Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1, DPM2 and DPM3.
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DPM3 is a 92-amino-acid third subunit of the human DPM synthase complex that associates with DPM1 via its C-terminal domain and with DPM2 via its N-terminal portion; DPM3 directly stabilizes DPM1 and is required for DPM biosynthesis.
"The third subunit, DPM3, comprises 92 amino acids associated with DPM1"
Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2.
Defining the membrane proteome of NK cells.
Congenital disorder of glycosylation due to DPM1 mutations presenting with dystroglycanopathy-type congenital muscular dystrophy.
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DPM3 is described as an essential, non-catalytic subunit of the DPM complex; a pathogenic DPM1 variant showed reduced binding to DPM3, indicating a disease mechanism via impaired DPM1-DPM3 interaction.
"non-catalytic subunit of the DPM complex"
DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate.
dolichyl phosphate + GDP-alpha-D-mannose -> dolichyl phosphate D-mannose
Defective DPM1 does not transfer mannose to DOLP to form DOLPman
Defective DPM3 does not transfer mannose to DOLP to form DOLPman
Defective DPM2 does not transfer mannose to DOLP to form DOLPman
UniProtKB entry Q9P2X0 (DPM3_HUMAN)
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DPM3 is the stabilizer subunit of the DPM synthase complex that tethers the catalytic DPM1 subunit to the ER membrane; it is a multi-pass ER membrane protein and its loss causes DPM3-CDG dystroglycanopathy.
"synthase complex; tethers catalytic subunit DPM1 to the endoplasmic"