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Protein

Decaprenyl-diphosphate synthase subunit 2

Gene

Pdss2

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

Functioni

Supplies decaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone-10.1 Publication

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. protein heterodimerization activity Source: HGNC
  2. trans-hexaprenyltranstransferase activity Source: Ensembl

GO - Biological processi

  1. isoprenoid biosynthetic process Source: HGNC
  2. protein heterotetramerization Source: MGI
  3. regulation of body fluid levels Source: MGI
  4. ubiquinone biosynthetic process Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Isoprene biosynthesis, Ubiquinone biosynthesis

Enzyme and pathway databases

ReactomeiREACT_196568. Ubiquinol biosynthesis.
UniPathwayiUPA00232.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Pdss2
Synonyms:Dlp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1918615. Pdss2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. mitochondrion Source: MGI
  3. transferase complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 401401Decaprenyl-diphosphate synthase subunit 2PRO_0000123979Add
BLAST

Proteomic databases

MaxQBiQ33DR3.
PaxDbiQ33DR3.
PRIDEiQ33DR3.

PTM databases

PhosphoSiteiQ33DR3.

Expressioni

Gene expression databases

BgeeiQ33DR3.
ExpressionAtlasiQ33DR3. baseline and differential.
GenevestigatoriQ33DR3.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000093393.

Structurei

3D structure databases

ProteinModelPortaliQ33DR3.
SMRiQ33DR3. Positions 73-385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPP/GGPP synthase family.Curated

Phylogenomic databases

eggNOGiCOG0142.
GeneTreeiENSGT00530000063378.
HOGENOMiHOG000294216.
HOVERGENiHBG058860.
InParanoidiQ33DR3.
KOiK12505.
OMAiPEQEWEC.
OrthoDBiEOG7XPZ5X.
PhylomeDBiQ33DR3.
TreeFamiTF354277.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
IPR008949. Terpenoid_synth.
[Graphical view]
PANTHERiPTHR12001. PTHR12001. 1 hit.
PfamiPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q33DR3-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSLRQLLLRL SGYLGASGPP SRHWWYFRSL DSISSAGSWR GRSSRSPAHW
60 70 80 90 100
NQVVSEAEKI VGYPASFMSL RCLLSDELSN IAMQVRKLVG TGHPLLTTAR
110 120 130 140 150
ALVHDSRHNL QLRGLVVLLI SKAAGPSTRN AACQNYDMVS GVYSCQRSLA
160 170 180 190 200
EITELIHTAL LVHRGIVNLS ELQSSDGPLK DMQFGNKIAI LSGDFLLANA
210 220 230 240 250
CNGLALLQNT KVVELLSSAL MDLVHGVYQE NSASTKENSI PDDIGISTWK
260 270 280 290 300
EQTFLSHCAL LAKSCQAAME LAKHDAAVQD MAFQYGKHMA MSHKINADLQ
310 320 330 340 350
PFIKDKASDS KTFNLNSAPV VLHQEFLGRD LWIKQIGEAQ EKGSLNYSKL
360 370 380 390 400
RETIKAGKGV TSAIDLCRYH GNKALEALES FPPSEARSAL ENIVFAVTRF

S
Length:401
Mass (Da):43,980
Last modified:January 24, 2006 - v2
Checksum:iDB7835A83019E5AA
GO
Isoform 2 (identifier: Q33DR3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     350-352: LRE → VVS
     353-401: Missing.

Note: No experimental confirmation available.

Show »
Length:352
Mass (Da):38,618
Checksum:i22895FB1C1B55490
GO
Isoform 3 (identifier: Q33DR3-3) [UniParc]FASTAAdd to basket

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

Show »
Length:264
Mass (Da):28,599
Checksum:iEDE79A90E66D6F6E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321A → S in BAE48218 (PubMed:16262699).Curated
Sequence conflicti204 – 2041L → I in BAB30693 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei213 – 26452VELLS…LLAKS → KAERLTCAHTASGVSCLAAE ATDRGVCVLLLSSSMWMLTE TDDGDLGSDNMK in isoform 3. 2 PublicationsVSP_017102Add
BLAST
Alternative sequencei265 – 401137Missing in isoform 3. 2 PublicationsVSP_017103Add
BLAST
Alternative sequencei350 – 3523LRE → VVS in isoform 2. 1 PublicationVSP_017104
Alternative sequencei353 – 40149Missing in isoform 2. 1 PublicationVSP_017105Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35891.1. [Q33DR3-1]
CCDS48552.1. [Q33DR3-2]
RefSeqiNP_001161761.1. NM_001168289.1. [Q33DR3-2]
NP_082048.2. NM_027772.2. [Q33DR3-1]
XP_006512914.1. XM_006512851.1. [Q33DR3-1]
UniGeneiMm.490430.

Genome annotation databases

EnsembliENSMUST00000095725; ENSMUSP00000093393; ENSMUSG00000038240. [Q33DR3-1]
ENSMUST00000159139; ENSMUSP00000124864; ENSMUSG00000038240. [Q33DR3-2]
GeneIDi71365.
KEGGimmu:71365.
UCSCiuc007ezh.2. mouse. [Q33DR3-3]
uc007ezi.2. mouse. [Q33DR3-1]
uc011xdk.1. mouse. [Q33DR3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35891.1. [Q33DR3-1]
CCDS48552.1. [Q33DR3-2]
RefSeqiNP_001161761.1. NM_001168289.1. [Q33DR3-2]
NP_082048.2. NM_027772.2. [Q33DR3-1]
XP_006512914.1. XM_006512851.1. [Q33DR3-1]
UniGeneiMm.490430.

3D structure databases

ProteinModelPortaliQ33DR3.
SMRiQ33DR3. Positions 73-385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000093393.

PTM databases

PhosphoSiteiQ33DR3.

Proteomic databases

MaxQBiQ33DR3.
PaxDbiQ33DR3.
PRIDEiQ33DR3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000095725; ENSMUSP00000093393; ENSMUSG00000038240. [Q33DR3-1]
ENSMUST00000159139; ENSMUSP00000124864; ENSMUSG00000038240. [Q33DR3-2]
GeneIDi71365.
KEGGimmu:71365.
UCSCiuc007ezh.2. mouse. [Q33DR3-3]
uc007ezi.2. mouse. [Q33DR3-1]
uc011xdk.1. mouse. [Q33DR3-2]

Organism-specific databases

CTDi57107.
MGIiMGI:1918615. Pdss2.

Phylogenomic databases

eggNOGiCOG0142.
GeneTreeiENSGT00530000063378.
HOGENOMiHOG000294216.
HOVERGENiHBG058860.
InParanoidiQ33DR3.
KOiK12505.
OMAiPEQEWEC.
OrthoDBiEOG7XPZ5X.
PhylomeDBiQ33DR3.
TreeFamiTF354277.

Enzyme and pathway databases

UniPathwayiUPA00232.
ReactomeiREACT_196568. Ubiquinol biosynthesis.

Miscellaneous databases

ChiTaRSiPdss2. mouse.
NextBioi333637.
PROiQ33DR3.
SOURCEiSearch...

Gene expression databases

BgeeiQ33DR3.
ExpressionAtlasiQ33DR3. baseline and differential.
GenevestigatoriQ33DR3.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
IPR008949. Terpenoid_synth.
[Graphical view]
PANTHERiPTHR12001. PTHR12001. 1 hit.
PfamiPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiDLP1_MOUSE
AccessioniPrimary (citable) accession number: Q33DR3
Secondary accession number(s): B2RWA7
, B2RWF3, Q3USU6, Q9D3K7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: March 4, 2015
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3

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 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.