id: G5EFW7
gene_symbol: daf-10
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:6239
  label: Caenorhabditis elegans
description: >-
  DAF-10 is the Caenorhabditis elegans ortholog of human IFT122, a core subunit
  of intraflagellar transport complex A (IFT-A). It is a large (1192 aa) WD40
  β-propeller plus tetratricopeptide-repeat (TPR) solenoid scaffold with a
  C-terminal zinc-ribbon and no catalytic domain, expressed in ciliated sensory
  neurons and shuttling along the axoneme of the non-motile sensory cilium at the
  same rate as IFT-B proteins. As part of IFT-A, DAF-10 is required for retrograde
  (ciliary tip-to-base) intraflagellar transport powered by cytoplasmic dynein-2,
  and thereby for assembly and maintenance of the sensory-cilium axoneme and for
  import of ciliary membrane cargo such as G protein-coupled receptors. Loss of
  DAF-10 produces structurally defective, disorganized sensory cilia with the
  characteristic IFT-A retrograde-defect signature (accumulation of IFT-B/OSM-6
  material in the ciliary endings), together with dye-filling and chemotaxis
  defects. Because worm sensory cilia detect environmental cues, daf-10 mutants
  are dauer-formation-defective (the origin of the gene name, abnormal DAuer
  Formation) and show altered sensory modulation of insulin/IGF and TGF-β
  signaling. IFT122 mutations cause human ciliopathies (cranioectodermal dysplasia
  / Sensenbrenner syndrome), underscoring a conserved role in cilium biogenesis.
references:
  - id: GO_REF:0000024
    title: Manual transfer of experimentally-verified manual GO annotation data to orthologs
      by curator judgment of sequence similarity
    findings: []
  - id: GO_REF:0000033
    title: Annotation inferences using phylogenetic trees
    findings: []
  - id: GO_REF:0000044
    title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location
      vocabulary mapping, accompanied by conservative changes to GO terms applied by
      UniProt
    findings: []
  - id: GO_REF:0000120
    title: Combined Automated Annotation using Multiple IEA Methods
    findings: []
  - id: PMID:16648645
    title: The molecular identities of the Caenorhabditis elegans intraflagellar transport
      genes dyf-6, daf-10 and osm-1.
    findings: []
    reference_review:
      relevance: HIGH
      correctness: VERIFIED
      review_notes: >-
        Founding molecular-identity paper for daf-10: the daf-10 product contains WD
        and WAA repeats and (per the full text, which the automated validator can only
        access as the PubMed abstract) is classified with che-11 as an IFT complex A
        component. Loss of daf-10/che-11 gives thicker-than-wild-type OSM-6::GFP
        patches in the ciliary endings (IFT-B accumulation), the classic IFT-A
        retrograde-defect signature. Supports the IFT-A membership and non-motile
        cilium assembly annotations.
  - id: PMID:28479320
    title: Dynein-Driven Retrograde Intraflagellar Transport Is Triphasic in C. elegans
      Sensory Cilia.
    findings: []
    reference_review:
      relevance: HIGH
      correctness: VERIFIED
      review_notes: >-
        Affinity purification / mass spectrometry defined the worm IFT-A complex
        (che-11, daf-10, dyf-2, ift-139, ift-43, ifta-1); basis for the ComplexPortal
        (CPX-1289) NAS annotations placing DAF-10 in IFT-A and in retrograde
        transport. Cached record is abstract-only (full_text_available: false); the
        abstract confirms the affinity-purification definition of IFT-A subunits but
        does not name daf-10, so the daf-10 datum rests on the full text / UniProt
        SUBUNIT curation.
  - id: PMID:21124868
    title: Localization of a guanylyl cyclase to chemosensory cilia requires the novel
      ciliary MYND domain protein DAF-25.
    findings: []
    reference_review:
      relevance: HIGH
      correctness: VERIFIED
      review_notes: >-
        Full text available and read. States that daf-10/IFT122 mutations disrupt
        ciliogenesis and genetically suppress the daf-25 dauer-constitutive
        phenotype, confirming daf-10 = IFT122 and its ciliogenesis role, and grounding
        the IGI regulation-of-dauer annotation (genetic interaction with daf-25).
  - id: PMID:1732156
    title: Genetic analysis of chemosensory control of dauer formation in Caenorhabditis
      elegans.
    findings: []
    reference_review:
      relevance: HIGH
      correctness: VERIFIED
      review_notes: >-
        Cached record is abstract-only. Classic epistasis study placing daf-10 among
        the dauer-defective genes whose mutations cause structurally defective
        chemosensory cilia; supports both the cilium-assembly (structural) role and
        the downstream dauer-formation role.
  - id: PMID:6583682
    title: 'A pheromone-induced developmental switch in Caenorhabditis elegans: Temperature-sensitive
      mutants reveal a wild-type temperature-dependent process.'
    findings: []
    reference_review:
      relevance: MEDIUM
      correctness: VERIFIED
      review_notes: >-
        Cached record is abstract-only; the abstract foregrounds daf-4/daf-7
        dauer-constitutive genes and states that dauer-defective mutants fail to
        respond to added pheromone. WormBase attaches a specific daf-10 allele
        (WBVar00143964) IMP for positive regulation of dauer larval development; the
        dauer role is well-established (gene name = abnormal DAuer Formation) but is a
        downstream sensory consequence of the ciliary defect, not a core molecular
        function.
  - id: PMID:24646679
    title: Diverse cell type-specific mechanisms localize G protein-coupled receptors
      to Caenorhabditis elegans sensory cilia.
    findings: []
    reference_review:
      relevance: MEDIUM
      correctness: VERIFIED
      review_notes: >-
        Cached record is abstract-only; describes the proteins required to localize
        GPCRs to AWB/ASK sensory cilia. daf-10 is not named in the abstract, but the
        WormBase IMP (receptor localization to non-motile cilium) reflects the
        full-text result; consistent with the established IFT-A requirement for
        ciliary import of membrane GPCRs.
  - id: PMID:27623382
    title: A Conserved Role for Girdin in Basal Body Positioning and Ciliogenesis.
    findings: []
    reference_review:
      relevance: LOW
      correctness: UNVERIFIED
      review_notes: >-
        Cached record is abstract-only; the abstract is about Girdin and basal-body
        positioning and does not name daf-10. The UniProt IDA (ciliary basal body)
        rests on the full text (DAF-10 likely used/scored as a ciliary-base marker).
        Basal-body/ciliary-base localization is biologically consistent with an IFT-A
        subunit (IFT proteins dock at transition fibres before axonemal entry), so
        the annotation is retained, but the daf-10-specific datum could not be
        independently verified from the cached abstract.
  - id: PMID:11381260
    title: Regulation of the Caenorhabditis elegans longevity protein DAF-16 by insulin/IGF-1
      and germline signaling.
    findings: []
    reference_review:
      relevance: LOW
      correctness: VERIFIED
      review_notes: >-
        Cached record is abstract-only. Establishes that sensory neurons and germline
        activity regulate DAF-16 nuclear accumulation systemically. Grounds the IGI
        regulation-of-insulin-receptor-signaling annotation, but the effect of daf-10
        is an indirect, whole-organism sensory input into insulin/IGF signaling, not a
        molecular function of an IFT-A structural subunit.
existing_annotations:
  - term:
      id: GO:0061512
      label: protein localization to cilium
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    qualifier: involved_in
    review:
      summary: >-
        As an IFT-A subunit, DAF-10 transports and localizes protein cargo along the
        ciliary axoneme; loss of daf-10 disrupts the distribution of IFT-B (OSM-6)
        material in the ciliary endings.
      action: ACCEPT
      reason: >-
        Core process. Phylogenetic inference agrees with the founding paper, which
        established daf-10 as an IFT gene mediating the bidirectional movement of
        particles along the ciliary axoneme (i.e. protein localization within the
        cilium).
      supported_by:
        - reference_id: PMID:16648645
          supporting_text: Some genes in this category are known to be required for intraflagellar
            transport (IFT), which is the bidirectional movement of raft-like particles
            along the axonemes of cilia and flagella
  - term:
      id: GO:0035721
      label: intraciliary retrograde transport
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    qualifier: involved_in
    review:
      summary: >-
        As a core IFT-A subunit, DAF-10 is required for retrograde (tip-to-base)
        intraflagellar transport, the defining function of IFT-A.
      action: ACCEPT
      reason: >-
        Represents the core biological process of the gene. Phylogenetic inference is
        corroborated by the IFT-A/retrograde-defect phenotype of daf-10 mutants and by
        mass-spec placement of DAF-10 in the worm IFT-A complex.
      supported_by:
        - reference_id: PMID:28479320
          supporting_text: Cytoplasmic dynein-2 powers retrograde intraflagellar transport
            that is essential for cilium formation and maintenance
  - term:
      id: GO:0097730
      label: non-motile cilium
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    qualifier: is_active_in
    review:
      summary: >-
        DAF-10 acts within the worm's non-motile sensory cilia, where it shuttles
        along the axoneme as part of IFT-A.
      action: ACCEPT
      reason: >-
        Core localization, accurately specific to the worm's non-motile sensory cilia.
        Phylogenetic inference agrees with the direct ciliary localization of DAF-10
        (IFT shuttling in amphid/phasmid cilia) and with the mutant cilia phenotype.
  - term:
      id: GO:1905515
      label: non-motile cilium assembly
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    qualifier: involved_in
    review:
      summary: >-
        IFT-A/retrograde transport by DAF-10 is required to build and maintain the
        non-motile sensory-cilium axoneme; loss of daf-10 gives structurally defective
        cilia.
      action: ACCEPT
      reason: >-
        Core process, accurately specific for the worm's non-motile sensory cilia.
        Phylogenetic inference is corroborated by the ciliogenesis defect of daf-10
        mutants.
      supported_by:
        - reference_id: PMID:21124868
          supporting_text: daf-10/IFT122 mutations (which disrupt ciliogenesis)
  - term:
      id: GO:0030991
      label: intraciliary transport particle A
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    qualifier: part_of
    review:
      summary: >-
        DAF-10 is a core subunit of the IFT-A complex, established by orthology to
        IFT122 and by direct mass-spec identification in the worm IFT-A complex.
      action: ACCEPT
      reason: >-
        Core complex membership. Phylogenetic inference agrees with the experimental
        (NAS/mass-spec, ISS) IFT-A assignments; the founding paper notes that the
        WAA-repeat architecture shared by daf-10 is characteristic of IFT particle
        components.
      supported_by:
        - reference_id: PMID:16648645
          supporting_text: The daf-10 and osm-1 gene products resemble each other and
            contain WD and WAA repeats
  - term:
      id: GO:0005929
      label: cilium
    evidence_type: IEA
    original_reference_id: GO_REF:0000044
    qualifier: located_in
    review:
      summary: >-
        Electronic (UniProt SubCell) assertion of ciliary localization, redundant
        with the more specific non-motile cilium annotation.
      action: ACCEPT
      reason: >-
        Correct location; consistent with the direct evidence that DAF-10 shuttles
        along sensory cilia, albeit less specific than the non-motile cilium term.
  - term:
      id: GO:0060271
      label: cilium assembly
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    qualifier: involved_in
    review:
      summary: >-
        Electronic (ARBA/InterPro) annotation of the IFT-A cilium-assembly role,
        redundant with the experimental IGI/IMP and phylogenetic annotations.
      action: ACCEPT
      reason: >-
        Correct core process; consistent with the ciliogenesis defect of daf-10
        mutants, though less specific than the non-motile cilium assembly term.
  - term:
      id: GO:0005929
      label: cilium
    evidence_type: NAS
    original_reference_id: PMID:28479320
    qualifier: located_in
    review:
      summary: >-
        ComplexPortal (CPX-1289) NAS assertion of ciliary localization for the IFT-A
        complex, based on the mass-spec study of worm retrograde IFT.
      action: ACCEPT
      reason: >-
        Correct core localization, consistent with the direct ciliary shuttling of
        DAF-10.
  - term:
      id: GO:0030991
      label: intraciliary transport particle A
    evidence_type: NAS
    original_reference_id: PMID:28479320
    qualifier: part_of
    review:
      summary: >-
        ComplexPortal NAS annotation placing DAF-10 in the IFT-A complex, based on
        affinity purification / mass spectrometry of the worm IFT-A complex (che-11,
        daf-10, dyf-2, ift-139, ift-43, ifta-1).
      action: ACCEPT
      reason: >-
        Core complex membership, experimentally grounded (mass-spec definition of the
        worm IFT-A complex, which includes DAF-10).
      supported_by:
        - reference_id: PMID:28479320
          supporting_text: our affinity purification and genetic analyses show that IFT-A
  - term:
      id: GO:0035721
      label: intraciliary retrograde transport
    evidence_type: NAS
    original_reference_id: PMID:28479320
    qualifier: involved_in
    review:
      summary: >-
        ComplexPortal NAS annotation of the IFT-A retrograde-transport role.
      action: ACCEPT
      reason: >-
        Core process, consistent with the experimental and phylogenetic evidence for
        DAF-10 as a retrograde IFT-A subunit.
      supported_by:
        - reference_id: PMID:28479320
          supporting_text: Cytoplasmic dynein-2 powers retrograde intraflagellar transport
            that is essential for cilium formation and maintenance
  - term:
      id: GO:0060271
      label: cilium assembly
    evidence_type: NAS
    original_reference_id: PMID:28479320
    qualifier: involved_in
    review:
      summary: >-
        ComplexPortal NAS annotation of the cilium-assembly role of IFT-A.
      action: ACCEPT
      reason: >-
        Correct; downstream outcome of the IFT-A transport function and consistent
        with the ciliogenesis defect of daf-10 mutants.
  - term:
      id: GO:0030991
      label: intraciliary transport particle A
    evidence_type: ISS
    original_reference_id: GO_REF:0000024
    qualifier: part_of
    review:
      summary: >-
        Sequence-similarity (ISS) transfer of IFT-A membership from the human ortholog
        IFT122 (Q9HBG6).
      action: ACCEPT
      reason: >-
        Core complex membership; the ISS to human IFT122 agrees with the direct
        mass-spec IFT-A assignment in the worm.
  - term:
      id: GO:0036064
      label: ciliary basal body
    evidence_type: IDA
    original_reference_id: PMID:27623382
    qualifier: located_in
    review:
      summary: >-
        Direct-assay assertion of DAF-10 at the ciliary basal body, from a study of
        Girdin-dependent basal-body positioning and ciliogenesis.
      action: ACCEPT
      reason: >-
        Biologically consistent location: IFT-A proteins concentrate at the ciliary
        base / transition-fibre region before axonemal entry. Retained as a genuine
        location per repo guidance not to overrule an experimental IDA; the cached
        record is abstract-only and does not name daf-10, so the datum is deferred to
        the curator's full-text reading (see reference_review). A secondary/base
        localization rather than the core axonemal-transport function.
  - term:
      id: GO:0061065
      label: regulation of dauer larval development
    evidence_type: IGI
    original_reference_id: PMID:21124868
    qualifier: involved_in
    review:
      summary: >-
        Genetic interaction with daf-25/Ankmy2: daf-10 loss (disrupting ciliogenesis)
        suppresses the daf-25 dauer-constitutive phenotype, implicating daf-10 in the
        chemosensory control of dauer formation.
      action: KEEP_AS_NON_CORE
      reason: >-
        Valid genetic-interaction phenotype, but a downstream consequence of the
        ciliary/IFT defect (functional chemosensory cilia are required to sense the
        dauer cues), not a core molecular function of an IFT-A structural subunit.
      supported_by:
        - reference_id: PMID:21124868
          supporting_text: daf-10/IFT122 mutations (which disrupt ciliogenesis)
  - term:
      id: GO:0060271
      label: cilium assembly
    evidence_type: IGI
    original_reference_id: PMID:1732156
    qualifier: involved_in
    review:
      summary: >-
        daf-10 is among the dauer-defective genes whose mutations cause structurally
        defective chemosensory cilia, implicating it in building the sensory cilium.
      action: ACCEPT
      reason: >-
        Core process; the cilium-structure defect of daf-10 mutants directly supports
        a requirement in ciliary assembly/maintenance.
      supported_by:
        - reference_id: PMID:1732156
          supporting_text: structurally defective chemosensory cilia
  - term:
      id: GO:0061066
      label: positive regulation of dauer larval development
    evidence_type: IMP
    original_reference_id: PMID:6583682
    qualifier: involved_in
    review:
      summary: >-
        daf-10 is required for dauer formation (loss-of-function is dauer-defective),
        so it positively regulates entry into the dauer larval stage; the classic
        dauer-pheromone-switch study frames dauer-defective mutants as unresponsive to
        pheromone.
      action: KEEP_AS_NON_CORE
      reason: >-
        Well-established phenotype (the gene is named for abnormal DAuer Formation),
        but a downstream sensory consequence of the ciliary defect rather than a core
        molecular function. The cached record is abstract-only and does not name
        daf-10; retained per guidance not to overrule the WormBase IMP.
      supported_by:
        - reference_id: PMID:6583682
          supporting_text: Dauer-defective mutants fail to respond to added pheromone
  - term:
      id: GO:0097500
      label: receptor localization to non-motile cilium
    evidence_type: IMP
    original_reference_id: PMID:24646679
    qualifier: involved_in
    review:
      summary: >-
        daf-10 is required for correct ciliary localization of G protein-coupled
        receptors in sensory neurons, reflecting the IFT-A role in ciliary import of
        membrane cargo.
      action: ACCEPT
      reason: >-
        A specific, well-grounded manifestation of IFT-A function: import/retention of
        ciliary membrane GPCRs depends on intact IFT. The cached record is
        abstract-only and does not name daf-10; retained per guidance not to overrule
        the WormBase IMP and because the requirement is consistent with the
        established IFT-A role in ciliary GPCR trafficking.
      supported_by:
        - reference_id: PMID:24646679
          supporting_text: localize GPCRs to the cilia of the AWB and ASK sensory neuron types
  - term:
      id: GO:1905515
      label: non-motile cilium assembly
    evidence_type: IMP
    original_reference_id: PMID:16648645
    qualifier: involved_in
    review:
      summary: >-
        Mutant analysis in the founding paper: daf-10 (complex A) is required for
        proper sensory-cilium structure; loss abnormally redistributes OSM-6::GFP in
        the ciliary endings.
      action: ACCEPT
      reason: >-
        Core process, accurately specific for the worm's non-motile sensory cilia and
        supported by the mutant phenotype. daf-10 is one of the IFT genes cloned in
        this paper whose loss perturbs sensory-cilium structure.
      supported_by:
        - reference_id: PMID:16648645
          supporting_text: The daf-10 and osm-1 gene products resemble each other and
            contain WD and WAA repeats
  - term:
      id: GO:0046626
      label: regulation of insulin receptor signaling pathway
    evidence_type: IGI
    original_reference_id: PMID:11381260
    qualifier: involved_in
    review:
      summary: >-
        Sensory (ciliated) neurons modulate DAF-16/insulin-IGF signaling
        systemically; daf-10 contributes to this via a genetic interaction, reflecting
        the sensory input of the ciliary system into insulin signaling.
      action: KEEP_AS_NON_CORE
      reason: >-
        Indirect, whole-organism sensory-modulation effect (ciliary sensory neurons
        influence DAF-16 nuclear localization), not a molecular function of an IFT-A
        structural subunit. Retained as a legitimate genetic-interaction phenotype but
        marked non-core/downstream.
      supported_by:
        - reference_id: PMID:11381260
          supporting_text: both sensory neurons and germline activity regulate DAF-16
            accumulation in nuclei
core_functions:
  - description: >-
      Structural constituent of intraflagellar transport complex A (IFT-A) that
      drives retrograde (ciliary tip-to-base) intraflagellar transport along the
      non-motile sensory cilium. As the IFT122 ortholog, DAF-10 has no catalytic
      activity; it acts as a WD40/TPR/Zn-ribbon scaffold within IFT-A that, with
      cytoplasmic dynein-2, returns IFT particles and turnover products from the
      ciliary tip to the base.
    molecular_function:
      id: GO:0005198
      label: structural molecule activity
    directly_involved_in:
      - id: GO:0035721
        label: intraciliary retrograde transport
      - id: GO:0042073
        label: intraciliary transport
    locations:
      - id: GO:0097730
        label: non-motile cilium
    in_complex:
      id: GO:0030991
      label: intraciliary transport particle A
    supported_by:
      - reference_id: PMID:16648645
        supporting_text: The daf-10 and osm-1 gene products resemble each other and
          contain WD and WAA repeats
      - reference_id: PMID:28479320
        supporting_text: IFT-139 and IFT-43 function redundantly to promote dynein-2 motility
  - description: >-
      Required for assembly and maintenance of the non-motile sensory cilium and for
      ciliary import of membrane cargo. IFT-A function via DAF-10 is needed to build
      and maintain the ciliary axoneme, to keep IFT-B/ciliary proteins correctly
      distributed, and to localize signaling receptors (GPCRs) to the ciliary
      compartment; loss of DAF-10 disrupts ciliogenesis.
    directly_involved_in:
      - id: GO:0060271
        label: cilium assembly
      - id: GO:1905515
        label: non-motile cilium assembly
      - id: GO:0061512
        label: protein localization to cilium
    locations:
      - id: GO:0097730
        label: non-motile cilium
    supported_by:
      - reference_id: PMID:21124868
        supporting_text: daf-10/IFT122 mutations (which disrupt ciliogenesis)
      - reference_id: PMID:1732156
        supporting_text: structurally defective chemosensory cilia
knowledge_gaps:
  - gap_statement: >-
      DAF-10 has no molecular-function annotation and no GO term that can express
      one. Its role is to be a structural constituent of the IFT-A particle, but GO
      has no "structural constituent of the intraflagellar transport particle"
      molecular-function term, so the gene reads as MF-dark despite a well-understood
      cellular and process-level role.
    boundary: >-
      It is firmly established that DAF-10 = IFT122 is a WD40+TPR+Zn-ribbon
      scaffolding subunit of IFT-A with no catalytic domain, required for retrograde
      IFT and cilium assembly. What is missing is a molecular-function
      representation: the worm GOA record carries only cellular-component and
      biological-process terms and no molecular_function annotation at all.
    gap_kind:
      - ONTOLOGY
      - CURATION
    dark_aspect: MF_DARK
    status: OPEN
    significance: >-
      This is the canonical "structural subunit" ontology gap: a mechanistically
      well-understood protein that cannot be annotated with an informative MF term,
      contributing to apparent molecular-function darkness across the IFT/ciliopathy
      gene set (the same gap affects dyf-2/WDR19 and other IFT-A/IFT-B subunits).
    resolution: >-
      Develop/adopt a molecular-function term for a structural constituent of the IFT
      particle (analogous to "structural constituent of ribosome"), then annotate
      DAF-10 (and other IFT-A/IFT-B core subunits) to it.
    provenance:
      - reference_id: PMID:16648645
        supporting_text: The daf-10 and osm-1 gene products resemble each other and
          contain WD and WAA repeats
        reference_section_type: ABSTRACT
    proposed_terms:
      - proposed_name: structural constituent of intraflagellar transport particle
        proposed_definition: >-
          The action of a protein that contributes to the structural integrity of an
          intraflagellar transport (IFT) particle (IFT-A or IFT-B subcomplex), for
          example by acting as a WD40/TPR scaffold that holds core IFT subunits
          together and enables their bidirectional transport along the ciliary
          axoneme, without itself catalyzing a biochemical reaction.
        proposed_parent:
          id: GO:0005198
          label: structural molecule activity
  - gap_statement: >-
      The subunit-resolved architecture of the C. elegans IFT-A complex, and which
      of DAF-10's ciliary functions (retrograde transport, axoneme assembly, GPCR
      import) are directly and specifically mediated by DAF-10 versus emerging from
      IFT-A as a whole, are not dissected. DAF-10's direct IFT-A neighbor contacts
      are inferred from cross-species orthology and worm mass-spec composition, not
      resolved structurally.
    boundary: >-
      The worm IFT-A composition (che-11, daf-10, dyf-2, ift-139, ift-43, ifta-1) is
      known from affinity purification / mass spectrometry, and daf-10 loss produces
      the IFT-A retrograde-defect signature (IFT-B accumulation in ciliary endings).
      What is not known is the position of DAF-10/IFT122 within a solved IFT-A
      structure, its direct binding partners in the worm, and any DAF-10-specific
      (as opposed to complex-level) contribution to cargo selection.
    gap_kind:
      - BIOLOGY
    dark_aspect: RESIDUAL_SUBGAP
    status: OPEN
    significance: >-
      IFT-A subunit architecture determines how retrograde IFT is organized and how
      ciliopathy-causing IFT122 mutations perturb it; a DAF-10-resolved structure and
      separation-of-function alleles would explain which ciliary phenotypes are
      directly attributable to DAF-10.
    resolution: >-
      Cryo-EM of the worm IFT-A complex with DAF-10/IFT122 assigned, plus
      structure-guided separation-of-function alleles scored in vivo for retrograde
      IFT (kymography of IFT-B markers), cilium length, and ciliary GPCR localization.
    provenance:
      - reference_id: PMID:28479320
        supporting_text: IFT-139 and IFT-43 function redundantly to promote dynein-2 motility
        reference_section_type: ABSTRACT
proposed_new_terms:
  - proposed_name: structural constituent of intraflagellar transport particle
    proposed_definition: >-
      The action of a protein that contributes to the structural integrity of an
      intraflagellar transport (IFT) particle (IFT-A or IFT-B subcomplex), for
      example by acting as a WD40/TPR scaffold that holds core IFT subunits together
      and enables their bidirectional transport along the ciliary axoneme, without
      itself catalyzing a biochemical reaction.
    proposed_parent:
      id: GO:0005198
      label: structural molecule activity
suggested_questions:
  - question: What is the subunit-resolved architecture of the C. elegans IFT-A
      complex, and which IFT-A subunits does DAF-10/IFT122 directly contact?
    experts:
      - Ou G
  - question: Which ciliary phenotypes (retrograde IFT, axoneme assembly, ciliary GPCR
      import) are specifically attributable to DAF-10 versus the IFT-A complex as a whole?
    experts:
      - Sengupta P
suggested_experiments:
  - hypothesis: DAF-10/IFT122 occupies a defined position within an IFT-A scaffold that
      can be resolved structurally.
    description: >-
      Affinity-purify or reconstitute the worm IFT-A complex and determine its
      architecture by cryo-EM, assigning DAF-10/IFT122 and its direct neighbors and
      testing whether ciliopathy-mimicking substitutions perturb specific interfaces.
    experiment_type: structural biology
  - hypothesis: DAF-10 makes a separable contribution to ciliary GPCR import distinct
      from its role in bulk retrograde IFT.
    description: >-
      Generate structure-guided separation-of-function alleles of daf-10 and score, in
      vivo, retrograde IFT (kymography of IFT-B markers), cilium length, and ciliary
      localization of tagged GPCRs in AWB/ASK neurons, to test whether cargo-import and
      transport functions can be genetically uncoupled.
    experiment_type: structure-function mutagenesis
tags:
  - caeel-ciliopathy