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Q33DR3 (DLP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 73. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Decaprenyl-diphosphate synthase subunit 2

EC=2.5.1.91
Alternative name(s):
All-trans-decaprenyl-diphosphate synthase subunit 2
Decaprenyl pyrophosphate synthase subunit 2
Solanesyl-diphosphate synthase subunit 2
Gene names
Name:Pdss2
Synonyms:Dlp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length401 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

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.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q33DR3-1)

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: Q33DR3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     350-352: LRE → VVS
     353-401: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q33DR3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     213-264: VELLSSALMD...LSHCALLAKS → KAERLTCAHT...DGDLGSDNMK
     265-401: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Decaprenyl-diphosphate synthase subunit 2
PRO_0000123979

Natural variations

Alternative sequence213 – 26452VELLS…LLAKS → KAERLTCAHTASGVSCLAAE ATDRGVCVLLLSSSMWMLTE TDDGDLGSDNMK in isoform 3.
VSP_017102
Alternative sequence265 – 401137Missing in isoform 3.
VSP_017103
Alternative sequence350 – 3523LRE → VVS in isoform 2.
VSP_017104
Alternative sequence353 – 40149Missing in isoform 2.
VSP_017105

Experimental info

Sequence conflict1321A → S in BAE48218. Ref.1
Sequence conflict2041L → I in BAB30693. Ref.2

Sequences

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

Last modified January 24, 2006. Version 2.
Checksum: DB7835A83019E5AA

FASTA40143,980
        10         20         30         40         50         60 
MSLRQLLLRL SGYLGASGPP SRHWWYFRSL DSISSAGSWR GRSSRSPAHW NQVVSEAEKI 

        70         80         90        100        110        120 
VGYPASFMSL RCLLSDELSN IAMQVRKLVG TGHPLLTTAR ALVHDSRHNL QLRGLVVLLI 

       130        140        150        160        170        180 
SKAAGPSTRN AACQNYDMVS GVYSCQRSLA EITELIHTAL LVHRGIVNLS ELQSSDGPLK 

       190        200        210        220        230        240 
DMQFGNKIAI LSGDFLLANA CNGLALLQNT KVVELLSSAL MDLVHGVYQE NSASTKENSI 

       250        260        270        280        290        300 
PDDIGISTWK EQTFLSHCAL LAKSCQAAME LAKHDAAVQD MAFQYGKHMA MSHKINADLQ 

       310        320        330        340        350        360 
PFIKDKASDS KTFNLNSAPV VLHQEFLGRD LWIKQIGEAQ EKGSLNYSKL RETIKAGKGV 

       370        380        390        400 
TSAIDLCRYH GNKALEALES FPPSEARSAL ENIVFAVTRF S 

« Hide

Isoform 2 [UniParc].

Checksum: 22895FB1C1B55490
Show »

FASTA35238,618
Isoform 3 [UniParc].

Checksum: EDE79A90E66D6F6E
Show »

FASTA26428,599

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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[2]"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. expand/collapse author list , 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] (ISOFORMS 2 AND 3).
Strain: C57BL/6J.
Tissue: Corpora quadrigemina and Head.
[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] (ISOFORMS 1 AND 3).
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB210840 mRNA. Translation: BAE48218.1.
AK017329 mRNA. Translation: BAB30693.1.
AK140091 mRNA. Translation: BAE24234.1.
BC147693 mRNA. Translation: AAI47694.1.
BC147694 mRNA. Translation: AAI47695.1.
BC147752 mRNA. Translation: AAI47753.1.
BC147753 mRNA. Translation: AAI47754.1.
CCDSCCDS35891.1. [Q33DR3-1]
CCDS48552.1. [Q33DR3-2]
RefSeqNP_001161761.1. NM_001168289.1. [Q33DR3-2]
NP_082048.2. NM_027772.2. [Q33DR3-1]
XP_006512914.1. XM_006512851.1. [Q33DR3-1]
UniGeneMm.490430.

3D structure databases

ProteinModelPortalQ33DR3.
SMRQ33DR3. Positions 73-385.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000093393.

PTM databases

PhosphoSiteQ33DR3.

Proteomic databases

MaxQBQ33DR3.
PaxDbQ33DR3.
PRIDEQ33DR3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000095725; ENSMUSP00000093393; ENSMUSG00000038240. [Q33DR3-1]
ENSMUST00000159139; ENSMUSP00000124864; ENSMUSG00000038240. [Q33DR3-2]
GeneID71365.
KEGGmmu:71365.
UCSCuc007ezh.2. mouse. [Q33DR3-3]
uc007ezi.2. mouse. [Q33DR3-1]
uc011xdk.1. mouse. [Q33DR3-2]

Organism-specific databases

CTD57107.
MGIMGI:1918615. Pdss2.

Phylogenomic databases

eggNOGCOG0142.
GeneTreeENSGT00530000063378.
HOGENOMHOG000294216.
HOVERGENHBG058860.
InParanoidB2RWA7.
KOK12505.
OMANNLQMRG.
OrthoDBEOG7XPZ5X.
PhylomeDBQ33DR3.
TreeFamTF354277.

Enzyme and pathway databases

UniPathwayUPA00232.

Gene expression databases

ArrayExpressQ33DR3.
BgeeQ33DR3.
GenevestigatorQ33DR3.

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.
ProtoNetSearch...

Other

ChiTaRSPDSS2. mouse.
NextBio333637.
PROQ33DR3.
SOURCESearch...

Entry information

Entry nameDLP1_MOUSE
AccessionPrimary (citable) accession number: Q33DR3
Secondary accession number(s): B2RWA7 expand/collapse secondary AC list , B2RWF3, Q3USU6, Q9D3K7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: July 9, 2014
This is version 73 of the entry and version 2 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