id: A4UZ54
gene_symbol: Pld
taxon:
  id: NCBITaxon:7227
  label: Drosophila melanogaster
status: COMPLETE
description: Lipid catabolism is supported but already implied by the characterized phospholipase reaction;
  cytoplasm is supported and less precise than cytoplasmic-vesicle localization.
source_documents:
- genes/DROME/Pld/Pld-predictions-source.json
- genes/DROME/Pld/Pld-uniprot-source.json
references:
- id: PMID:15883198
  title: Regulation of phototransduction responsiveness and retinal degeneration by a phospholipase D-generated
    signaling lipid.
  findings: []
  full_text_unavailable: false
- id: PMID:17156430
  title: A role for Phospholipase D in Drosophila embryonic cellularization.
  findings: []
  full_text_unavailable: false
predictions:
- source_method: ProtNLM2
  source_version: UniProt API snapshot 2026-09-08
  source_reference_id: file:DROME/Pld/Pld-predictions-source.json
  predicted_term:
    id: GO:0016042
    label: lipid catabolic process
  predicted_term_type: GO_BP
  review:
    assessment: CNN
    confidence_score: 2
    summary: Phosphatidylcholine hydrolysis is a lipid-catabolic reaction supported by measured Drosophila
      Pld activity. Although this exact biological-process ID is absent from the existing rows, the characterized
      D-type glycerophospholipase reaction already establishes the same lipid-breakdown biology, so it
      is correct but not biologically novel. This is reaction-level equivalence, not a claim that a molecular-function
      term is an ontology child of a biological-process term. The selected record retains both annotated
      PLD catalytic regions, supporting the broad reaction transfer.
    supported_by:
    - reference_id: PMID:15883198
      supporting_text: D. melanogaster Pld exhibits classic Pld activity, increases its activity in signaling
        contexts, and is inactivated by a point mutation to the conserved catalytic domain
    - reference_id: PMID:17156430
      supporting_text: Phospholipase D (PLD), which hydrolyzes the membrane phospholipid phosphatidylcholine
        to yield the lipid second messenger phosphatidic acid
- source_method: ProtNLM2
  source_version: UniProt API snapshot 2026-09-08
  source_reference_id: file:DROME/Pld/Pld-predictions-source.json
  predicted_term:
    id: GO:0005737
    label: cytoplasm
  predicted_term_type: GO_CC
  review:
    assessment: LSP
    confidence_score: 2
    summary: The cytoplasmic prediction is directly supported by immunolocalization in cellularizing embryos.
      It is broader than the existing cytoplasmic-vesicle localization, so it is less precise rather than
      an erroneous cytosolic default. The experiment describes both cytoplasm and cytosolic vesicles,
      without claiming exclusion from membrane-associated compartments.
    supported_by:
    - reference_id: PMID:17156430
      supporting_text: In cellularizing embryos, Pld localized to the cytoplasm and/or to cytosolic vesicles
        of uniform small size evenly distributed between apical and basal regions of the blastoderm (Fig.
        3A–D).