ID   FPPS_RAT                Reviewed;         353 AA.
AC   P05369; Q6GT82;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   04-NOV-2008, entry version 75.
DE   RecName: Full=Farnesyl pyrophosphate synthetase;
DE            Short=FPP synthetase;
DE            Short=FPS;
DE   AltName: Full=Farnesyl diphosphate synthetase;
DE   AltName: Full=Cholesterol-regulated 39 kDa protein;
DE            Short=CR 39;
DE   Includes:
DE     RecName: Full=Dimethylallyltranstransferase;
DE              EC=2.5.1.1;
DE   Includes:
DE     RecName: Full=Geranyltranstransferase;
DE              EC=2.5.1.10;
GN   Name=Fdps;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=88038866; PubMed=3670308;
RA   Clarke C.F., Tanaka R.D., Svenson K., Wamsley M., Fogelman A.M.,
RA   Edwards P.A.;
RT   "Molecular cloning and sequence of a cholesterol-repressible enzyme
RT   related to prenyltransferase in the isoprene biosynthetic pathway.";
RL   Mol. Cell. Biol. 7:3138-3146(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION.
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RX   MEDLINE=90220617; PubMed=2325654;
RA   Teruya J.H., Kutsunai S.Y., Spear D.H., Edwards P.A., Clarke C.F.;
RT   "Testis-specific transcription initiation sites of rat farnesyl
RT   pyrophosphate synthetase mRNA.";
RL   Mol. Cell. Biol. 10:2315-2326(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-110.
RC   TISSUE=Pituitary;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Key enzyme in isoprenoid biosynthesis which catalyzes
CC       the formation of farnesyl diphosphate (FPP), a precursor for
CC       several classes of essential metabolites including sterols,
CC       dolichols, carotenoids, and ubiquinones. FPP also serves as
CC       substrate for protein farnesylation and geranylgeranylation.
CC       Catalyzes the sequential condensation of isopentenyl pyrophosphate
CC       with the allylic pyrophosphates, dimethylallyl pyrophosphate, and
CC       then with the resultant geranylpyrophosphate to the ultimate
CC       product farnesyl pyrophosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl
CC       diphosphate = diphosphate + geranyl diphosphate.
CC   -!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate
CC       = diphosphate + trans,trans-farnesyl diphosphate.
CC   -!- ENZYME REGULATION: Inactivated by interferon-induced RSAD2. This
CC       inactivation may result of disruption of lipid rafts at the plasma
CC       membrane, and thus have an antiviral effect since many envelopped
CC       viruses need lipid rafts to bud efficiently out of the cell (By
CC       similarity).
CC   -!- PATHWAY: Isoprenoid biosynthesis; farnesyl-PP biosynthesis;
CC       farnesyl-PP from geranyl-PP and isopentenyl-PP: step 1/1.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranyl-PP biosynthesis;
CC       geranyl-PP from dimethylallyl-PP and isopentenyl-PP: step 1/1.
CC   -!- SUBUNIT: Homodimer. Interacts with RSAD2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Testis, liver, kidney, brain and adrenal
CC       gland.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthetase family.
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DR   EMBL; M34477; AAA41143.1; -; mRNA.
DR   EMBL; M17300; AAA40960.1; ALT_SEQ; mRNA.
DR   EMBL; BC059125; AAH59125.1; -; mRNA.
DR   PIR; A34713; A34713.
DR   PIR; B34713; B34713.
DR   RefSeq; NP_114028.1; -.
DR   UniGene; Rn.2848; -.
DR   HSSP; P08836; 1UBY.
DR   SMR; P05369; 8-353.
DR   GeneID; 83791; -.
DR   KEGG; rno:83791; -.
DR   RGD; 68953; Fdps.
DR   HOVERGEN; P05369; -.
DR   LinkHub; P05369; -.
DR   NextBio; 616373; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:EC.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IEA:EC.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR008949; Terpenoid_synth.
DR   Gene3D; G3DSA:1.10.600.10; Terpenoid_synth; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHET_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHET_2; 1.
PE   2: Evidence at transcript level;
KW   Cholesterol biosynthesis; Cytoplasm; Isoprene biosynthesis;
KW   Lipid synthesis; Steroid biosynthesis; Sterol biosynthesis;
KW   Transferase.
FT   CHAIN         1    353       Farnesyl pyrophosphate synthetase.
FT                                /FTId=PRO_0000123946.
FT   ACT_SITE    192    192       By similarity.
FT   VARIANT     110    110       Y -> H.
SQ   SEQUENCE   353 AA;  40830 MW;  27FD7E0DD6FEA001 CRC64;
     MNGDQKLDVH NQEKQNFIQH FSQIVKVLTE DELGHPEKGD AITRIKEVLE YNTVGGKYNR
     GLTVVQTFQE LVEPRKQDAE SLQRALTVGW CVELLQAFFL VLDDIMDSSY TRRGQICWYQ
     KPGIGLDAIN DALLLEAAIY RLLKFYCREQ PYYLNLLELF LQSSYQTEIG QTLDLITAPQ
     GQVDLGRYTE KRYKSIVKYK TAFYSFYLPI AAAMYMAGID GEKEHANALK ILLEMGEFFQ
     IQDDYLDLFG DPSVTGKVGT DIQDNKCSWL VVQCLLRATP QQRQILEENY GQKDPEKVAR
     VKALYEELDL RSVFFKYEED SYNRLKSLIE QCSAPLPPSI FLELANKIYK RRK
//