ID DLP1_MOUSE Reviewed; 401 AA.
AC Q33DR3; B2RWA7; B2RWF3; Q3USU6; Q9D3K7;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 24-JAN-2024, entry version 128.
DE RecName: Full=All trans-polyprenyl-diphosphate synthase PDSS2 {ECO:0000305};
DE AltName: Full=All-trans-decaprenyl-diphosphate synthase subunit 2 {ECO:0000250|UniProtKB:Q86YH6};
DE EC=2.5.1.91 {ECO:0000250|UniProtKB:Q86YH6};
DE AltName: Full=Decaprenyl-diphosphate synthase subunit 2 {ECO:0000312|MGI:MGI:1918615};
DE AltName: Full=Solanesyl-diphosphate synthase subunit 2;
GN Name=Pdss2 {ECO:0000312|MGI:MGI:1918615};
GN Synonyms=Dlp1 {ECO:0000303|PubMed:16262699};
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP 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 MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain;
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 DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18437205; DOI=10.1371/journal.pgen.1000061;
RA Peng M., Falk M.J., Haase V.H., King R., Polyak E., Selak M., Yudkoff M.,
RA Hancock W.W., Meade R., Saiki R., Lunceford A.L., Clarke C.F., Gasser D.L.;
RT "Primary coenzyme Q deficiency in Pdss2 mutant mice causes isolated renal
RT disease.";
RL PLoS Genet. 4:e1000061-e1000061(2008).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21871565; DOI=10.1016/j.nbd.2011.08.006;
RA Lu S., Lu L.Y., Liu M.F., Yuan Q.J., Sham M.H., Guan X.Y., Huang J.D.;
RT "Cerebellar defects in Pdss2 conditional knockout mice during embryonic
RT development and in adulthood.";
RL Neurobiol. Dis. 45:219-233(2012).
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). May play a role during cerebellar development
CC (PubMed:21871565). May regulate mitochondrial respiratory chain
CC function (PubMed:18437205). {ECO:0000269|PubMed:16262699,
CC ECO:0000269|PubMed:18437205, ECO:0000269|PubMed:21871565}.
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:Q86YH6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27803;
CC Evidence={ECO:0000250|UniProtKB:Q86YH6};
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 -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000269|PubMed:16262699}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q33DR3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q33DR3-2; Sequence=VSP_017104, VSP_017105;
CC Name=3;
CC IsoId=Q33DR3-3; Sequence=VSP_017102, VSP_017103;
CC -!- DISRUPTION PHENOTYPE: Homozygous mice for PDSS2 are embryonic lethal
CC (PubMed:18437205, PubMed:21871565). The oldest PDSS2 embryo identified
CC is at E9.5, and its morphology resembles normal E6.5 mouse embryo, so
CC the development of mutant embryo may be blocked at late gastrula stage
CC (PubMed:18437205, PubMed:21871565). Conditional knockout mice lacking
CC PDSS2 in cerebellum show severe cerebellum hypoplasia during cerebellum
CC development, whereas conditional knockout mice lacking PDSS2 in
CC Purkinje cells at postnatal stages leads to the development of
CC cerebellar ataxia (PubMed:21871565). Conditional knockout mice lacking
CC PDSS2 in glomeruli show interstitial nephritis characterized by greatly
CC dilated tubules and extensive interstitial infiltration associated with
CC hypercholesterolemia (PubMed:18437205). Liver-conditional knockout mice
CC have no overt disease but their livers have undetectable COQ9 levels,
CC impaired respiratory capacity, and significantly altered intermediary
CC metabolism (PubMed:18437205). {ECO:0000269|PubMed:18437205,
CC ECO:0000269|PubMed:21871565}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AB210840; BAE48218.1; -; mRNA.
DR EMBL; AK017329; BAB30693.1; -; mRNA.
DR EMBL; AK140091; BAE24234.1; -; mRNA.
DR EMBL; BC147693; AAI47694.1; -; mRNA.
DR EMBL; BC147694; AAI47695.1; -; mRNA.
DR EMBL; BC147752; AAI47753.1; -; mRNA.
DR EMBL; BC147753; AAI47754.1; -; mRNA.
DR CCDS; CCDS35891.1; -. [Q33DR3-1]
DR CCDS; CCDS48552.1; -. [Q33DR3-2]
DR RefSeq; NP_001161761.1; NM_001168289.1. [Q33DR3-2]
DR RefSeq; NP_082048.2; NM_027772.2. [Q33DR3-1]
DR AlphaFoldDB; Q33DR3; -.
DR SMR; Q33DR3; -.
DR STRING; 10090.ENSMUSP00000093393; -.
DR PhosphoSitePlus; Q33DR3; -.
DR EPD; Q33DR3; -.
DR MaxQB; Q33DR3; -.
DR PaxDb; 10090-ENSMUSP00000093393; -.
DR PeptideAtlas; Q33DR3; -.
DR ProteomicsDB; 279435; -. [Q33DR3-1]
DR ProteomicsDB; 279436; -. [Q33DR3-2]
DR ProteomicsDB; 279437; -. [Q33DR3-3]
DR Pumba; Q33DR3; -.
DR Antibodypedia; 32171; 390 antibodies from 24 providers.
DR Ensembl; ENSMUST00000095725.11; ENSMUSP00000093393.5; ENSMUSG00000038240.14. [Q33DR3-1]
DR Ensembl; ENSMUST00000159139.8; ENSMUSP00000124864.2; ENSMUSG00000038240.14. [Q33DR3-2]
DR GeneID; 71365; -.
DR KEGG; mmu:71365; -.
DR UCSC; uc007ezh.2; mouse. [Q33DR3-3]
DR UCSC; uc007ezi.2; mouse. [Q33DR3-1]
DR UCSC; uc011xdk.1; mouse. [Q33DR3-2]
DR AGR; MGI:1918615; -.
DR CTD; 57107; -.
DR MGI; MGI:1918615; Pdss2.
DR VEuPathDB; HostDB:ENSMUSG00000038240; -.
DR eggNOG; KOG0776; Eukaryota.
DR GeneTree; ENSGT00940000153498; -.
DR HOGENOM; CLU_014015_3_1_1; -.
DR InParanoid; Q33DR3; -.
DR OMA; HEQVRWT; -.
DR OrthoDB; 2899987at2759; -.
DR PhylomeDB; Q33DR3; -.
DR TreeFam; TF354277; -.
DR Reactome; R-MMU-2142789; Ubiquinol biosynthesis.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 71365; 20 hits in 80 CRISPR screens.
DR ChiTaRS; Pdss2; mouse.
DR PRO; PR:Q33DR3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q33DR3; Protein.
DR Bgee; ENSMUSG00000038240; Expressed in floor plate of midbrain and 197 other cell types or tissues.
DR ExpressionAtlas; Q33DR3; baseline and differential.
DR Genevisible; Q33DR3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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: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:0021549; P:cerebellum development; IMP:UniProtKB.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:HGNC-UCL.
DR GO; GO:0050878; P:regulation of body fluid levels; IMP:MGI.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IDA:HGNC-UCL.
DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR PANTHER; PTHR12001:SF55; ALL TRANS-POLYPRENYL-DIPHOSPHATE SYNTHASE PDSS2; 1.
DR PANTHER; PTHR12001; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; Terpenoid synthases; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isoprene biosynthesis; Lipid metabolism;
KW Mitochondrion; Reference proteome; Transferase; Ubiquinone biosynthesis.
FT CHAIN 1..401
FT /note="All trans-polyprenyl-diphosphate synthase PDSS2"
FT /id="PRO_0000123979"
FT VAR_SEQ 213..264
FT /note="VELLSSALMDLVHGVYQENSASTKENSIPDDIGISTWKEQTFLSHCALLAKS
FT -> KAERLTCAHTASGVSCLAAEATDRGVCVLLLSSSMWMLTETDDGDLGSDNMK (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_017102"
FT VAR_SEQ 265..401
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_017103"
FT VAR_SEQ 350..352
FT /note="LRE -> VVS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017104"
FT VAR_SEQ 353..401
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017105"
FT CONFLICT 132
FT /note="A -> S (in Ref. 1; BAE48218)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="L -> I (in Ref. 2; BAB30693)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 43980 MW; DB7835A83019E5AA CRC64;
MSLRQLLLRL SGYLGASGPP SRHWWYFRSL DSISSAGSWR GRSSRSPAHW NQVVSEAEKI
VGYPASFMSL RCLLSDELSN IAMQVRKLVG TGHPLLTTAR ALVHDSRHNL QLRGLVVLLI
SKAAGPSTRN AACQNYDMVS GVYSCQRSLA EITELIHTAL LVHRGIVNLS ELQSSDGPLK
DMQFGNKIAI LSGDFLLANA CNGLALLQNT KVVELLSSAL MDLVHGVYQE NSASTKENSI
PDDIGISTWK EQTFLSHCAL LAKSCQAAME LAKHDAAVQD MAFQYGKHMA MSHKINADLQ
PFIKDKASDS KTFNLNSAPV VLHQEFLGRD LWIKQIGEAQ EKGSLNYSKL RETIKAGKGV
TSAIDLCRYH GNKALEALES FPPSEARSAL ENIVFAVTRF S
//
