ID   DPS1_MOUSE              Reviewed;         409 AA.
AC   Q33DR2; B8JJW9; Q9WU69;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=All trans-polyprenyl-diphosphate synthase PDSS1 {ECO:0000305};
DE   AltName: Full=All-trans-decaprenyl-diphosphate synthase subunit 1 {ECO:0000250|UniProtKB:Q5T2R2};
DE            EC=2.5.1.91 {ECO:0000250|UniProtKB:Q5T2R2};
DE   AltName: Full=Decaprenyl-diphosphate synthase subunit 1 {ECO:0000312|MGI:MGI:1889278};
DE   AltName: Full=Solanesyl-diphosphate synthase subunit 1;
DE   AltName: Full=Trans-prenyltransferase 1;
DE            Short=TPT 1;
GN   Name=Pdss1 {ECO:0000312|MGI:MGI:1889278};
GN   Synonyms=Dps1, Sps1 {ECO:0000303|PubMed:16262699}, Tprt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=16262699; DOI=10.1111/j.1742-4658.2005.04956.x;
RA   Saiki R., Nagata A., Kainou T., Matsuda H., Kawamukai M.;
RT   "Characterization of solanesyl and decaprenyl diphosphate synthases in mice
RT   and humans.";
RL   FEBS J. 272:5606-5622(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 67-409.
RX   PubMed=10972372; DOI=10.1016/s0140-6736(00)02531-9;
RA   Roetig A., Appelkvist E.-L., Geromel V., Chretien D., Kadhom N., Edery P.,
RA   Lebideau M., Dallner G., Munnich A., Ernster L., Rustin P.;
RT   "Quinone-responsive multiple respiratory-chain dysfunction due to
RT   widespread coenzyme Q10 deficiency.";
RL   Lancet 356:391-395(2000).
CC   -!- FUNCTION: Heterotetrameric enzyme that catalyzes the condensation of
CC       farnesyl diphosphate (FPP), which acts as a primer, and isopentenyl
CC       diphosphate (IPP) to produce prenyl diphosphates of varying chain
CC       lengths and participates in the determination of the side chain of
CC       ubiquinone (PubMed:16262699). Supplies nona and decaprenyl diphosphate,
CC       the precursors for the side chain of the isoprenoid quinones
CC       ubiquinone-9 (Q9)and ubiquinone-10 (Q10) respectively
CC       (PubMed:16262699). The enzyme adds isopentenyl diphosphate molecules
CC       sequentially to farnesyl diphosphate with trans stereochemistry
CC       (PubMed:16262699). {ECO:0000269|PubMed:16262699}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate =
CC         all-trans-decaprenyl diphosphate + 7 diphosphate;
CC         Xref=Rhea:RHEA:27802, ChEBI:CHEBI:33019, ChEBI:CHEBI:60721,
CC         ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.91;
CC         Evidence={ECO:0000250|UniProtKB:Q5T2R2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27803;
CC         Evidence={ECO:0000250|UniProtKB:Q5T2R2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + 6 isopentenyl diphosphate =
CC         all-trans-nonaprenyl diphosphate + 6 diphosphate;
CC         Xref=Rhea:RHEA:55364, ChEBI:CHEBI:33019, ChEBI:CHEBI:58391,
CC         ChEBI:CHEBI:128769, ChEBI:CHEBI:175763;
CC         Evidence={ECO:0000269|PubMed:16262699};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55365;
CC         Evidence={ECO:0000305|PubMed:16262699};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC   -!- SUBUNIT: Heterotetramer composed of 2 PDSS1/DPS1 and 2 PDSS2/DLP1
CC       subunits. {ECO:0000269|PubMed:16262699}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD24462.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH26820.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB210841; BAE48219.1; -; mRNA.
DR   EMBL; CT030013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026820; AAH26820.1; ALT_INIT; mRNA.
DR   EMBL; BC107273; AAI07274.2; -; mRNA.
DR   EMBL; BC107274; AAI07275.2; -; mRNA.
DR   EMBL; AF118855; AAD24462.1; ALT_INIT; mRNA.
DR   CCDS; CCDS38057.1; -.
DR   RefSeq; NP_062374.2; NM_019501.3.
DR   AlphaFoldDB; Q33DR2; -.
DR   SMR; Q33DR2; -.
DR   BioGRID; 207803; 3.
DR   STRING; 10090.ENSMUSP00000055689; -.
DR   iPTMnet; Q33DR2; -.
DR   PhosphoSitePlus; Q33DR2; -.
DR   SwissPalm; Q33DR2; -.
DR   EPD; Q33DR2; -.
DR   MaxQB; Q33DR2; -.
DR   PaxDb; 10090-ENSMUSP00000055689; -.
DR   PeptideAtlas; Q33DR2; -.
DR   ProteomicsDB; 277605; -.
DR   Pumba; Q33DR2; -.
DR   Antibodypedia; 25917; 75 antibodies from 17 providers.
DR   DNASU; 56075; -.
DR   Ensembl; ENSMUST00000053729.14; ENSMUSP00000055689.8; ENSMUSG00000026784.15.
DR   GeneID; 56075; -.
DR   KEGG; mmu:56075; -.
DR   UCSC; uc008inq.1; mouse.
DR   AGR; MGI:1889278; -.
DR   CTD; 23590; -.
DR   MGI; MGI:1889278; Pdss1.
DR   VEuPathDB; HostDB:ENSMUSG00000026784; -.
DR   eggNOG; KOG0776; Eukaryota.
DR   GeneTree; ENSGT00940000153498; -.
DR   HOGENOM; CLU_014015_1_2_1; -.
DR   InParanoid; Q33DR2; -.
DR   OMA; GKQMRPM; -.
DR   OrthoDB; 25272at2759; -.
DR   PhylomeDB; Q33DR2; -.
DR   TreeFam; TF313548; -.
DR   Reactome; R-MMU-2142789; Ubiquinol biosynthesis.
DR   UniPathway; UPA00232; -.
DR   BioGRID-ORCS; 56075; 17 hits in 78 CRISPR screens.
DR   ChiTaRS; Pdss1; mouse.
DR   PRO; PR:Q33DR2; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q33DR2; Protein.
DR   Bgee; ENSMUSG00000026784; Expressed in paneth cell and 235 other cell types or tissues.
DR   ExpressionAtlas; Q33DR2; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:1990234; C:transferase complex; IDA:BHF-UCL.
DR   GO; GO:0097269; F:all-trans-decaprenyl-diphosphate synthase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:HGNC-UCL.
DR   GO; GO:0000010; F:trans-hexaprenyltranstransferase activity; IEA:Ensembl.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:HGNC-UCL.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IDA:HGNC-UCL.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   PANTHER; PTHR12001; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR12001:SF69; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
DR   Genevisible; Q33DR2; MM.
PE   1: Evidence at protein level;
KW   Isoprene biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW   Mitochondrion; Reference proteome; Transferase; Ubiquinone biosynthesis.
FT   CHAIN           1..409
FT                   /note="All trans-polyprenyl-diphosphate synthase PDSS1"
FT                   /id="PRO_0000123976"
FT   BINDING         128
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         131
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         167
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         178
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         178
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         183
FT                   /ligand="an all-trans-polyprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58914"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         260
FT                   /ligand="an all-trans-polyprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58914"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="an all-trans-polyprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58914"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="an all-trans-polyprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58914"
FT                   /evidence="ECO:0000250"
FT   BINDING         315
FT                   /ligand="an all-trans-polyprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58914"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        1
FT                   /note="M -> V (in Ref. 3; AAH26820)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   409 AA;  45895 MW;  EF94459BD78F48B2 CRC64;
     MAMRWSCWRR GCSWRPTAVG SPRRERPGCV EPLGTRAASD TRAQIPYFSL MKILMSASPT
     MHSISQFHQR TPAMCSCRQT QSGEKYSDPF KLGWRDLKGL YEDIRKELHI STRELKDMSE
     YYFDGKGKAF RPIIVVLMAR ACNIHHNNAR EMQASQRSIA LVAEMIHTAT LVHDDVIDDA
     SSRRGKHTVN KIWGEKKAVL AGDLILSAAS VALARIGNTA VVSMLAQVIE DLVRGEFLQL
     GSKENENERF AHYLEKTFKK TASLIANSCK AVSVLGCPDP VVHEIAYQYG KNVGIAFQLI
     DDVLDFTSCS DQMGKPTSAD LKLGIATGPV LFACQQFPEM NAMIMRRFSL PGDVDRARQY
     VLQSDGVQQT TYLAQQYCHK AVREIRKLRP STERDALIQL SESVLTRDK
//