UniProt ID: Q6DHR8 |
FUNCTION: With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol. Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator. {ECO:0000250|UniProtKB:Q96E22}. CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di- trans,poly-cis-polyprenyl diphosphate + n diphosphate; Xref=Rhea:RHEA:53008, Rhea:RHEA-COMP:13431, ChEBI:CHEBI:33019, ChEBI:CHEBI:128769, ChEBI:CHEBI:136960, ChEBI:CHEBI:175763; EC=2.5.1.87; Evidence={ECO:0000250|UniProtKB:Q96E22}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q86SQ9}; PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96E22}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96E22}. MISCELLANEOUS: Nus1 seems to exist in two topological orientations, a minor glycosylated species with its C-terminus oriented towards the lumen regulating NPC2 stability, and a major fraction oriented with its C-terminus directed towards the cytosol where it regulates cis-IPTase activity. {ECO:0000250|UniProtKB:Q96E22}. SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}. SEQUENCE CAUTION: Sequence=CAQ13477.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; |
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