The selected horse ALG5 A0A5F5PM72 retains the N-terminal hydrophobic membrane anchor, but the 294-aa sequence deletes canonical human residues 95–124. The remaining 294 residues align at 94.6% identity. Do not equate sequence-family identity with demonstrated activity of a deletion-bearing model. The horse GOA enzyme activity is UNDECIDED pending model/structure validation; ER membrane residence remains supported by the preserved anchor.
PMID:10359825(https://pubmed.ncbi.nlm.nih.gov/10359825/), DOI 10.1073/pnas.96.12.6982, studies BOTH ALG5 and ALG6 despite its ALG6-focused title. “Expression of the human ALG5 and ALG6 cDNA could partially complement the respective S. cerevisiae alg5 and alg6 deficiency.” This supports human ALG5 glucose-donor pathway identity and demonstrates why title-only paralog attribution is unsafe. The independent human UniProt biochemical statement is explicitly experimental-source-derived, not ARBA.
The ProtNLM paragraph instead describes GDP-mannose transfer and DPM synthase, which are not established properties of this ALG5-family sequence. The internal deletion does not itself establish conversion to a GDP-mannose-dependent enzyme. No horse functional paper was identified; human deep research is prioritized.