{"gene":"CLXN","run_date":"2026-06-09T22:57:18","timeline":{"discoveries":[{"year":2019,"finding":"Calaxin (encoded by Efcab1/CLXN) is required for normal motile cilia function in vertebrates; null mutation in mice causes primary ciliary dyskinesia phenotypes (hydrocephalus, situs inversus, abnormal tracheal cilia and sperm flagella motility). The 9+2 axonemal structures of multicilia and sperm flagella are preserved, but 9+0 nodal cilia formation is significantly disrupted. Knockout in zebrafish causes situs inversus due to irregular ciliary beating in Kupffer's vesicle, with 9+2 axonemal structure remaining normal.","method":"Germline knockout mouse (Efcab1 null), transmission electron microscopy of axonemal ultrastructure, high-speed video microscopy of ciliary beating; zebrafish knockout with Kupffer's vesicle cilia analysis","journal":"Communications biology","confidence":"High","confidence_rationale":"Tier 2 / Strong — loss-of-function in two vertebrate model organisms (mouse and zebrafish) with defined structural and functional readouts, replicated across species","pmids":["31240264"],"is_preprint":false},{"year":2023,"finding":"Pathogenic variants in CLXN (EFCAB1/ODAD5) cause primary ciliary dyskinesia with defects specifically in distal ODA assembly in respiratory cilia. CLXN protein is absent from ciliary axonemes in affected individuals, and ODA components DNAH5, DNAI1, DNAI2 are absent from distal axonemes while DNAH9 is mislocalized or absent. CLXN is also undetectable in ciliary axonemes of individuals with defects in ODA-docking complex proteins ODAD1, ODAD2, ODAD3, and ODAD4, placing CLXN within the ODA-docking complex as ODAD5. Knockdown of SMED-EFCAB1 in planaria causes ciliary dysmotility.","method":"Clinical exome sequencing, immunofluorescence microscopy of ciliary axonemes, transmission electron microscopy of ODA ultrastructure, planaria RNAi knockdown","journal":"Genetics in medicine","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (TEM, IF, genetic analysis in three organisms) establishing pathway position and molecular mechanism","pmids":["36727596"],"is_preprint":false},{"year":2023,"finding":"Calaxin/Efcab1 stabilizes the docking of outer arm dynein (OAD) onto ciliary doublet microtubules (DMT) in vertebrates. In zebrafish, calaxin mutation causes only partial OAD loss (unlike armc4 mutation which causes complete OAD loss). Calaxin-deficient OADs remain tethered to DMT through other docking complex components. Recombinant Calaxin can autonomously rescue the deficient docking complex structure and OAD instability, demonstrating a discrete stabilizing role distinct from that of Armc4.","method":"Zebrafish calaxin and armc4 mutants, cryo-electron tomography of spermatozoa axonemes, recombinant Calaxin rescue experiment","journal":"eLife","confidence":"High","confidence_rationale":"Tier 1 / Strong — cryo-electron tomography structural analysis combined with recombinant protein rescue, multiple mutant comparisons, single rigorous study with multiple orthogonal methods","pmids":["37057896"],"is_preprint":false},{"year":2021,"finding":"EFCAB1 overexpression in lung adenocarcinoma cell lines (A549, PC9) inhibits cell proliferation, migration, and invasion while promoting apoptosis. DNMT3B mRNA expression was elevated in EFCAB1-low cell lines, suggesting a functional relationship between EFCAB1 levels and DNMT3B expression.","method":"EFCAB1 overexpression in A549 and PC9 cell lines; CCK-8 proliferation assay, migration/invasion assays, colony formation assay, apoptosis assay; qPCR for DNMT expression","journal":"Journal of clinical laboratory analysis","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, cell-line overexpression with phenotypic readouts but no defined molecular mechanism or pathway placement; DNMT3B relationship is correlative","pmids":["34904288"],"is_preprint":false}],"current_model":"CLXN (Calaxin/EFCAB1/ODAD5) is a Ca²⁺-binding protein that functions as a component of the outer dynein arm docking complex (ODAD5) in motile cilia, where it stabilizes the attachment of outer arm dynein onto ciliary doublet microtubules; loss of CLXN causes primary ciliary dyskinesia with selective defects in distal ODA assembly and disrupted nodal cilia formation, while its localization to axonemes depends on the integrity of the broader ODA-docking complex."},"narrative":{"mechanistic_narrative":"CLXN (Calaxin/EFCAB1/ODAD5) is a Ca²⁺-binding protein essential for the function of motile cilia and flagella in vertebrates [PMID:31240264]. It operates as the ODAD5 component of the outer dynein arm (ODA)-docking complex, where it stabilizes the attachment of outer arm dynein onto ciliary doublet microtubules; cryo-electron tomography shows that loss of Calaxin causes only partial OAD loss because the dynein remains tethered through other docking-complex subunits, and recombinant Calaxin autonomously rescues the deficient docking structure, establishing a discrete stabilizing role distinct from that of Armc4 [PMID:37057896]. CLXN's incorporation into the axoneme depends on the integrity of the broader docking complex, as it is undetectable when ODAD1–ODAD4 are defective [PMID:36727596]. Loss of CLXN function produces primary ciliary dyskinesia: in humans, pathogenic variants cause selective failure of distal ODA assembly with absence of DNAH5, DNAI1, and DNAI2 from distal axonemes and mislocalization of DNAH9 [PMID:36727596], while mouse and zebrafish nulls show hydrocephalus, situs inversus, and abnormal ciliary/flagellar beating with preserved 9+2 axonemal structure but disrupted 9+0 nodal cilia [PMID:31240264].","teleology":[{"year":2019,"claim":"Established that Calaxin is functionally required for motile cilia and flagella in vertebrates, answering whether this Ca²⁺-binding protein has an essential ciliary role in vivo.","evidence":"Germline Efcab1-null mice and zebrafish knockouts analyzed by TEM and high-speed video microscopy of cilia/flagella","pmids":["31240264"],"confidence":"High","gaps":["Molecular partners and biochemical mechanism not defined","Preserved 9+2 structure left the structural basis of motility defect unexplained","Why nodal (9+0) cilia are selectively disrupted not resolved"]},{"year":2023,"claim":"Placed CLXN within the ODA-docking complex as ODAD5 and defined its molecular consequence, answering where in the cilia assembly pathway the protein acts.","evidence":"Clinical exome sequencing, immunofluorescence and TEM of patient ciliary axonemes, and planaria RNAi knockdown","pmids":["36727596"],"confidence":"High","gaps":["Direct binding interfaces between CLXN and other ODAD subunits not mapped","Role of Ca²⁺ binding in docking-complex function not tested","Mechanism of selective distal versus proximal ODA assembly unresolved"]},{"year":2023,"claim":"Resolved the discrete structural function of Calaxin in stabilizing OAD docking, distinguishing it from Armc4 and demonstrating autonomous sufficiency.","evidence":"Cryo-electron tomography of zebrafish calaxin and armc4 mutant spermatozoa axonemes with recombinant Calaxin rescue","pmids":["37057896"],"confidence":"High","gaps":["Atomic-level interactions within the docking complex not determined","How Ca²⁺ modulates the stabilizing activity not addressed","Stoichiometry of Calaxin within the complex not defined"]},{"year":2021,"claim":"Reported a candidate non-ciliary role for EFCAB1 as a suppressor of lung adenocarcinoma cell growth, raising whether the protein has functions outside motile cilia.","evidence":"EFCAB1 overexpression in A549 and PC9 cell lines with proliferation, migration, invasion, apoptosis assays and qPCR for DNMT3B","pmids":["34904288"],"confidence":"Low","gaps":["Overexpression phenotype not validated by loss-of-function","DNMT3B relationship is correlative with no mechanism","Connection to the established ciliary function unknown"]},{"year":null,"claim":"How Ca²⁺ binding by CLXN regulates outer dynein arm docking and ciliary beat, and the structural basis of its interaction with other ODAD subunits, remain open.","evidence":"","pmids":[],"confidence":"High","gaps":["No atomic structure of CLXN within the docking complex","Functional role of Ca²⁺ sensing in docking not tested","Direct binding partners within the complex not biochemically mapped"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[2]},{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[1,2]}],"localization":[{"term_id":"GO:0005929","term_label":"cilium","supporting_discovery_ids":[0,1,2]},{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[2]}],"pathway":[{"term_id":"R-HSA-1852241","term_label":"Organelle biogenesis and maintenance","supporting_discovery_ids":[1,2]},{"term_id":"R-HSA-1643685","term_label":"Disease","supporting_discovery_ids":[1]}],"complexes":["outer dynein arm-docking complex (ODA-DC)"],"partners":["ODAD1","ODAD2","ODAD3","ODAD4","ARMC4"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q9HAE3","full_name":"Calaxin","aliases":["EF-hand calcium-binding domain-containing protein 1"],"length_aa":211,"mass_kda":24.5,"function":"Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Seems to regulate the assembly of both ODAs and their axonemal docking complex onto ciliary microtubules (By similarity). Regulates ciliary and flagellar motility and is required for cilia-driven determination of body laterality (By similarity)","subcellular_location":"Cytoplasm, cytoskeleton, cilium axoneme; Cell projection, cilium; Cell projection, cilium, flagellum","url":"https://www.uniprot.org/uniprotkb/Q9HAE3/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/CLXN","classification":"Not Classified","n_dependent_lines":4,"n_total_lines":1208,"dependency_fraction":0.0033112582781456954},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/CLXN","total_profiled":1310},"omim":[{"mim_id":"620642","title":"CILIARY DYSKINESIA, PRIMARY, 53; CILD53","url":"https://www.omim.org/entry/620642"},{"mim_id":"619564","title":"CALAXIN; CLXN","url":"https://www.omim.org/entry/619564"},{"mim_id":"244400","title":"CILIARY DYSKINESIA, PRIMARY, 1; CILD1","url":"https://www.omim.org/entry/244400"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Mid piece","reliability":"Approved"},{"location":"Principal piece","reliability":"Approved"},{"location":"Nucleoplasm","reliability":"Additional"}],"tissue_specificity":"Group enriched","tissue_distribution":"Detected in many","driving_tissues":[{"tissue":"choroid plexus","ntpm":51.3},{"tissue":"fallopian tube","ntpm":86.1},{"tissue":"testis","ntpm":35.9}],"url":"https://www.proteinatlas.org/search/CLXN"},"hgnc":{"alias_symbol":["FLJ11767","ODAD5"],"prev_symbol":["EFCAB1"]},"alphafold":{"accession":"Q9HAE3","domains":[{"cath_id":"1.10.238.10","chopping":"2-99_190-201","consensus_level":"medium","plddt":90.4543,"start":2,"end":201},{"cath_id":"1.10.238.10","chopping":"101-179","consensus_level":"medium","plddt":91.642,"start":101,"end":179}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9HAE3","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9HAE3-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9HAE3-F1-predicted_aligned_error_v6.png","plddt_mean":89.62},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=CLXN","jax_strain_url":"https://www.jax.org/strain/search?query=CLXN"},"sequence":{"accession":"Q9HAE3","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9HAE3.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9HAE3/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9HAE3"}},"corpus_meta":[{"pmid":"31240264","id":"PMC_31240264","title":"Calaxin is required for cilia-driven determination of vertebrate laterality.","date":"2019","source":"Communications biology","url":"https://pubmed.ncbi.nlm.nih.gov/31240264","citation_count":32,"is_preprint":false},{"pmid":"28069692","id":"PMC_28069692","title":"Genes involved in development and differentiation are commonly methylated in cancers derived from multiple organs: a single-institutional methylome analysis using 1007 tissue specimens.","date":"2017","source":"Carcinogenesis","url":"https://pubmed.ncbi.nlm.nih.gov/28069692","citation_count":21,"is_preprint":false},{"pmid":"32650755","id":"PMC_32650755","title":"Evaluation of MiR-1908-3p as a novel serum biomarker for breast cancer and analysis its oncogenic function and target genes.","date":"2020","source":"BMC cancer","url":"https://pubmed.ncbi.nlm.nih.gov/32650755","citation_count":17,"is_preprint":false},{"pmid":"36727596","id":"PMC_36727596","title":"Pathogenic variants in CLXN encoding the outer dynein arm docking-associated calcium-binding protein calaxin cause primary ciliary dyskinesia.","date":"2023","source":"Genetics in medicine : official journal of the American College of Medical Genetics","url":"https://pubmed.ncbi.nlm.nih.gov/36727596","citation_count":10,"is_preprint":false},{"pmid":"37057896","id":"PMC_37057896","title":"Calaxin stabilizes the docking of outer arm dyneins onto ciliary doublet microtubule in vertebrates.","date":"2023","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/37057896","citation_count":10,"is_preprint":false},{"pmid":"31001336","id":"PMC_31001336","title":"Identifying and Validating Genes with DNA Methylation Data in the Context of Biological Network for Chinese Patients with Graves' Orbitopathy.","date":"2019","source":"International journal of endocrinology","url":"https://pubmed.ncbi.nlm.nih.gov/31001336","citation_count":8,"is_preprint":false},{"pmid":"37956402","id":"PMC_37956402","title":"Dopamine receptor D2 regulates genes involved in germ cell movement and sperm motility in rat testes†.","date":"2024","source":"Biology of reproduction","url":"https://pubmed.ncbi.nlm.nih.gov/37956402","citation_count":7,"is_preprint":false},{"pmid":"34904288","id":"PMC_34904288","title":"Low-level EFCAB1 promoted progress by upregulated DNMT3B and could be as a potential biomarker in lung adenocarcinoma.","date":"2021","source":"Journal of clinical laboratory analysis","url":"https://pubmed.ncbi.nlm.nih.gov/34904288","citation_count":3,"is_preprint":false},{"pmid":"37437553","id":"PMC_37437553","title":"Genome-Wide Association Studies for Albuminuria of Nondiabetic Taiwanese Population.","date":"2023","source":"American journal of nephrology","url":"https://pubmed.ncbi.nlm.nih.gov/37437553","citation_count":3,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6922,"output_tokens":1367,"usd":0.020636,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":8048,"output_tokens":2011,"usd":0.045257,"stage2_stop_reason":"end_turn"},"total_usd":0.065893,"stage1_batch_id":"msgbatch_01ACAxJQabDsht39JXeWG22d","stage2_batch_id":"msgbatch_01QEU22A9U5sbPTgsMzTmvSf","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2019,\n      \"finding\": \"Calaxin (encoded by Efcab1/CLXN) is required for normal motile cilia function in vertebrates; null mutation in mice causes primary ciliary dyskinesia phenotypes (hydrocephalus, situs inversus, abnormal tracheal cilia and sperm flagella motility). The 9+2 axonemal structures of multicilia and sperm flagella are preserved, but 9+0 nodal cilia formation is significantly disrupted. Knockout in zebrafish causes situs inversus due to irregular ciliary beating in Kupffer's vesicle, with 9+2 axonemal structure remaining normal.\",\n      \"method\": \"Germline knockout mouse (Efcab1 null), transmission electron microscopy of axonemal ultrastructure, high-speed video microscopy of ciliary beating; zebrafish knockout with Kupffer's vesicle cilia analysis\",\n      \"journal\": \"Communications biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — loss-of-function in two vertebrate model organisms (mouse and zebrafish) with defined structural and functional readouts, replicated across species\",\n      \"pmids\": [\"31240264\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"Pathogenic variants in CLXN (EFCAB1/ODAD5) cause primary ciliary dyskinesia with defects specifically in distal ODA assembly in respiratory cilia. CLXN protein is absent from ciliary axonemes in affected individuals, and ODA components DNAH5, DNAI1, DNAI2 are absent from distal axonemes while DNAH9 is mislocalized or absent. CLXN is also undetectable in ciliary axonemes of individuals with defects in ODA-docking complex proteins ODAD1, ODAD2, ODAD3, and ODAD4, placing CLXN within the ODA-docking complex as ODAD5. Knockdown of SMED-EFCAB1 in planaria causes ciliary dysmotility.\",\n      \"method\": \"Clinical exome sequencing, immunofluorescence microscopy of ciliary axonemes, transmission electron microscopy of ODA ultrastructure, planaria RNAi knockdown\",\n      \"journal\": \"Genetics in medicine\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (TEM, IF, genetic analysis in three organisms) establishing pathway position and molecular mechanism\",\n      \"pmids\": [\"36727596\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"Calaxin/Efcab1 stabilizes the docking of outer arm dynein (OAD) onto ciliary doublet microtubules (DMT) in vertebrates. In zebrafish, calaxin mutation causes only partial OAD loss (unlike armc4 mutation which causes complete OAD loss). Calaxin-deficient OADs remain tethered to DMT through other docking complex components. Recombinant Calaxin can autonomously rescue the deficient docking complex structure and OAD instability, demonstrating a discrete stabilizing role distinct from that of Armc4.\",\n      \"method\": \"Zebrafish calaxin and armc4 mutants, cryo-electron tomography of spermatozoa axonemes, recombinant Calaxin rescue experiment\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — cryo-electron tomography structural analysis combined with recombinant protein rescue, multiple mutant comparisons, single rigorous study with multiple orthogonal methods\",\n      \"pmids\": [\"37057896\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"EFCAB1 overexpression in lung adenocarcinoma cell lines (A549, PC9) inhibits cell proliferation, migration, and invasion while promoting apoptosis. DNMT3B mRNA expression was elevated in EFCAB1-low cell lines, suggesting a functional relationship between EFCAB1 levels and DNMT3B expression.\",\n      \"method\": \"EFCAB1 overexpression in A549 and PC9 cell lines; CCK-8 proliferation assay, migration/invasion assays, colony formation assay, apoptosis assay; qPCR for DNMT expression\",\n      \"journal\": \"Journal of clinical laboratory analysis\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, cell-line overexpression with phenotypic readouts but no defined molecular mechanism or pathway placement; DNMT3B relationship is correlative\",\n      \"pmids\": [\"34904288\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"CLXN (Calaxin/EFCAB1/ODAD5) is a Ca²⁺-binding protein that functions as a component of the outer dynein arm docking complex (ODAD5) in motile cilia, where it stabilizes the attachment of outer arm dynein onto ciliary doublet microtubules; loss of CLXN causes primary ciliary dyskinesia with selective defects in distal ODA assembly and disrupted nodal cilia formation, while its localization to axonemes depends on the integrity of the broader ODA-docking complex.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"CLXN (Calaxin/EFCAB1/ODAD5) is a Ca²⁺-binding protein essential for the function of motile cilia and flagella in vertebrates [#0]. It operates as the ODAD5 component of the outer dynein arm (ODA)-docking complex, where it stabilizes the attachment of outer arm dynein onto ciliary doublet microtubules; cryo-electron tomography shows that loss of Calaxin causes only partial OAD loss because the dynein remains tethered through other docking-complex subunits, and recombinant Calaxin autonomously rescues the deficient docking structure, establishing a discrete stabilizing role distinct from that of Armc4 [#2]. CLXN's incorporation into the axoneme depends on the integrity of the broader docking complex, as it is undetectable when ODAD1–ODAD4 are defective [#1]. Loss of CLXN function produces primary ciliary dyskinesia: in humans, pathogenic variants cause selective failure of distal ODA assembly with absence of DNAH5, DNAI1, and DNAI2 from distal axonemes and mislocalization of DNAH9 [#1], while mouse and zebrafish nulls show hydrocephalus, situs inversus, and abnormal ciliary/flagellar beating with preserved 9+2 axonemal structure but disrupted 9+0 nodal cilia [#0].\",\n  \"teleology\": [\n    {\n      \"year\": 2019,\n      \"claim\": \"Established that Calaxin is functionally required for motile cilia and flagella in vertebrates, answering whether this Ca²⁺-binding protein has an essential ciliary role in vivo.\",\n      \"evidence\": \"Germline Efcab1-null mice and zebrafish knockouts analyzed by TEM and high-speed video microscopy of cilia/flagella\",\n      \"pmids\": [\"31240264\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular partners and biochemical mechanism not defined\", \"Preserved 9+2 structure left the structural basis of motility defect unexplained\", \"Why nodal (9+0) cilia are selectively disrupted not resolved\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Placed CLXN within the ODA-docking complex as ODAD5 and defined its molecular consequence, answering where in the cilia assembly pathway the protein acts.\",\n      \"evidence\": \"Clinical exome sequencing, immunofluorescence and TEM of patient ciliary axonemes, and planaria RNAi knockdown\",\n      \"pmids\": [\"36727596\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Direct binding interfaces between CLXN and other ODAD subunits not mapped\", \"Role of Ca²⁺ binding in docking-complex function not tested\", \"Mechanism of selective distal versus proximal ODA assembly unresolved\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Resolved the discrete structural function of Calaxin in stabilizing OAD docking, distinguishing it from Armc4 and demonstrating autonomous sufficiency.\",\n      \"evidence\": \"Cryo-electron tomography of zebrafish calaxin and armc4 mutant spermatozoa axonemes with recombinant Calaxin rescue\",\n      \"pmids\": [\"37057896\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Atomic-level interactions within the docking complex not determined\", \"How Ca²⁺ modulates the stabilizing activity not addressed\", \"Stoichiometry of Calaxin within the complex not defined\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Reported a candidate non-ciliary role for EFCAB1 as a suppressor of lung adenocarcinoma cell growth, raising whether the protein has functions outside motile cilia.\",\n      \"evidence\": \"EFCAB1 overexpression in A549 and PC9 cell lines with proliferation, migration, invasion, apoptosis assays and qPCR for DNMT3B\",\n      \"pmids\": [\"34904288\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Overexpression phenotype not validated by loss-of-function\", \"DNMT3B relationship is correlative with no mechanism\", \"Connection to the established ciliary function unknown\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How Ca²⁺ binding by CLXN regulates outer dynein arm docking and ciliary beat, and the structural basis of its interaction with other ODAD subunits, remain open.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No atomic structure of CLXN within the docking complex\", \"Functional role of Ca²⁺ sensing in docking not tested\", \"Direct binding partners within the complex not biochemically mapped\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [2]},\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005929\", \"supporting_discovery_ids\": [0, 1, 2]},\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1852241\", \"supporting_discovery_ids\": [1, 2]},\n      {\"term_id\": \"R-HSA-1643685\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"complexes\": [\"outer dynein arm-docking complex (ODA-DC)\"],\n    \"partners\": [\"ODAD1\", \"ODAD2\", \"ODAD3\", \"ODAD4\", \"ARMC4\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":4,"faith_total":4,"faith_pct":100.0}}