Overview
| Uniprot ID | Q96E22 |
|---|
| Protein Name | Dehydrodolichyl diphosphate synthase complex subunit NUS1 |
|---|
| Gene Name | NUS1 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 58 |
PLGFTLRKPPAVGRN |
Function
With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery (PubMed:21572394, PubMed:25066056, PubMed:28842490, PubMed:32817466, PubMed:33077723). 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) (PubMed:21572394, PubMed:25066056, PubMed:28842490, PubMed:32817466, PubMed:33077723). Synthesizes long-chain polyprenols, mostly of C95 and C100 chain length (PubMed:32817466). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol (PubMed:21572394). Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator (PubMed:16835300)
Protein Sequence
10
MTGLYELVWR
20
VLHALLCLHR
30
TLTSWLRVRF
40
GTWNWIWRRC
50
CRAASAAVLA
60
PLGFTLRKPP
70
AVGRNRRHHR
80
HPRGGSCLAA
90
AHHRMRWRAD
100
GRSLEKLPVH
110
MGLVITEVEQ
120
EPSFSDIASL
130
VVWCMAVGIS
140
YISVYDHQGI
150
FKRNNSRLMD
160
EILKQQQELL
170
GLDCSKYSPE
180
FANSNDKDDQ
190
VLNCHLAVKV
200
LSPEDGKADI
210
VRAAQDFCQL
220
VAQKQKRPTD
230
LDVDTLASLL
240
SSNGCPDPDL
250
VLKFGPVDST
260
LGFLPWHIRL
270
TEIVSLPSHL
280
NISYEDFFSA
290
LRQYAACEQR
LGK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:1904423 |
dehydrodolichyl diphosphate synthase complex |
| Cellular Component |
GO:0005789 |
endoplasmic reticulum membrane |
| Molecular Function |
GO:0045547 |
ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] activity |
| Molecular Function |
GO:0046872 |
metal ion binding |
| Biological Process |
GO:0001525 |
angiogenesis |
| Biological Process |
GO:0030154 |
cell differentiation |
| Biological Process |
GO:0006489 |
dolichyl diphosphate biosynthetic process |
| Biological Process |
GO:0043048 |
dolichyl monophosphate biosynthetic process |
| Biological Process |
GO:1903589 |
positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis |
| Biological Process |
GO:0090050 |
positive regulation of cell migration involved in sprouting angiogenesis |
| Biological Process |
GO:0032383 |
regulation of intracellular cholesterol transport |
| Biological Process |
GO:0038084 |
vascular endothelial growth factor signaling pathway |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.