DPS1_MOUSE
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 03-AUG-2022, entry version 120.
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; Q33DR2; -.
DR PeptideAtlas; Q33DR2; -.
DR PRIDE; Q33DR2; -.
DR ProteomicsDB; 277605; -.
DR Antibodypedia; 25917; 61 antibodies from 17 providers.
DR DNASU; 56075; -.
DR Ensembl; ENSMUST00000053729; ENSMUSP00000055689; ENSMUSG00000026784.
DR GeneID; 56075; -.
DR KEGG; mmu:56075; -.
DR UCSC; uc008inq.1; mouse.
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; 381154at2759; -.
DR PhylomeDB; Q33DR2; -.
DR TreeFam; TF313548; -.
DR Reactome; R-MMU-2142789; Ubiquinol biosynthesis.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 56075; 16 hits in 73 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 232 other tissues.
DR ExpressionAtlas; Q33DR2; baseline and differential.
DR Genevisible; Q33DR2; MM.
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; ISO:MGI.
DR GO; GO:0050347; F:trans-octaprenyltranstransferase activity; IDA:MGI.
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; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
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
