Gene Ontology annotation through association of InterPro records with GO terms
Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1, DPM2 and DPM3.
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The primary mammalian complex study distinguishes catalytic DPM1 from regulatory subunits; it does not demonstrate activity of the short worm product.
"mammalian DPM synthase contains catalytic DPM1 and regulatory DPM2"
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DPM3 binds DPM1 and stabilises it, so the catalytic subunit relies on partner subunits in the mammalian complex.
"DPM3 directly stabilized DPM1"
DPM1, the catalytic subunit of dolichol-phosphate mannose synthase, is tethered to and stabilized on the endoplasmic reticulum membrane by DPM3.
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Mammalian DPM1 is the catalytic subunit and depends on DPM3 for ER-membrane tethering, stability and activity.
"DPM1 was rapidly degraded by the proteasome in the absence of DPM3."
Complete absence of the reference glycosyltransferase domain
dpm-1 re-review isoform mapping and ortholog comparison
Falcon deep research on dpm-1
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No worm-specific biochemical, genetic or localisation study of the dpm-1 products was found; function rests on family membership.
"In particular, no purified-enzyme assay, mutant rescue, endogenous localization experiment, or pathway-resolved glycomic analysis was found for this exact worm protein."
WormBase gene description for dpm-1 (worm)
Frozen exact-input ProtNLM output and UniProt sequence for U4PF58