Selected accession A0A9L0TTC1; ordinary UniProt record is TrEMBL and cites genome sequencing/submission rather than a gene-specific functional experiment. Human evidence is summarized in the paired human investigation. Sequence comparison records the exact target gaps and transfer limits. The targeted Europe PMC search found no decisive gene-specific horse functional assay warranting a separate horse Edison investigation; general omics/association hits were not counted as mechanistic validation.
The substrate donor is acyl-CoA and the acceptor is the sn-1 hydroxyl of glycerol-3-phosphate. Lysophosphatidic acid enters several glycerolipid routes, so pathway participation is broader than the one catalyzed reaction. The 2023 structural work reports an N-terminal catalytic domain and associated C-terminal domain, and replaces a conventional multi-pass-transmembrane picture with an amphipathic surface/N-terminal loop-helix membrane association mechanism. The UniProt record links this reaction to direct experimental sources; the acyl-CoA statement is therefore not an ARBA corroboration. Papers mainly describing another GPAT paralog may include GPAT1 comparator assays, so title alone cannot justify discarding their GO annotations.
Sources: PMID:36522428(https://pubmed.ncbi.nlm.nih.gov/36522428/), PMID:18238778(https://pubmed.ncbi.nlm.nih.gov/18238778/), PMID:19075029(https://pubmed.ncbi.nlm.nih.gov/19075029/).