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Q33DR3

- DLP1_MOUSE

UniProt

Q33DR3 - DLP1_MOUSE

Protein

Decaprenyl-diphosphate synthase subunit 2

Gene

Pdss2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 2 (24 Jan 2006)
      Previous versions | rss
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    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

    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. mitochondrion Source: MGI

    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

    ArrayExpressiQ33DR3.
    BgeeiQ33DR3.
    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.
    InParanoidiB2RWA7.
    KOiK12505.
    OMAiNNLQMRG.
    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. Align

    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

    MSLRQLLLRL SGYLGASGPP SRHWWYFRSL DSISSAGSWR GRSSRSPAHW    50
    NQVVSEAEKI VGYPASFMSL RCLLSDELSN IAMQVRKLVG TGHPLLTTAR 100
    ALVHDSRHNL QLRGLVVLLI SKAAGPSTRN AACQNYDMVS GVYSCQRSLA 150
    EITELIHTAL LVHRGIVNLS ELQSSDGPLK DMQFGNKIAI LSGDFLLANA 200
    CNGLALLQNT KVVELLSSAL MDLVHGVYQE NSASTKENSI PDDIGISTWK 250
    EQTFLSHCAL LAKSCQAAME LAKHDAAVQD MAFQYGKHMA MSHKINADLQ 300
    PFIKDKASDS KTFNLNSAPV VLHQEFLGRD LWIKQIGEAQ EKGSLNYSKL 350
    RETIKAGKGV TSAIDLCRYH GNKALEALES FPPSEARSAL ENIVFAVTRF 400
    S 401
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS35891.1. [Q33DR3-1 ]
    CCDS48552.1. [Q33DR3-2 ]
    RefSeqi NP_001161761.1. NM_001168289.1. [Q33DR3-2 ]
    NP_082048.2. NM_027772.2. [Q33DR3-1 ]
    XP_006512914.1. XM_006512851.1. [Q33DR3-1 ]
    UniGenei Mm.490430.

    3D structure databases

    ProteinModelPortali Q33DR3.
    SMRi Q33DR3. Positions 73-385.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000093393.

    PTM databases

    PhosphoSitei Q33DR3.

    Proteomic databases

    MaxQBi Q33DR3.
    PaxDbi Q33DR3.
    PRIDEi Q33DR3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000095725 ; ENSMUSP00000093393 ; ENSMUSG00000038240 . [Q33DR3-1 ]
    ENSMUST00000159139 ; ENSMUSP00000124864 ; ENSMUSG00000038240 . [Q33DR3-2 ]
    GeneIDi 71365.
    KEGGi mmu:71365.
    UCSCi uc007ezh.2. mouse. [Q33DR3-3 ]
    uc007ezi.2. mouse. [Q33DR3-1 ]
    uc011xdk.1. mouse. [Q33DR3-2 ]

    Organism-specific databases

    CTDi 57107.
    MGIi MGI:1918615. Pdss2.

    Phylogenomic databases

    eggNOGi COG0142.
    GeneTreei ENSGT00530000063378.
    HOGENOMi HOG000294216.
    HOVERGENi HBG058860.
    InParanoidi B2RWA7.
    KOi K12505.
    OMAi NNLQMRG.
    OrthoDBi EOG7XPZ5X.
    PhylomeDBi Q33DR3.
    TreeFami TF354277.

    Enzyme and pathway databases

    UniPathwayi UPA00232 .
    Reactomei REACT_196568. Ubiquinol biosynthesis.

    Miscellaneous databases

    ChiTaRSi PDSS2. mouse.
    NextBioi 333637.
    PROi Q33DR3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q33DR3.
    Bgeei Q33DR3.
    Genevestigatori Q33DR3.

    Family and domain databases

    Gene3Di 1.10.600.10. 1 hit.
    InterProi IPR000092. Polyprenyl_synt.
    IPR017446. Polyprenyl_synth-rel.
    IPR008949. Terpenoid_synth.
    [Graphical view ]
    PANTHERi PTHR12001. PTHR12001. 1 hit.
    Pfami PF00348. polyprenyl_synt. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48576. SSF48576. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 75 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