{"gene":"PEF1","run_date":"2026-06-10T05:19:53","timeline":{"discoveries":[{"year":2019,"finding":"The penta-EF-hand protein PEF1 of Neurospora crassa accumulates at sites of plasma membrane injury in a Ca2+-dependent manner, as shown by live-cell imaging of GFP-tagged PEF1. Site-directed mutagenesis of Ca2+-binding EF-hand domains abolished both the spatial dynamics and the membrane-repair function of the protein.","method":"Live-cell fluorescence imaging of GFP-PEF1, site-directed mutagenesis of Ca2+-binding domains, deletion mutant analysis with membrane integrity assays","journal":"Genetics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct live imaging with functional mutagenesis of Ca2+-binding domains in a single lab study with multiple orthogonal methods","pmids":["31270133"],"is_preprint":false},{"year":2019,"finding":"Deletion of pef1 in Neurospora crassa impairs plasma membrane integrity during cell-cell fusion and in the presence of pore-forming drugs (e.g., tomatine), establishing PEF1 as required for membrane repair in fungi.","method":"Gene knockout, cell-cell fusion assays, pore-forming drug (tomatine) treatment with viability/integrity readouts","journal":"Genetics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean KO with defined cellular phenotype, multiple perturbation conditions, single lab","pmids":["31270133"],"is_preprint":false},{"year":2024,"finding":"In Candida albicans, GFP-tagged Pef1 (penta-EF-hand protein, ortholog of human ALG-2/PEF1) localizes to sites of polarized growth in yeast and hyphal cells, and redistributes to punctate membrane spots upon treatment with amphotericin B or tomatine, indicating Ca2+-dependent recruitment to sites of membrane perturbation.","method":"Live-cell fluorescence imaging of GFP-Pef1, pharmacological membrane disruption (amphotericin B, tomatine), genetic deletion of calcineurin (cna1Δ)","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct live imaging with pharmacological and genetic perturbations, but preprint status lowers certainty","pmids":["bio_10.1101_2024.09.06.611525"],"is_preprint":true},{"year":2026,"finding":"Deletion of PEF1 in C. albicans does not affect filamentation but causes failure to maintain plasma membrane integrity in serum (specifically in hyphae), and attenuates virulence in an insect larvae infection model, placing PEF1 in a membrane integrity pathway downstream of calcineurin A (Cna1) but not Crz1.","method":"Gene deletion (pef1Δ), membrane integrity assays in serum, genetic epistasis with cna1Δ and crz1Δ mutants, insect larvae virulence model","journal":"G3 (Bethesda, Md.)","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean KO with defined cellular and virulence phenotype, epistasis with calcineurin pathway, single lab","pmids":["41920808"],"is_preprint":false}],"current_model":"PEF1 (a penta-EF-hand Ca2+-binding protein orthologous to human ALG-2/PEF1A) is recruited in a Ca2+-dependent manner to sites of plasma membrane injury and polarized growth, where it promotes membrane integrity and repair; its Ca2+-binding EF-hand domains are essential for both its localization dynamics and function, and it operates downstream of calcineurin A but independently of the Crz1 transcription factor."},"narrative":{"mechanistic_narrative":"PEF1 is a penta-EF-hand Ca2+-binding protein that functions in the maintenance and repair of plasma membrane integrity in fungi [PMID:31270133]. In Neurospora crassa, GFP-tagged PEF1 accumulates at sites of plasma membrane injury in a Ca2+-dependent manner, and mutation of its Ca2+-binding EF-hand domains abolishes both this spatial recruitment and the protein's membrane-repair function, establishing that Ca2+ sensing through the EF-hands drives localization and activity [PMID:31270133]. Loss of PEF1 compromises membrane integrity during cell-cell fusion and upon challenge with pore-forming agents such as tomatine [PMID:31270133]. In Candida albicans, the ortholog localizes to sites of polarized growth and redistributes into punctate membrane spots upon membrane perturbation by amphotericin B or tomatine [PMID:bio_10.1101_2024.09.06.611525], and is required for hyphal plasma membrane integrity in serum and for full virulence, operating downstream of calcineurin A (Cna1) but independently of the Crz1 transcription factor [PMID:41920808]. Beyond this Ca2+-dependent membrane-repair role, no molecular partners or biochemical mechanism of PEF1 have been characterized in the available corpus.","teleology":[{"year":2019,"claim":"Established that a fungal penta-EF-hand protein acts as a Ca2+-triggered effector at sites of membrane damage, linking Ca2+ sensing to membrane repair.","evidence":"Live-cell imaging of GFP-PEF1 with site-directed mutagenesis of EF-hand Ca2+-binding domains and deletion-mutant membrane integrity assays in Neurospora crassa","pmids":["31270133"],"confidence":"High","gaps":["No direct biochemical demonstration of Ca2+ binding or the membrane species engaged","Molecular mechanism of repair (membrane resealing partners) not identified","No interacting proteins characterized"]},{"year":2024,"claim":"Extended the membrane-perturbation response to a second fungal species and connected PEF1 recruitment to polarized growth sites and the calcineurin pathway.","evidence":"Live-cell imaging of GFP-Pef1 with pharmacological membrane disruption (amphotericin B, tomatine) and cna1Δ deletion in Candida albicans (preprint)","pmids":["bio_10.1101_2024.09.06.611525"],"confidence":"Medium","gaps":["Preprint status lowers certainty","Functional consequence of polarized-growth localization not resolved","Direct epistasis with calcineurin not yet established at this stage"]},{"year":2026,"claim":"Defined PEF1's physiological role in hyphal membrane integrity and virulence and placed it genetically downstream of calcineurin A but separate from Crz1.","evidence":"pef1Δ deletion with serum membrane-integrity assays, epistasis with cna1Δ and crz1Δ, and an insect larvae virulence model in Candida albicans","pmids":["41920808"],"confidence":"Medium","gaps":["Crz1-independent branch of calcineurin signaling acting through PEF1 not molecularly defined","How calcineurin regulates PEF1 (direct dephosphorylation vs. indirect) unknown","Relevance to mammalian ortholog ALG-2/PEF1A not addressed"]},{"year":null,"claim":"The molecular partners and biochemical mechanism by which PEF1 promotes membrane resealing, and how calcineurin controls it, remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No physical interaction partners or substrates identified","No structural model of Ca2+-bound PEF1 or its membrane engagement","Mechanistic link between calcineurin A activity and PEF1 recruitment undefined"]}],"mechanism_profile":{"molecular_activity":[],"localization":[{"term_id":"GO:0005886","term_label":"plasma membrane","supporting_discovery_ids":[0,1,2,3]}],"pathway":[],"complexes":[],"partners":[],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q9UBV8","full_name":"Peflin","aliases":["PEF protein with a long N-terminal hydrophobic domain","Penta-EF hand domain-containing protein 1"],"length_aa":284,"mass_kda":30.4,"function":"Calcium-binding protein that acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium. Together with PDCD6, acts as a calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in endoplasmic reticulum (ER)-Golgi transport by regulating the size of COPII coats (PubMed:27716508). In response to cytosolic calcium increase, the heterodimer formed with PDCD6 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification (PubMed:27716508). Its role in the heterodimer formed with PDCD6 is however unclear: some evidence shows that PEF1 and PDCD6 work together and promote association between PDCD6 and SEC31 in presence of calcium (PubMed:27716508). Other reports show that PEF1 dissociates from PDCD6 in presence of calcium, and may act as a negative regulator of PDCD6 (PubMed:11278427). Also acts as a negative regulator of ER-Golgi transport; possibly by inhibiting interaction between PDCD6 and SEC31 (By similarity)","subcellular_location":"Cytoplasm; Endoplasmic reticulum; Membrane; Cytoplasmic vesicle, COPII-coated vesicle membrane","url":"https://www.uniprot.org/uniprotkb/Q9UBV8/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/PEF1","classification":"Common Essential","n_dependent_lines":456,"n_total_lines":1208,"dependency_fraction":0.37748344370860926},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"PDCD6","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/PEF1","total_profiled":1310},"omim":[{"mim_id":"610033","title":"PENTA-EF-HAND DOMAIN-CONTAINING PROTEIN 1; PEF1","url":"https://www.omim.org/entry/610033"},{"mim_id":"601057","title":"PROGRAMMED CELL DEATH 6; PDCD6","url":"https://www.omim.org/entry/601057"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nucleoplasm","reliability":"Approved"},{"location":"Vesicles","reliability":"Approved"},{"location":"Cytosol","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/PEF1"},"hgnc":{"alias_symbol":["PEF1A"],"prev_symbol":[]},"alphafold":{"accession":"Q9UBV8","domains":[{"cath_id":"1.10.238.10","chopping":"116-280","consensus_level":"medium","plddt":94.1204,"start":116,"end":280}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9UBV8","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9UBV8-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9UBV8-F1-predicted_aligned_error_v6.png","plddt_mean":73.31},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=PEF1","jax_strain_url":"https://www.jax.org/strain/search?query=PEF1"},"sequence":{"accession":"Q9UBV8","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9UBV8.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9UBV8/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9UBV8"}},"corpus_meta":[{"pmid":"7769658","id":"PMC_7769658","title":"The enhancer in the long control region of human papillomavirus type 16 is up-regulated by PEF-1 and down-regulated by Oct-1.","date":"1995","source":"Journal of virology","url":"https://pubmed.ncbi.nlm.nih.gov/7769658","citation_count":38,"is_preprint":false},{"pmid":"32788233","id":"PMC_32788233","title":"The S. pombe CDK5 ortholog Pef1 regulates sexual differentiation through control of the TORC1 pathway and autophagy.","date":"2020","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/32788233","citation_count":11,"is_preprint":false},{"pmid":"16893567","id":"PMC_16893567","title":"Molecular analysis of the 21-kb bacteriocin-encoding plasmid pEF1 from Enterococcus faecium 6T1a.","date":"2006","source":"Plasmid","url":"https://pubmed.ncbi.nlm.nih.gov/16893567","citation_count":10,"is_preprint":false},{"pmid":"31270133","id":"PMC_31270133","title":"Plasma Membrane Integrity During Cell-Cell Fusion and in Response to Pore-Forming Drugs Is Promoted by the Penta-EF-Hand Protein PEF1 in Neurospora crassa.","date":"2019","source":"Genetics","url":"https://pubmed.ncbi.nlm.nih.gov/31270133","citation_count":7,"is_preprint":false},{"pmid":"39335057","id":"PMC_39335057","title":"Characterization of Two Novel Endolysins from Bacteriophage PEF1 and Evaluation of Their Combined Effects on the Control of Enterococcus faecalis Planktonic and Biofilm Cells.","date":"2024","source":"Antibiotics (Basel, Switzerland)","url":"https://pubmed.ncbi.nlm.nih.gov/39335057","citation_count":4,"is_preprint":false},{"pmid":"31895039","id":"PMC_31895039","title":"The CDK Pef1 and protein phosphatase 4 oppose each other for regulating cohesin binding to fission yeast chromosomes.","date":"2020","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/31895039","citation_count":3,"is_preprint":false},{"pmid":"33445784","id":"PMC_33445784","title":"The S. pombe CDK5 Orthologue Pef1 Cooperates with Three Cyclins, Clg1, Pas1 and Psl1, to Promote Pre-Meiotic DNA Replication.","date":"2021","source":"Biomolecules","url":"https://pubmed.ncbi.nlm.nih.gov/33445784","citation_count":3,"is_preprint":false},{"pmid":"9820151","id":"PMC_9820151","title":"PEF-1, an epithelial cell transcription factor which activates the long control region of human papillomavirus type 16, is glycosylated with N-acetylglucosamine.","date":"1998","source":"The Journal of general virology","url":"https://pubmed.ncbi.nlm.nih.gov/9820151","citation_count":2,"is_preprint":false},{"pmid":"38915521","id":"PMC_38915521","title":"In Vivo Proximity Labeling Identifies a New Function for the Lifespan and Autophagy-regulating Kinase Pef1, an Ortholog of Human Cdk5.","date":"2024","source":"bioRxiv : the preprint server for biology","url":"https://pubmed.ncbi.nlm.nih.gov/38915521","citation_count":0,"is_preprint":false},{"pmid":"41920808","id":"PMC_41920808","title":"The penta-EF-hand protein Pef1 of Candida albicans functions at sites of membrane perturbation to support polarized growth and membrane integrity.","date":"2026","source":"G3 (Bethesda, Md.)","url":"https://pubmed.ncbi.nlm.nih.gov/41920808","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2024.09.06.611525","title":"The penta-EF-hand protein Pef1 of  <i>Candida albicans</i>  functions at sites of membrane perturbation to support polarized growth and membrane integrity","date":"2024-09-07","source":"bioRxiv","url":"https://doi.org/10.1101/2024.09.06.611525","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":7157,"output_tokens":1482,"usd":0.02185,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7628,"output_tokens":1592,"usd":0.03897,"stage2_stop_reason":"end_turn"},"total_usd":0.06082,"stage1_batch_id":"msgbatch_013a8chtv3AWyTqv4z4sEF4C","stage2_batch_id":"msgbatch_01AHsuW63vinsvuTgzmQ3n62","note":"batch pricing = 50% of standard"},"stage1_raw":"Looking at the corpus, I need to identify which papers are about the human/mammalian gene PEF1 (also known as PEF1A).\n\n**Classification:**\n- Papers [1] and [8]: About \"PEF-1,\" a transcription factor binding HPV-16 LCR. This appears to be a different protein (a transcription factor, ~110 kDa, GC-rich DNA binding) — NOT the canonical PEF1/PEF1A penta-EF-hand protein. This is likely a symbol collision with a different factor described in older HPV literature.\n- Papers [2], [6], [7], [9]: About S. pombe Pef1, described as ortholog of mammalian CDK5. The human gene PEF1 (PEF1A) is NOT CDK5 — it's a penta-EF-hand protein. These are symbol collisions with fission yeast CDK5 ortholog.\n- Papers [3], [5]: About a bacteriocin plasmid pEF1 from Enterococcus — clearly a symbol collision, microbial plasmid.\n- Papers [4], [10], [11]: About Neurospora crassa and Candida albicans penta-EF-hand protein Pef1, which is described as ortholog of human ALG-2. PEF1/PEF1A in humans is indeed a penta-EF-hand protein (paralog of ALG-2/PDCD6). These are fungal orthologs of the human PEF1 protein — INCLUDE.\n\nPapers [4], [10], [11] describe penta-EF-hand Pef1 functionally consistent with the human PEF1/PEF1A protein.\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2019,\n      \"finding\": \"The penta-EF-hand protein PEF1 of Neurospora crassa accumulates at sites of plasma membrane injury in a Ca2+-dependent manner, as shown by live-cell imaging of GFP-tagged PEF1. Site-directed mutagenesis of Ca2+-binding EF-hand domains abolished both the spatial dynamics and the membrane-repair function of the protein.\",\n      \"method\": \"Live-cell fluorescence imaging of GFP-PEF1, site-directed mutagenesis of Ca2+-binding domains, deletion mutant analysis with membrane integrity assays\",\n      \"journal\": \"Genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct live imaging with functional mutagenesis of Ca2+-binding domains in a single lab study with multiple orthogonal methods\",\n      \"pmids\": [\"31270133\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"Deletion of pef1 in Neurospora crassa impairs plasma membrane integrity during cell-cell fusion and in the presence of pore-forming drugs (e.g., tomatine), establishing PEF1 as required for membrane repair in fungi.\",\n      \"method\": \"Gene knockout, cell-cell fusion assays, pore-forming drug (tomatine) treatment with viability/integrity readouts\",\n      \"journal\": \"Genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean KO with defined cellular phenotype, multiple perturbation conditions, single lab\",\n      \"pmids\": [\"31270133\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"In Candida albicans, GFP-tagged Pef1 (penta-EF-hand protein, ortholog of human ALG-2/PEF1) localizes to sites of polarized growth in yeast and hyphal cells, and redistributes to punctate membrane spots upon treatment with amphotericin B or tomatine, indicating Ca2+-dependent recruitment to sites of membrane perturbation.\",\n      \"method\": \"Live-cell fluorescence imaging of GFP-Pef1, pharmacological membrane disruption (amphotericin B, tomatine), genetic deletion of calcineurin (cna1Δ)\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct live imaging with pharmacological and genetic perturbations, but preprint status lowers certainty\",\n      \"pmids\": [\"bio_10.1101_2024.09.06.611525\"],\n      \"is_preprint\": true\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"Deletion of PEF1 in C. albicans does not affect filamentation but causes failure to maintain plasma membrane integrity in serum (specifically in hyphae), and attenuates virulence in an insect larvae infection model, placing PEF1 in a membrane integrity pathway downstream of calcineurin A (Cna1) but not Crz1.\",\n      \"method\": \"Gene deletion (pef1Δ), membrane integrity assays in serum, genetic epistasis with cna1Δ and crz1Δ mutants, insect larvae virulence model\",\n      \"journal\": \"G3 (Bethesda, Md.)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean KO with defined cellular and virulence phenotype, epistasis with calcineurin pathway, single lab\",\n      \"pmids\": [\"41920808\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"PEF1 (a penta-EF-hand Ca2+-binding protein orthologous to human ALG-2/PEF1A) is recruited in a Ca2+-dependent manner to sites of plasma membrane injury and polarized growth, where it promotes membrane integrity and repair; its Ca2+-binding EF-hand domains are essential for both its localization dynamics and function, and it operates downstream of calcineurin A but independently of the Crz1 transcription factor.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PEF1 is a penta-EF-hand Ca2+-binding protein that functions in the maintenance and repair of plasma membrane integrity in fungi [#0, #1]. In Neurospora crassa, GFP-tagged PEF1 accumulates at sites of plasma membrane injury in a Ca2+-dependent manner, and mutation of its Ca2+-binding EF-hand domains abolishes both this spatial recruitment and the protein's membrane-repair function, establishing that Ca2+ sensing through the EF-hands drives localization and activity [#0]. Loss of PEF1 compromises membrane integrity during cell-cell fusion and upon challenge with pore-forming agents such as tomatine [#1]. In Candida albicans, the ortholog localizes to sites of polarized growth and redistributes into punctate membrane spots upon membrane perturbation by amphotericin B or tomatine [#2], and is required for hyphal plasma membrane integrity in serum and for full virulence, operating downstream of calcineurin A (Cna1) but independently of the Crz1 transcription factor [#3]. Beyond this Ca2+-dependent membrane-repair role, no molecular partners or biochemical mechanism of PEF1 have been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2019,\n      \"claim\": \"Established that a fungal penta-EF-hand protein acts as a Ca2+-triggered effector at sites of membrane damage, linking Ca2+ sensing to membrane repair.\",\n      \"evidence\": \"Live-cell imaging of GFP-PEF1 with site-directed mutagenesis of EF-hand Ca2+-binding domains and deletion-mutant membrane integrity assays in Neurospora crassa\",\n      \"pmids\": [\"31270133\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"No direct biochemical demonstration of Ca2+ binding or the membrane species engaged\",\n        \"Molecular mechanism of repair (membrane resealing partners) not identified\",\n        \"No interacting proteins characterized\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Extended the membrane-perturbation response to a second fungal species and connected PEF1 recruitment to polarized growth sites and the calcineurin pathway.\",\n      \"evidence\": \"Live-cell imaging of GFP-Pef1 with pharmacological membrane disruption (amphotericin B, tomatine) and cna1Δ deletion in Candida albicans (preprint)\",\n      \"pmids\": [\"bio_10.1101_2024.09.06.611525\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Preprint status lowers certainty\",\n        \"Functional consequence of polarized-growth localization not resolved\",\n        \"Direct epistasis with calcineurin not yet established at this stage\"\n      ]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Defined PEF1's physiological role in hyphal membrane integrity and virulence and placed it genetically downstream of calcineurin A but separate from Crz1.\",\n      \"evidence\": \"pef1Δ deletion with serum membrane-integrity assays, epistasis with cna1Δ and crz1Δ, and an insect larvae virulence model in Candida albicans\",\n      \"pmids\": [\"41920808\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Crz1-independent branch of calcineurin signaling acting through PEF1 not molecularly defined\",\n        \"How calcineurin regulates PEF1 (direct dephosphorylation vs. indirect) unknown\",\n        \"Relevance to mammalian ortholog ALG-2/PEF1A not addressed\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The molecular partners and biochemical mechanism by which PEF1 promotes membrane resealing, and how calcineurin controls it, remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No physical interaction partners or substrates identified\",\n        \"No structural model of Ca2+-bound PEF1 or its membrane engagement\",\n        \"Mechanistic link between calcineurin A activity and PEF1 recruitment undefined\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [],\n    \"localization\": [\n      {\"term_id\": \"GO:0005886\", \"supporting_discovery_ids\": [0, 1, 2, 3]}\n    ],\n    \"pathway\": [],\n    \"complexes\": [],\n    \"partners\": [],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":4,"faith_total":4,"faith_pct":100.0}}