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Q33DR2 (DPS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Decaprenyl-diphosphate synthase subunit 1

EC=2.5.1.91
Alternative name(s):
All-trans-decaprenyl-diphosphate synthase subunit 1
Decaprenyl pyrophosphate synthase subunit 1
Solanesyl-diphosphate synthase subunit 1
Trans-prenyltransferase 1
Short name=TPT 1
Gene names
Name:Pdss1
Synonyms:Dps1, Sps1, Tprt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Supplies decaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone-10. Ref.1

Catalytic activity

(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + all-trans-decaprenyl diphosphate. Ref.1

Cofactor

Binds 3 magnesium ions per subunit By similarity.

Pathway

Cofactor biosynthesis; ubiquinone biosynthesis.

Subunit structure

Heterotetramer of 2 DPS1/TPRT and 2 DLP1 subunits. Ref.1

Subcellular location

Mitochondrion Potential.

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Sequence caution

The sequence AAD24462.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH26820.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 409409Decaprenyl-diphosphate synthase subunit 1
PRO_0000123976

Sites

Metal binding1741Magnesium 1 By similarity
Metal binding1741Magnesium 2 By similarity
Metal binding1781Magnesium 1 By similarity
Metal binding1781Magnesium 2 By similarity
Metal binding3011Magnesium 3 By similarity
Binding site1281Isopentenyl diphosphate By similarity
Binding site1311Isopentenyl diphosphate By similarity
Binding site1671Isopentenyl diphosphate By similarity
Binding site1831Polyprenyl diphosphate By similarity
Binding site1841Isopentenyl diphosphate By similarity
Binding site2601Polyprenyl diphosphate By similarity
Binding site2611Polyprenyl diphosphate By similarity
Binding site2981Polyprenyl diphosphate By similarity
Binding site3151Polyprenyl diphosphate By similarity

Experimental info

Sequence conflict11M → V in AAH26820. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q33DR2 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: EF94459BD78F48B2

FASTA40945,895
        10         20         30         40         50         60 
MAMRWSCWRR GCSWRPTAVG SPRRERPGCV EPLGTRAASD TRAQIPYFSL MKILMSASPT 

        70         80         90        100        110        120 
MHSISQFHQR TPAMCSCRQT QSGEKYSDPF KLGWRDLKGL YEDIRKELHI STRELKDMSE 

       130        140        150        160        170        180 
YYFDGKGKAF RPIIVVLMAR ACNIHHNNAR EMQASQRSIA LVAEMIHTAT LVHDDVIDDA 

       190        200        210        220        230        240 
SSRRGKHTVN KIWGEKKAVL AGDLILSAAS VALARIGNTA VVSMLAQVIE DLVRGEFLQL 

       250        260        270        280        290        300 
GSKENENERF AHYLEKTFKK TASLIANSCK AVSVLGCPDP VVHEIAYQYG KNVGIAFQLI 

       310        320        330        340        350        360 
DDVLDFTSCS DQMGKPTSAD LKLGIATGPV LFACQQFPEM NAMIMRRFSL PGDVDRARQY 

       370        380        390        400 
VLQSDGVQQT TYLAQQYCHK AVREIRKLRP STERDALIQL SESVLTRDK 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of solanesyl and decaprenyl diphosphate synthases in mice and humans."
Saiki R., Nagata A., Kainou T., Matsuda H., Kawamukai M.
FEBS J. 272:5606-5622(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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: C57BL/6J and FVB/N.
Tissue: Mammary tumor.
[4]"Quinone-responsive multiple respiratory-chain dysfunction due to widespread coenzyme Q10 deficiency."
Roetig A., Appelkvist E.-L., Geromel V., Chretien D., Kadhom N., Edery P., Lebideau M., Dallner G., Munnich A., Ernster L., Rustin P.
Lancet 356:391-395(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 67-409.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB210841 mRNA. Translation: BAE48219.1.
CT030013 Genomic DNA. Translation: CAX15884.1.
BC026820 mRNA. Translation: AAH26820.1. Different initiation.
BC107273 mRNA. Translation: AAI07274.2.
BC107274 mRNA. Translation: AAI07275.2.
AF118855 mRNA. Translation: AAD24462.1. Different initiation.
RefSeqNP_062374.2. NM_019501.3.
UniGeneMm.249752.

3D structure databases

ProteinModelPortalQ33DR2.
SMRQ33DR2. Positions 88-409.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000055689.

PTM databases

PhosphoSiteQ33DR2.

Proteomic databases

PRIDEQ33DR2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000053729; ENSMUSP00000055689; ENSMUSG00000026784.
GeneID56075.
KEGGmmu:56075.
UCSCuc008inq.1. mouse.

Organism-specific databases

CTD23590.
MGIMGI:1889278. Pdss1.

Phylogenomic databases

eggNOGCOG0142.
GeneTreeENSGT00530000063378.
HOGENOMHOG000009104.
HOVERGENHBG054389.
InParanoidQ33DR2.
KOK12504.
OMAIYTMREG.
OrthoDBEOG7DNNWF.
PhylomeDBQ33DR2.
TreeFamTF313548.

Enzyme and pathway databases

BRENDA2.5.1.11. 3474.
UniPathwayUPA00232.

Gene expression databases

ArrayExpressQ33DR2.
BgeeQ33DR2.
GenevestigatorQ33DR2.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
InterProIPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
IPR008949. Terpenoid_synth.
[Graphical view]
PANTHERPTHR12001. PTHR12001. 1 hit.
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMSSF48576. SSF48576. 1 hit.
PROSITEPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio311864.
PROQ33DR2.
SOURCESearch...

Entry information

Entry nameDPS1_MOUSE
AccessionPrimary (citable) accession number: Q33DR2
Secondary accession number(s): B8JJW9, Q9WU69
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot