The selected Caenorhabditis elegans dpm-1 product is a 51-residue polypeptide corresponding to the extreme C terminus of the longer dolichol-phosphate mannosyltransferase protein. It lacks the glycosyltransferase domain required for dolichol-phosphate mannose synthesis. Stable expression, localization and any noncatalytic role of this short product are unknown.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004582 dolichyl-phosphate beta-D-mannosyltransferase activity | IEA GO_REF:0000002 | REMOVE | Summary: U4PF58 consists only of the last 51 residues of DPM1 and lacks its entire glycosyltransferase domain. The electronic catalytic annotation cannot apply to this isolated product, even though the full-length same-gene protein is the appropriate enzyme. Supporting Evidence: file:worm/dpm-1/dpm-1-bioinformatics/RESULTS.md | Domain: Glycosyltransferase 2-like | 8–176 | 0 / 169 | 0 | file:worm/dpm-1/dpm-1-bioinformatics/RESULTS.md | 189–239 | 1–51 | 51 | PMID:10835346 mammalian DPM synthase contains catalytic DPM1 and regulatory DPM2 |
Loading supporting content…
Download this section (compressed HTML)Q: Is Y66H1A.2b translated, and does its C-terminal peptide interact with the dolichol-phosphate mannose synthesis complex?
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)