(data stored in ACNUC14511 zone)

HOGENOM: RAT2_PE1192

ID   RAT2_PE1192                          STANDARD;      PRT;   287 AA.
AC   RAT2_PE1192; P05369; Q6GT82;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   Flags: Fragments;
DE   RecName: Full=Farnesyl pyrophosphate synthase; Short=FPP synthase;
DE   Short=FPS; EC=2.5.1.10;AltName: Full=(2E,6E)-farnesyl diphosphate
DE   synthase;AltName: Full=Cholesterol-regulated 39 kDa protein; Short=CR
DE   39;AltName: Full=Dimethylallyltranstransferase; EC=2.5.1 1;AltName:
DE   Full=Farnesyl diphosphate synthase;AltName: Full=Geranyltranstransferase;
DE   (RAT2.PE1192).
GN   Name=Fdps;
OS   RATTUS NORVEGICUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RAT2.PE1192.
CC       Rattus norvegicus chromosome 2 RGSC3.4  sequence 1..258207540
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:FPPS_RAT
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 + (2E,6E)-farnesyl diphosphate.
CC   -!- COFACTOR: Binds 3 magnesium ions per subunit (By similarity).
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 diphosphate
CC       biosynthesis; farnesyl diphosphate from geranyl diphosphate and
CC       isopentenyl diphosphate: step 1/1.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate
CC       biosynthesis; geranyl diphosphate from dimethylallyl diphosphate
CC       and isopentenyl diphosphate: 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 synthase family.
CC   -!- GENE_FAMILY: HOG000160912 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Rattus_norvegicus;ENSRNOG00000043377;ENSRNOT00000065065;ENSRNOP00000058918.
DR   EMBL; BC059125; - ;
DR   EMBL; M17300; - ;
DR   EMBL; M34477; - ;
DR   UniProtKB/Swiss-Prot; P05369; Q6GT82; -.
DR   EMBL; M34477; AAA41143.1; -; mRNA.
DR   EMBL; M17300; AAA40960.1; ALT_SEQ; mRNA.
DR   EMBL; BC059125; AAH59125.1; -; mRNA.
DR   IPI; IPI00325147; -.
DR   PIR; A34713; A34713.
DR   PIR; B34713; B34713.
DR   RefSeq; NP_114028.1; NM_031840.1.
DR   UniGene; Rn.2848; -.
DR   ProteinModelPortal; P05369; -.
DR   SMR; P05369; 8-353.
DR   STRING; P05369; -.
DR   PhosphoSite; P05369; -.
DR   PRIDE; P05369; -.
DR   GeneID; 83791; -.
DR   KEGG; rno:83791; -.
DR   CTD; 2224; -.
DR   RGD; 68953; Fdps.
DR   eggNOG; roNOG14739; -.
DR   GeneTree; ENSGT00530000064127; -.
DR   OrthoDB; EOG4ZGPCS; -.
DR   PhylomeDB; P05369; -.
DR   NextBio; 616373; -.
DR   Genevestigator; P05369; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
DR   GO; GO:0005777; C:peroxisome; IDA:RGD.
DR   GO; GO:0005625; C:soluble fraction; IDA:RGD.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:EC.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; IGI:RGD.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071398; P:cellular response to fatty acid; IEP:RGD.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; TAS:RGD.
DR   GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IDA:RGD.
DR   GO; GO:0008584; P:male gonad development; IEP:RGD.
DR   GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; IMP:RGD.
DR   GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IMP:RGD.
DR   GO; GO:0070723; P:response to cholesterol; IEP:RGD.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0043434; P:response to peptide hormone stimulus; IEP:RGD.
DR   GO; GO:0033574; P:response to testosterone stimulus; IEP:RGD.
DR   GO; GO:0007283; P:spermatogenesis; IEP:RGD.
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   SUPFAM; SSF48576; Terpenoid_synth; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
DR   HOGENOMDNA; RAT2.PE1192; -.
KW   ENSRNOG00000043377820036002503210000011;
KW   Fdps; RGD1561594; FPPS_RAT; BC059125; M17300; M34477;
KW   Acetylation; Cholesterol biosynthesis; Complete proteome; Cytoplasm;
KW   Isoprene biosynthesis; Lipid synthesis; Magnesium; Metal-binding;
KW   Reference proteome; Steroid biosynthesis; Sterol biosynthesis;
KW   Transferase.
SQ   SEQUENCE   287 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNGDQKLDVH NQEKQNFIQH FSQIVKVLTE DELGHPEKGD AITRIKEVLE YNTVGGKYNR
     GLTVVQTFQE LVEPRKQDAE SLQRALTVGW CVELLQAFFL VLDDIMDSSH TRRGQICWYQ
     KPGIGLDAIN DALLLEAAIY RLLKFYCREQ PYYLNLLELF LQSSYQTEIG QTLDLITAPQ
     GQVDLGRYTE KRYKSIVKYK TAFYSFYLPI AAAMYMAGID GEKEHANALK ILLEMGEFFQ
     IQDDYLDLFG DPSVTGKVGT DIQDNKCSWL VVQCLLRATP QQRQILE
//

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