DLP1_RAT
ID DLP1_RAT Reviewed; 401 AA.
AC Q5U2R1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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|RGD:1359372};
DE AltName: Full=Solanesyl-diphosphate synthase subunit 2 {ECO:0000250|UniProtKB:Q33DR3};
GN Name=Pdss2 {ECO:0000312|RGD:1359372};
GN Synonyms=Dlp1 {ECO:0000250|UniProtKB:Q86YH6};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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).
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. Supplies nona and decaprenyl diphosphate, the precursors
CC for the side chain of the isoprenoid quinones ubiquinone-9 (Q9) and
CC ubiquinone-10 (Q10) respectively. The enzyme adds isopentenyl
CC diphosphate molecules sequentially to farnesyl diphosphate with trans
CC stereochemistry (By similarity). May play a role during cerebellar
CC development (By similarity). May regulate mitochondrial respiratory
CC chain function (By similarity). {ECO:0000250|UniProtKB:Q33DR3,
CC ECO:0000250|UniProtKB:Q86YH6}.
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:0000250|UniProtKB:Q33DR3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55365;
CC Evidence={ECO:0000250|UniProtKB:Q33DR3};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000250|UniProtKB:Q33DR3}.
CC -!- SUBUNIT: Heterotetramer composed of 2 PDSS1/DPS1 and 2 PDSS2/DLP1
CC subunits. {ECO:0000250|UniProtKB:Q33DR3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; BC085898; AAH85898.1; -; mRNA.
DR RefSeq; NP_001014271.1; NM_001014249.1.
DR AlphaFoldDB; Q5U2R1; -.
DR SMR; Q5U2R1; -.
DR STRING; 10116.ENSRNOP00000059060; -.
DR PaxDb; Q5U2R1; -.
DR Ensembl; ENSRNOT00000067169; ENSRNOP00000059060; ENSRNOG00000042962.
DR GeneID; 365592; -.
DR KEGG; rno:365592; -.
DR UCSC; RGD:1359372; rat.
DR CTD; 57107; -.
DR RGD; 1359372; Pdss2.
DR eggNOG; KOG0776; Eukaryota.
DR GeneTree; ENSGT00940000153498; -.
DR HOGENOM; CLU_014015_3_1_1; -.
DR InParanoid; Q5U2R1; -.
DR OMA; GRNNMQA; -.
DR OrthoDB; 858404at2759; -.
DR PhylomeDB; Q5U2R1; -.
DR Reactome; R-RNO-2142789; Ubiquinol biosynthesis.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q5U2R1; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000042962; Expressed in heart and 20 other tissues.
DR Genevisible; Q5U2R1; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:1990234; C:transferase complex; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0000010; F:trans-hexaprenyltranstransferase activity; IEA:Ensembl.
DR GO; GO:0050347; F:trans-octaprenyltranstransferase activity; IEA:Ensembl.
DR GO; GO:0021549; P:cerebellum development; ISS:UniProtKB.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; ISO:RGD.
DR GO; GO:0050878; P:regulation of body fluid levels; ISO:RGD.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; ISO:RGD.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 2: Evidence at transcript level;
KW Isoprene biosynthesis; Lipid metabolism; Mitochondrion; Reference proteome;
KW Transferase; Ubiquinone biosynthesis.
FT CHAIN 1..401
FT /note="All trans-polyprenyl-diphosphate synthase PDSS2"
FT /id="PRO_0000123980"
SQ SEQUENCE 401 AA; 44295 MW; 46F8D7D24CF3E874 CRC64;
MSLRQLLLRL SGYLGASGPP NRHWWYFRSL DTISSVGSWR GRSSRSPAHW NQVVSEAEKI
VGYPASFMSL RCLLSDELSN VAMQVRKLVG TQHPLLTTAR GFVHDSRHNL QLRGLVVLLI
SKAAGPSTRN SSSQNYDMVS GIYSCQRNLA EITELIHTAL LVHRGIVNLS ELQSSDGPLK
DMKFGNKIAV LSGDFLLANA CNGLALLQNT KVVELLASAL MDLVQGIYQE NSASTQGNPI
PDDIRISTWK EQTFLSHCAL LAKSCKAAME LAKHDAAVQD MAFQYGKHMA MSHKINSDLQ
PFIKDKASDS KTFNLNSAPV VLHQEFLGRD LWIKQIGEAQ EKGRLNYTKL RETIKAGKGV
TSAIDLCRYH GNKALEALES FPPSEARSAL ENIVFAVTRF S
