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Q5T2R2 (DPS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Trans-prenyltransferase 1
Short name=TPT 1
Gene names
Name:PDSS1
Synonyms:DPS1, TPRT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length415 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.2

Catalytic activity

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

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.2

Subcellular location

Mitochondrion Potential.

Involvement in disease

Coenzyme Q10 deficiency, primary, 2 (COQ10D2) [MIM:614651]: An autosomal recessive multisystem disorder characterized by early-onset deafness, optic atrophy, mild mental retardation, peripheral neuropathy, obesity, livedo reticularis, and cardiac valvulopathy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5T2R2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q5T2R2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     279-415: SVLGCPDPVV...LSEIVLTRDK → FPRNECYDHATVQFAWRCRQSSTVCTTE
Note: No experimental confirmation available.
Isoform 3 (identifier: Q5T2R2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: MASRWWRWRRGCSWKPAARSPGPGSPGRAGPLGPSAAAEVRA → MPA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 415415Decaprenyl-diphosphate synthase subunit 1
PRO_0000123975

Sites

Metal binding1801Magnesium 1 By similarity
Metal binding1801Magnesium 2 By similarity
Metal binding1841Magnesium 1 By similarity
Metal binding1841Magnesium 2 By similarity
Metal binding3071Magnesium 3 By similarity
Binding site1341Isopentenyl diphosphate By similarity
Binding site1371Isopentenyl diphosphate By similarity
Binding site1731Isopentenyl diphosphate By similarity
Binding site1891Polyprenyl diphosphate By similarity
Binding site1901Isopentenyl diphosphate By similarity
Binding site2661Polyprenyl diphosphate By similarity
Binding site2671Polyprenyl diphosphate By similarity
Binding site3041Polyprenyl diphosphate By similarity
Binding site3211Polyprenyl diphosphate By similarity

Natural variations

Alternative sequence1 – 4242MASRW…AEVRA → MPA in isoform 3.
VSP_017100
Alternative sequence279 – 415137SVLGC…LTRDK → FPRNECYDHATVQFAWRCRQ SSTVCTTE in isoform 2.
VSP_017101
Natural variant3081D → E in COQ10D2. Ref.6
VAR_034879

Experimental info

Sequence conflict301G → V in AAH63635. Ref.5
Sequence conflict441V → A in AAD28559. Ref.1
Sequence conflict471R → Q in AAD28559. Ref.1
Sequence conflict581I → F in AAD28559. Ref.1
Sequence conflict661S → P in AAD28559. Ref.1
Sequence conflict72 – 732CR → YS in AAD28559. Ref.1
Sequence conflict761R → Q in AAD28559. Ref.1
Sequence conflict831D → Y in AAD28559. Ref.1
Sequence conflict1091D → G in AAD28559. Ref.1
Sequence conflict1141L → P in AAD28559. Ref.1
Sequence conflict1191S → T in AAD28559. Ref.1
Sequence conflict1241M → I in AAD28559. Ref.1
Sequence conflict1311G → V in AAD28559. Ref.1
Sequence conflict1421A → V in AAD28559. Ref.1
Sequence conflict1861A → V in BAD97134. Ref.3
Sequence conflict2981N → D in BAD97134. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: F0B073C75CBD06D2

FASTA41546,261
        10         20         30         40         50         60 
MASRWWRWRR GCSWKPAARS PGPGSPGRAG PLGPSAAAEV RAQVHRRKGL DLSQIPYINL 

        70         80         90        100        110        120 
VKHLTSACPN VCRISRFHHT TPDSKTHSGE KYTDPFKLGW RDLKGLYEDI RKELLISTSE 

       130        140        150        160        170        180 
LKEMSEYYFD GKGKAFRPII VALMARACNI HHNNSRHVQA SQRAIALIAE MIHTASLVHD 

       190        200        210        220        230        240 
DVIDDASSRR GKHTVNKIWG EKKAVLAGDL ILSAASIALA RIGNTTVISI LTQVIEDLVR 

       250        260        270        280        290        300 
GEFLQLGSKE NENERFAHYL EKTFKKTASL IANSCKAVSV LGCPDPVVHE IAYQYGKNVG 

       310        320        330        340        350        360 
IAFQLIDDVL DFTSCSDQMG KPTSADLKLG LATGPVLFAC QQFPEMNAMI MRRFSLPGDV 

       370        380        390        400        410 
DRARQYVLQS DGVQQTTYLA QQYCHEAIRE ISKLRPSPER DALIQLSEIV LTRDK 

« Hide

Isoform 2 [UniParc].

Checksum: D5195700E8AFF902
Show »

FASTA30634,304
Isoform 3 [UniParc].

Checksum: BB32C9961B92ED00
Show »

FASTA37642,089

References

« Hide 'large scale' references
[1]"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] (ISOFORM 3).
[2]"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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Coronary arterial endothelium.
[4]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-415 (ISOFORM 1).
Tissue: Brain and Duodenum.
[6]"Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders."
Mollet J., Giurgea I., Schlemmer D., Dallner G., Chretien D., Delahodde A., Bacq D., de Lonlay P., Munnich A., Rotig A.
J. Clin. Invest. 117:765-772(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT COQ10D2 GLU-308.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF118395 mRNA. Translation: AAD28559.1.
AB210838 mRNA. Translation: BAE48216.1.
AK223414 mRNA. Translation: BAD97134.1.
AL390961 Genomic DNA. Translation: CAI17280.1.
BC049211 mRNA. Translation: AAH49211.1.
BC063635 mRNA. Translation: AAH63635.1.
CCDSCCDS31168.1. [Q5T2R2-1]
RefSeqNP_055132.2. NM_014317.3. [Q5T2R2-1]
UniGeneHs.558468.

3D structure databases

ProteinModelPortalQ5T2R2.
SMRQ5T2R2. Positions 94-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117125. 1 interaction.
STRING9606.ENSP00000365388.

PTM databases

PhosphoSiteQ5T2R2.

Polymorphism databases

DMDM74744657.

Proteomic databases

MaxQBQ5T2R2.
PaxDbQ5T2R2.
PRIDEQ5T2R2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376203; ENSP00000365376; ENSG00000148459. [Q5T2R2-2]
ENST00000376215; ENSP00000365388; ENSG00000148459. [Q5T2R2-1]
GeneID23590.
KEGGhsa:23590.
UCSCuc001isv.3. human. [Q5T2R2-1]
uc001isw.3. human. [Q5T2R2-2]

Organism-specific databases

CTD23590.
GeneCardsGC10P026986.
HGNCHGNC:17759. PDSS1.
HPAHPA038032.
MIM607429. gene.
614651. phenotype.
neXtProtNX_Q5T2R2.
Orphanet254898. Deafness - encephaloneuropathy - obesity - valvulopathy.
PharmGKBPA134982512.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0142.
HOGENOMHOG000009104.
HOVERGENHBG054389.
InParanoidQ5T2R2.
KOK12504.
OMAKAFRPMI.
OrthoDBEOG7DNNWF.
PhylomeDBQ5T2R2.
TreeFamTF313548.

Enzyme and pathway databases

BioCycMetaCyc:HS07530-MONOMER.
BRENDA2.5.1.11. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00232.

Gene expression databases

BgeeQ5T2R2.
CleanExHS_PDSS1.
GenevestigatorQ5T2R2.

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

GeneWikiPDSS1.
GenomeRNAi23590.
NextBio46232.
PROQ5T2R2.
SOURCESearch...

Entry information

Entry nameDPS1_HUMAN
AccessionPrimary (citable) accession number: Q5T2R2
Secondary accession number(s): Q53F75 expand/collapse secondary AC list , Q6P473, Q86WQ8, Q9Y2W5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM