\": \"SLC37A3 forms a complex with ATRAID (all-trans retinoic acid-induced differentiation factor) and both proteins localize to lysosomes. SLC37A3 is required for releasing nitrogen-containing bisphosphonates (N-BPs) that have trafficked to lysosomes via fluid-phase endocytosis into the cytosol, thereby enabling N-BPs to reach their cytosolic target (the mevalonate pathway).\",\n      \"method\": \"CRISPRi genome-wide screen, co-localization, complex identification, functional rescue assays\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — genome-wide CRISPRi screen identified SLC37A3, validated by complex formation with ATRAID, lysosomal localization, and functional N-BP transport assays; multiple orthogonal methods in a single rigorous study\",\n      \"pmids\": [\"29745899\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"SLC37A3 is an endoplasmic reticulum-associated protein belonging to the sugar-phosphate/phosphate exchanger family (SLC37); its transport activity (substrate specificity) remains unknown, unlike the other three family members (SLC37A1, A2, A4) which are Pi-linked glucose-6-phosphate antiporters.\",\n      \"method\": \"Sequence homology analysis and functional comparison across SLC37 family members; review of biochemical characterization data\",\n      \"journal\": \"Current topics in membranes\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Strong — conclusion about unknown transport activity is based on absence of functional data replicated across multiple independent reviews; ER localization inferred from family membership\",\n      \"pmids\": [\"24745989\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"Homozygous null variants in SLC37A3 cause autosomal recessive retinitis pigmentosa (ARRP); two of the identified variants cause exon skipping, establishing loss-of-function as the pathogenic mechanism.\",\n      \"method\": \"Exome sequencing of IRD patient cohort, transcript analysis (exon skipping demonstrated), protein expression analysis in fibroblast cell lines and retinal sections\",\n      \"journal\": \"Genetics in medicine\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — human genetics with molecular validation (transcript/protein analysis), multiple families, but mechanism of retinal degeneration not fully elucidated\",\n      \"pmids\": [\"35486108\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"In CLL cells, lncRNA TUSC7 acts as a sponge for miR-211-5p, which targets SLC37A3; silencing SLC37A3 or upregulating miR-211-5p reverses the anti-proliferative and pro-apoptotic effects of TUSC7 overexpression, placing SLC37A3 downstream of the TUSC7/miR-211-5p axis in regulation of CLL cell proliferation.\",\n      \"method\": \"RT-qPCR, gain-of-function (TUSC7 overexpression), RNA pulldown/interaction assays, siRNA silencing of SLC37A3, rescue experiments measuring cell proliferation and apoptosis\",\n      \"journal\": \"The Kaohsiung journal of medical sciences\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, rescue experiments establish pathway placement but molecular mechanism of SLC37A3 action in CLL is not defined\",\n      \"pmids\": [\"40056063\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"SLC37A3 is a lysosome-localized transporter that forms a complex with ATRAID and is required for the release of nitrogen-containing bisphosphonates from lysosomes into the cytosol; it belongs to the ER-associated SLC37 sugar-phosphate/phosphate exchanger family but its intrinsic transport substrate remains uncharacterized, and loss-of-function variants cause autosomal recessive retinitis pigmentosa.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"SLC37A3 is a membrane transporter of the SLC37 sugar-phosphate/phosphate exchanger family whose principal characterized role is in lysosomal export of nitrogen-containing bisphosphonates (N-BPs) [#0, #1]. At the lysosome, SLC37A3 forms a complex with ATRAID and is required to release N-BPs that have entered cells via fluid-phase endocytosis from the lysosome into the cytosol, enabling these drugs to reach their cytosolic target in the mevalonate pathway [#0]. While the other three SLC37 family members are Pi-linked glucose-6-phosphate antiporters, the intrinsic physiological transport substrate of SLC37A3 has not been defined in the available corpus [#1]. Homozygous loss-of-function variants in SLC37A3, including variants that cause exon skipping, cause autosomal recessive retinitis pigmentosa [#2]. Beyond these findings, the molecular basis of SLC37A3 transport activity and its role in retinal degeneration have not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Establishing where SLC37A3 sits among transporters set the initial expectation that it is a sugar-phosphate/phosphate exchanger, while flagging that its substrate was uniquely undefined within the family.\",\n      \"evidence\": \"Sequence homology and functional comparison across SLC37 family members\",\n      \"pmids\": [\"24745989\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No direct transport assay identifying a substrate\",\n        \"ER localization inferred from family membership rather than measured for SLC37A3\",\n        \"Does not address physiological cargo or directionality\"\n      ]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"A genome-wide screen for N-BP sensitivity revealed an unexpected functional role: SLC37A3 partners with ATRAID at the lysosome to export endocytosed N-BPs into the cytosol, answering how these drugs escape the lysosome to reach their target.\",\n      \"evidence\": \"CRISPRi genome-wide screen with co-localization, complex identification, and functional N-BP rescue assays in human cells\",\n      \"pmids\": [\"29745899\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Whether N-BP export reflects the native physiological substrate or an opportunistic activity is unresolved\",\n        \"Stoichiometry and transport mechanism of the SLC37A3-ATRAID complex not defined\",\n        \"Reconciliation with the earlier ER-localization assignment not addressed\"\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Human genetics tied SLC37A3 to disease, showing that complete loss of function causes autosomal recessive retinitis pigmentosa and establishing the gene as essential for retinal health.\",\n      \"evidence\": \"Exome sequencing of an inherited retinal disease cohort with transcript (exon skipping) and protein expression analysis across multiple families\",\n      \"pmids\": [\"35486108\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Mechanism linking SLC37A3 loss to photoreceptor degeneration not elucidated\",\n        \"Whether the retinal phenotype involves a transport substrate distinct from N-BPs is unknown\",\n        \"No animal model establishing causality\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"A regulatory context was added by placing SLC37A3 downstream of a lncRNA/miRNA axis controlling chronic lymphocytic leukemia cell proliferation.\",\n      \"evidence\": \"RT-qPCR, TUSC7 overexpression, RNA pulldown, siRNA silencing, and rescue assays measuring proliferation/apoptosis in CLL cells\",\n      \"pmids\": [\"40056063\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Single-lab study; molecular mechanism of SLC37A3 action in CLL not defined\",\n        \"Whether transport activity underlies the proliferative phenotype unknown\",\n        \"No independent confirmation of the TUSC7/miR-211-5p/SLC37A3 axis\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The intrinsic physiological transport substrate of SLC37A3 and the mechanism connecting its loss to retinal degeneration remain unknown.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No direct biochemical identification of a native substrate\",\n        \"No structural model of the transporter or the SLC37A3-ATRAID complex\",\n        \"Causal mechanism in retinitis pigmentosa undefined\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005215\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005764\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [],\n    \"complexes\": [\"SLC37A3-ATRAID complex\"],\n    \"partners\": [\"ATRAID\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":3,"faith_total":3,"faith_pct":100.0}}