id: A0A8M9QG43
gene_symbol: dnajc6
taxon:
  id: NCBITaxon:7955
  label: Danio rerio
status: COMPLETE
description: >-
  The auxilin-family architecture supports a noncatalytic PTEN-like domain. Participation in dephosphorylation
  is not established by that fold.
source_documents:
  - genes/DANRE/A0A8M9QG43/A0A8M9QG43-uniprot.txt
  - genes/DANRE/A0A8M9QG43/A0A8M9QG43-goa.tsv
  - publications/PMID_20826345.md
  - genes/DANRE/A0A8M9QG43/A0A8M9QG43-hypotheses/prediction-dephosphorylation/openscientist.md
predictions:
  - source_method: ProtNLM2
    source_version: UniProt 2024_06 pilot
    predicted_term:
      id: GO:0016311
      label: dephosphorylation
    predicted_term_type: GO_BP
    review:
      assessment: NPI
      confidence_score: 0
      error_type: PSEUDOENZYME_OVERANNOTATION
      summary: >-
        The target has the PTEN-like, C2, and J-domain architecture of auxilin/DNAJC6, but the PTEN-like
        region is a conserved pseudophosphatase rather than an active phosphatase. Structural work on
        bovine auxilin shows that this region lacks phosphatase activity and instead participates in
        membrane binding (PMID:20826345), and the focused sequence comparison found the dead C-X3-R
        P-loop across human, mouse, and zebrafish DNAJC6 instead of PTEN's active C-X5-R loop. The predicted
        dephosphorylation biological-process term is an over-propagation from a catalytic PTEN-like ancestor:
        no evidence establishes that dnajc6 itself catalyzes or directly executes a dephosphorylation
        step.
      supported_by:
        - reference_id: file:DANRE/A0A8M9QG43/A0A8M9QG43-uniprot.txt
          supporting_text: >-
            ID   A0A8M9QG43_DANRE        Unreviewed;       974 AA. ... DR   InterPro; IPR029023; Tensin_phosphatase.
            ... DR   PANTHER; PTHR23172:SF4; TYROSINE-PROTEIN PHOSPHATASE AUXILIN-RELATED; 1. ... FT   DOMAIN          109..276
            ... FT                   /note="Phosphatase tensin-type" ... FT   DOMAIN          282..417
            ... FT                   /note="C2 tensin-type" ... FT   DOMAIN          910..974 ... FT                   /note="J"
        - reference_id: PMID:20826345
          supporting_text: >-
            A change in the structure of the P loop accounts for the lack of phosphatase activity
        - reference_id: file:DANRE/A0A8M9QG43/A0A8M9QG43-hypotheses/prediction-dephosphorylation/openscientist.md
          supporting_text: >-
            No `C.{5}R` match in auxilin.
references:
  - id: file:DANRE/A0A8M9QG43/A0A8M9QG43-uniprot.txt
    title: A0A8M9QG43-uniprot.txt
  - id: PMID:20826345
    title: Structure of the PTEN-like region of auxilin, a detector of clathrin-coated vesicle
      budding.
  - id: file:DANRE/A0A8M9QG43/A0A8M9QG43-hypotheses/prediction-dephosphorylation/openscientist.md
    title: openscientist.md