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Protein

Dehydrodolichyl diphosphate synthase complex subunit Nus1

Gene

Nus1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 precusrosor 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.By similarity

Catalytic activityi

(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n = 10-55).1 PublicationBy similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.Curated
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

  • prenyltransferase activity Source: MGI

GO - Biological processi

  • angiogenesis Source: UniProtKB-KW
  • cell differentiation Source: UniProtKB-KW
  • cholesterol homeostasis Source: MGI
  • dolichol biosynthetic process Source: MGI
  • protein mannosylation Source: MGI
  • regulation of intracellular cholesterol transport Source: MGI
  • sterol homeostasis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor, Transferase

Keywords - Biological processi

Angiogenesis, Differentiation

Enzyme and pathway databases

ReactomeiR-MMU-446199. Synthesis of Dolichyl-phosphate.
UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Dehydrodolichyl diphosphate synthase complex subunit Nus1Curated (EC:2.5.1.87By similarity)
Alternative name(s):
Di-trans,poly-cis-decaprenylcistransferaseCurated
Nogo-B receptorBy similarity
Short name:
NgBRBy similarity
Nuclear undecaprenyl pyrophosphate synthase 1 homologCurated
Gene namesi
Name:Nus1Imported
Synonyms:D10Ertd438e, Ngbr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1196365. Nus1.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity

  • Note: Colocalizes with Nogo-B during VEGF and wound healing angiogenesis.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2620Helical; Name=1By similarityAdd
BLAST
Transmembranei40 – 5617Helical; Name=2By similarityAdd
BLAST
Transmembranei121 – 13919Helical; Name=3By similarityAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Leads to early embryonic lethality in vivo and defective cis-prenyltransferase activity and cholesterol levels in isolated fibroblasts.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297Dehydrodolichyl diphosphate synthase complex subunit Nus1PRO_0000273168Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi148 – 1481N-linked (GlcNAc...)Sequence analysis
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ99LJ8.
PaxDbiQ99LJ8.
PRIDEiQ99LJ8.

Expressioni

Tissue specificityi

Highly expressed in heart, liver, kidney and pancreas.1 Publication

Gene expression databases

BgeeiQ99LJ8.
ExpressionAtlasiQ99LJ8. baseline and differential.
GenevisibleiQ99LJ8. MM.

Interactioni

Subunit structurei

Forms an active dehydrodolichyl diphosphate synthase complex with DHDDS. Interacts with NPC2.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023830.

Structurei

3D structure databases

ProteinModelPortaliQ99LJ8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UPP synthase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2818. Eukaryota.
COG0020. LUCA.
GeneTreeiENSGT00390000003223.
HOGENOMiHOG000007321.
HOVERGENiHBG082024.
InParanoidiQ99LJ8.
KOiK19177.
OMAiYVSVYDH.
OrthoDBiEOG773XGR.
PhylomeDBiQ99LJ8.
TreeFamiTF332448.

Family and domain databases

Gene3Di3.40.1180.10. 1 hit.
InterProiIPR001441. UPP_synth-like.
[Graphical view]
PfamiPF01255. Prenyltransf. 1 hit.
[Graphical view]
SUPFAMiSSF64005. SSF64005. 1 hit.

Sequencei

Sequence statusi: Complete.

Q99LJ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGLYELVWR VLHALLCLHL TLTSWLRVRF GTWNWIWRRC CRAASAAVLA
60 70 80 90 100
PLGFTLRKPR AVGRNRRHHR HPHGGPGPGP GPAATHPRLR WRADVRSLQK
110 120 130 140 150
LPVHMGLLVT EEVQEPSFSD IASLVVWCMA VGISYISVYD HQGIFKRNNS
160 170 180 190 200
RLMDEILKQQ QELLGQDCSK YSAEFANSND KDDQDLNCPS AVKVLSPEDG
210 220 230 240 250
KADIVRAAQD FCQLVAQQQR KPTDLDVDLL GSLLSSHGFP DPDLVLKFGP
260 270 280 290
VDSTLGFLPW QIRLTEIVSL PSHLNISYED FFSALRQYAA CEQRLGK
Length:297
Mass (Da):33,485
Last modified:June 1, 2001 - v1
Checksum:iB1B5C1EFB2336A9E
GO

Sequence cautioni

The sequence AAH18372.1 differs from that shown. Reason: Frameshift at position 10. Curated
The sequence BAE33349.1 differs from that shown. Reason: Frameshift at position 252. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291R → H in BAE39779 (PubMed:16141072).Curated
Sequence conflicti91 – 911W → L in BAE39943 (PubMed:16141072).Curated
Sequence conflicti213 – 2131Q → K in BAE39943 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK155620 mRNA. Translation: BAE33349.1. Sequence problems.
AK167741 mRNA. Translation: BAE39779.1.
AK167939 mRNA. Translation: BAE39943.1.
BC003223 mRNA. Translation: AAH03223.1.
BC018372 mRNA. Translation: AAH18372.1. Frameshift.
CCDSiCCDS23841.1.
RefSeqiNP_084526.1. NM_030250.2.
UniGeneiMm.199964.

Genome annotation databases

EnsembliENSMUST00000023830; ENSMUSP00000023830; ENSMUSG00000023068.
GeneIDi52014.
KEGGimmu:52014.
UCSCiuc007fbi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK155620 mRNA. Translation: BAE33349.1. Sequence problems.
AK167741 mRNA. Translation: BAE39779.1.
AK167939 mRNA. Translation: BAE39943.1.
BC003223 mRNA. Translation: AAH03223.1.
BC018372 mRNA. Translation: AAH18372.1. Frameshift.
CCDSiCCDS23841.1.
RefSeqiNP_084526.1. NM_030250.2.
UniGeneiMm.199964.

3D structure databases

ProteinModelPortaliQ99LJ8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023830.

Proteomic databases

MaxQBiQ99LJ8.
PaxDbiQ99LJ8.
PRIDEiQ99LJ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023830; ENSMUSP00000023830; ENSMUSG00000023068.
GeneIDi52014.
KEGGimmu:52014.
UCSCiuc007fbi.2. mouse.

Organism-specific databases

CTDi116150.
MGIiMGI:1196365. Nus1.

Phylogenomic databases

eggNOGiKOG2818. Eukaryota.
COG0020. LUCA.
GeneTreeiENSGT00390000003223.
HOGENOMiHOG000007321.
HOVERGENiHBG082024.
InParanoidiQ99LJ8.
KOiK19177.
OMAiYVSVYDH.
OrthoDBiEOG773XGR.
PhylomeDBiQ99LJ8.
TreeFamiTF332448.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-MMU-446199. Synthesis of Dolichyl-phosphate.

Miscellaneous databases

ChiTaRSiNus1. mouse.
PROiQ99LJ8.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LJ8.
ExpressionAtlasiQ99LJ8. baseline and differential.
GenevisibleiQ99LJ8. MM.

Family and domain databases

Gene3Di3.40.1180.10. 1 hit.
InterProiIPR001441. UPP_synth-like.
[Graphical view]
PfamiPF01255. Prenyltransf. 1 hit.
[Graphical view]
SUPFAMiSSF64005. SSF64005. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ and C57BL/6J.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells."
    Miao R.Q., Gao Y., Harrison K.D., Prendergast J., Acevedo L.M., Yu J., Hu F., Strittmatter S.M., Sessa W.C.
    Proc. Natl. Acad. Sci. U.S.A. 103:10997-11002(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. "Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation."
    Park E.J., Grabinska K.A., Guan Z., Stranecky V., Hartmannova H., Hodanova K., Baresova V., Sovova J., Jozsef L., Ondruskova N., Hansikova H., Honzik T., Zeman J., Hulkova H., Wen R., Kmoch S., Sessa W.C.
    Cell Metab. 20:448-457(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, CONDITIONAL KNOCKOUT IN FIBROBLATS.

Entry informationi

Entry nameiNGBR_MOUSE
AccessioniPrimary (citable) accession number: Q99LJ8
Secondary accession number(s): Q0P6D7
, Q3TIA3, Q3TIR7, Q3U1Z4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.