ALG5 is assigned to the dolichyl-phosphate beta-glucosyltransferase family, which supplies dolichyl-phosphate glucose for endoplasmic-reticulum N-glycan precursor assembly. The selected 294-residue horse protein retains the N-terminal membrane anchor but has an internal 30-residue deletion relative to the canonical human enzyme. Its glucose-donor pathway identity is well supported, while catalytic competence of this particular protein model remains unresolved.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004581 dolichyl-phosphate beta-glucosyltransferase activity | IEA GO_REF:0000003 | UNDECIDED | Summary: ALG5-family identity supports this activity, but the selected sequence has a consequential internal deletion. Reason: Human ALG5 complements yeast alg5 deficiency and supplies dolichyl-phosphate glucose. The horse record is highly conserved and assigned to ALG5, but lacks human residues95–124 within the enzyme body. Without an isoform/structure assessment, transfer of active glucosyltransferase catalysis to this exact model is uncertain. The concern is sequence completeness, not evidence for GDP-mannose specificity. Supporting Evidence: PMID:10359825 Expression of the human ALG5 and ALG6 cDNA could partially complement the respective S. cerevisiae alg5 and alg6 deficiency. |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: The N-terminal membrane anchor supports ER membrane residence. Reason: The selected horse sequence preserves the hydrophobic region corresponding to the human transmembrane helix at residues8–28. This supports ER membrane localization by conserved ALG5 architecture, independently of whether the internal deletion preserves catalytic activity. Supporting Evidence: file:human/ALG5/ALG5-uniprot.txt FT TRANSMEM 8..28 file:HORSE/ALG5/ALG5-bioinformatics/RESULTS.md | TRANSMEM | 8–28 | 8,9,10,11,12,13,14,15,16,17,18,19,20,21,22,23,24,25,26,27,28 | 16/21 | |
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