(data stored in ACNUC14511 zone)

HOGENOM: MOUSE3_PE908

ID   MOUSE3_PE908                         STANDARD;      PRT;   353 AA.
AC   MOUSE3_PE908; Q920E5;
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   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   (MOUSE3.PE908).
GN   Name=Fdps;
OS   MUS MUSCULUS.
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; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE3.PE908.
CC       Mus musculus chromosome 3 NCBIM37  sequence 1..159599783 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:FPPS_MOUSE
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
CC   -!- GENE_FAMILY: HOG000160912 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000059743;ENSMUST00000081848;ENSMUSP00000080531.
DR   EMBL; AF309508; - ;
DR   EMBL; AK088601; - ;
DR   EMBL; AK140881; - ;
DR   EMBL; AK166026; - ;
DR   EMBL; AK168008; - ;
DR   EMBL; BC048497; - ;
DR   EMBL; BC087886; - ;
DR   EMBL; CH466547; - ;
DR   EMBL; CT010365; - ;
DR   UniProtKB/Swiss-Prot; Q920E5; -.
DR   EMBL; AF309508; AAL09445.1; -; mRNA.
DR   EMBL; AK088601; BAC40446.1; -; mRNA.
DR   EMBL; BC048497; AAH48497.1; -; mRNA.
DR   IPI; IPI00120457; -.
DR   RefSeq; NP_608219.1; NM_134469.3.
DR   UniGene; Mm.39472; -.
DR   ProteinModelPortal; Q920E5; -.
DR   SMR; Q920E5; 10-350.
DR   STRING; Q920E5; -.
DR   PhosphoSite; Q920E5; -.
DR   PRIDE; Q920E5; -.
DR   Ensembl; ENSMUST00000081848; ENSMUSP00000080531; ENSMUSG00000059743.
DR   GeneID; 110196; -.
DR   KEGG; mmu:110196; -.
DR   NMPDR; fig|10090.3.peg.26163; -.
DR   CTD; 2224; -.
DR   MGI; MGI:104888; Fdps.
DR   GeneTree; ENSGT00530000064127; -.
DR   InParanoid; Q920E5; -.
DR   OMA; RDFMAVF; -.
DR   OrthoDB; EOG4ZGPCS; -.
DR   PhylomeDB; Q920E5; -.
DR   NextBio; 363511; -.
DR   ArrayExpress; Q920E5; -.
DR   Bgee; Q920E5; -.
DR   CleanEx; MM_FDPS; -.
DR   Genevestigator; Q920E5; -.
DR   GermOnline; ENSMUSG00000059743; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:EC.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid 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   SUPFAM; SSF48576; Terpenoid_synth; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
DR   HOGENOMDNA; MOUSE3.PE908; -.
KW   ENSMUSG000000597435old_1320000031; ENSMUSP000000805311old_1320000031;
KW   Q3TMB3_MOUSE; Q3US29_MOUSE; Q4FJN9_MOUSE; Q5M8R9_MOUSE; AF309508;
KW   AK140881; AK166026; AK168008; BC048497; BC087886; CH466547; CT010365;
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   353 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNGNQKLDAY NQEKQNFIQH FSQIVKVLTE KELGHPEIGD AIARLKEVLE YNALGGKYNR
     GLTVVQAFQE LVEPKKQDAE SLQRALTVGW CVELLQAFFL VSDDIMDSSL TRRGQICWYQ
     KPGIGLDAIN DALLLEASIY RLLKFYCREQ PYYLNLLELF LQSSYQTEIG QTLDLMTAPQ
     GHVDLGRYTE KRYKSIVKYK TAFYSFYLPI AAAMYMAGID GEKEHANALK ILMEMGEFFQ
     VQDDYLDLFG DPSVTGKVGT DIQDNKCSWL VVQCLLRASP QQRQILEENY GQKDPEKVAR
     VKALYEALDL QSAFFKYEED SYNRLKSLIE QCSAPLPPSI FMELANKIYK RRK
//

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