Pld / A4UZ54

The selected A4UZ54 sequence has 1260 residues, whereas the cloned protein described in PMID:17156430(https://pubmed.ncbi.nlm.nih.gov/17156430/) has1278. Both catalytic regions are retained in the selected record (592–619 and1072–1099), supporting transfer of the defining phospholipase reaction without assuming every published construct is identical. The article has cached full text; it reports “Pld localized to the cytoplasm and/or to cytosolic vesicles”. PMID:15883198(https://pubmed.ncbi.nlm.nih.gov/15883198/) provides activity and catalytic-mutant evidence. ProtNLM lipid catabolism is CNN because the characterized phospholipase reaction already establishes the lipid-breakdown biology, while cytoplasm is LSP relative to cytoplasmic vesicle. Existing developmental and phototransduction phenotypes are retained as noncore consequences of the lipid-trafficking mechanism. Phosphatidylinositol binding remains unresolved at the exact ligand level. ARBA reaction and localization text is not independent validation.

Sequence and research provenance

The selected frozen UniProt record is retained in Pld-uniprot-source.json, with the complete original prediction metadata in Pld-predictions-source.json. It maps the exact accession to this FlyBase gene; current sequence identity does not establish the historical predictor input. Gene-level experiments support conserved functions unless a relevant isoform difference is established. Falcon research was requested with perplexity-lite fallback alongside publication caching. Primary publications and sequence observations, rather than AI summaries or ARBA assertions, support the curated conclusions.

Provider readback

The completed Falcon report was inspected. Its conventional phosphatidylcholine-specific PLD identification and embryonic vesicle localization agree with inspected primary articles. It quotes the older 1278-residue construct; the selected A4UZ54 sequence is 1260 residues with both catalytic domains retained. The report also describes later photoreceptor recycling studies, which reinforce membrane trafficking but are not needed as independent evidence for the two broad predictions. The exact lipid-catabolism GO ID is absent from GOA, but its biological content is already captured by the characterized PC-hydrolysis reaction; CNN is appropriate without treating BP and MF terms as ontology parent/child.