Overview
| Uniprot ID | Q86SQ9 |
| Protein Name | Dehydrodolichyl diphosphate synthase complex subunit DHDDS |
| Gene Name | DHDDS |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 108 |
FSRLMEEKEKLQKHG |
| 110 |
RLMEEKEKLQKHGVC |
Function
With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery (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: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)
Protein Sequence
10
MSWIKEGELS
20
LWERFCANII
30
KAGPMPKHIA
40
FIMDGNRRYA
50
KKCQVERQEG
60
HSQGFNKLAE
70
TLRWCLNLGI
80
LEVTVYAFSI
90
ENFKRSKSEV
100
DGLMDLARQK
110
FSRLMEEKEK
120
LQKHGVCIRV
130
LGDLHLLPLD
140
LQELIAQAVQ
150
ATKNYNKCFL
160
NVCFAYTSRH
170
EISNAVREMA
180
WGVEQGLLDP
190
SDISESLLDK
200
CLYTNRSPHP
210
DILIRTSGEV
220
RLSDFLLWQT
230
SHSCLVFQPV
240
LWPEYTFWNL
250
FEAILQFQMN
260
HSVLQKARDM
270
YAEERKRQQL
280
ERDQATVTEQ
290
LLREGLQASG
300
DAQLRRTRLH
310
KLSARREERV
320
QGFLQALELK
330
RADWLARLGT
ASA
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:1904423 |
dehydrodolichyl diphosphate synthase complex |
| Cellular Component |
GO:0005783 |
endoplasmic reticulum |
| 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:0006489 |
dolichyl diphosphate biosynthetic process |
| Biological Process |
GO:0043048 |
dolichyl monophosphate biosynthetic process |
| Biological Process |
GO:0016094 |
polyprenol biosynthetic process |
Reference
[1] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.