Recombinant Mouse Dehydrodolichyl diphosphate synthase complex subunit Nus1 (Nus1), partial

Function

With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery (PubMed:25066056). Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol phosphate which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER) (By similarity). Synthesizes long-chain polyprenols, mostly of C95 and C100 chain length (By similarity). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol (By similarity). Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator (By similarity)

Subcellular Location

Endoplasmic reticulum membrane (Multi-pass membrane protein)

Tissue Specificity

Highly expressed in heart, liver, kidney and pancreas

Subunit

The active dehydrodolichyl diphosphate synthase complex is a heterotetramer composed of a dimer of heterodimer of DHDDS and NUS1. Interacts with NPC2

Pathway

Lipid metabolism

• Carninci P. et al. The transcriptional landscape of the mammalian genome. — Science (2005)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Miao R.Q. et al. Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells. — Proc. Natl. Acad. Sci. U.S.A. (2006)
• Park E.J. et al. Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation. — Cell Metab. (2014)
• Park E.J. et al. NgBR is essential for endothelial cell glycosylation and vascular development. — EMBO Rep. (2016)