Use of the ND evidence code for Gene Ontology (GO) terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Identification of CHE-13, a novel intraflagellar transport protein required for cilia formation.
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CHE-13 (F59C6.7) is required for cilia assembly and its function is disrupted in che-13 ciliogenic mutants; fluorescent-tagged CHE-13 concentrates at the ciliary base and moves along the axoneme like an IFT protein, and loss of che-13 mislocalizes the IFT-B proteins OSM-5 and OSM-6, placing CHE-13 in IFT complex B.
"loss of che-13 differentially affects the localization of two known IFT complex B proteins, OSM-5 and OSM-6, implying that CHE-13 functions as part of this complex."
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che-13 expression is controlled by the RFX transcription factor DAF-19, like other IFT-B genes.
"expression of che-13 (F59C6.7/9) is regulated by the RFX-type transcription factor DAF-19"
Caenorhabditis elegans DYF-2, an orthologue of human WDR19, is a component of the intraflagellar transport machinery in sensory cilia.
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Study of the IFT machinery in which che-13 mutant analysis contributed to the WormBase IMP that che-13 is required for proper localization of IFT proteins.
"The intraflagellar transport (IFT) machinery required to build functional cilia consists of a multisubunit complex"
Sensory ciliogenesis in Caenorhabditis elegans: assignment of IFT components into distinct modules based on transport and phenotypic profiles.
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The C. elegans IFT machinery is organized into modules, including an IFT subcomplex B module to which che-13 belongs, based on in vivo transport and phenotypic profiles.
"the C. elegans IFT machinery has a modular design, consisting of modules IFT-subcomplex A, IFT-subcomplex B, and a BBS protein complex"
Genetic analysis of chemosensory control of dauer formation in Caenorhabditis elegans.
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che-13 is among the cilium-structure genes whose mutation causes structurally defective chemosensory cilia, placing it at a single step in the dauer-formation epistasis pathway.
"Dauer-defective mutations in nine genes cause structurally defective chemosensory cilia, thereby blocking chemosensation."
Functional redundancy of the B9 proteins and nephrocystins in Caenorhabditis elegans ciliogenesis.
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Study of B9/nephrocystin ciliogenesis in which che-13 was used as an IFT/ciliary reference; source of a WormBase axoneme IDA for che-13.
"the C. elegans B9 proteins form a complex that localizes to the base of cilia"
The BBSome controls IFT assembly and turnaround in cilia.
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Establishes that the IFT particle (including IFT-B) is assembled at the ciliary base before entering the cilium; used here as the MGI reference for che-13 ciliary basal body localization.
"the BBSome (refs 3, 4), a group of conserved proteins affected in human Bardet-Biedl syndrome"
Mutant sensory cilia in the nematode Caenorhabditis elegans.
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che-13(e1805) mutants have normal ciliary transition zones but severely shortened axonemes with ectopic doublet microtubules, establishing CHE-13 as required for axoneme (cilium) assembly rather than transition-zone formation, and they are dye-filling / chemosensory defective.
"The cilia in che-13 (e1805), osm-1 (p808), osm-5 (p813), and osm-6 (p811) mutants have normal transition zones and severely shortened axonemes."
Dynein-Driven Retrograde Intraflagellar Transport Is Triphasic in C. elegans Sensory Cilia.
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Ciliary entry of dynein-2 requires an intact IFT-B complex (of which CHE-13 is a component); this study is the ComplexPortal source (CPX-1290) for che-13 IFT-B/IFT particle B membership, intraciliary transport, cilium assembly and ciliary localization.
"Disruption of the dynein-2 tail domain, light intermediate chain, or intraflagellar transport (IFT)-B complex abolishes dynein-2's ciliary localization"