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UniProtKB/Swiss-Prot entry Q920E5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FPPS_MOUSE
Primary accession number Q920E5
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 2005
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 54)
Name and origin of the protein
Protein name Farnesyl pyrophosphate synthetase
Synonyms FPP synthetase
FPS
Farnesyl diphosphate synthetase
Cholesterol-regulated 39 kDa protein
CR 39
Includes Dimethylallyltranstransferase
     (EC 2.5.1.1)
Geranyltranstransferase
     (EC 2.5.1.10)
Gene name
Name: Fdps
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1042/BJ20020560; PubMed=12020352 [NCBI, ExPASy, EBI, Israel, Japan]
Reilly J.F., Martinez S.D., Mickey G., Maher P.A.;
"A novel role for farnesyl pyrophosphate synthase in fibroblast growth factor-mediated signal transduction.";
Biochem. J. 366:501-510(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD;
TISSUE=Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF309508; AAL09445.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK088601; BAC40446.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC048497; AAH48497.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_608219.1; -.
UniGene Mm.39472
3D structure databases
HSSP P08836; 1FPS. [HSSP ENTRY / PDB]
SMR Q920E5; 8-353.
ModBase Q920E5.
PTM databases
PhosphoSite Q920E5; -.
Organism-specific databases
MGI MGI:104888; Fdps.
Gene expression databases
ArrayExpress Q920E5; -.
CleanEx MM_FDPS; -.
GermOnline ENSMUSG00000059743; Mus musculus.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004161; Molecular function: dimethylallyltranstransferase activity (inferred from electronic annotation from EC).
GO:0004337; Molecular function: geranyltranstransferase activity (inferred from electronic annotation from EC).
GO:0006695; Biological process: cholesterol biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0008299; Biological process: isoprenoid biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000092; Polyprenyl_synt.
IPR008949; Terpenoid_synth.
Graphical view of domain structure.
Gene3D G3DSA:1.10.600.10; Terpenoid_synth; 1.
Pfam PF00348; polyprenyl_synt; 1.
Pfam graphical view of domain structure.
PROSITE PS00723; POLYPRENYL_SYNTHET_1; 1.
PS00444; POLYPRENYL_SYNTHET_2; 1.
ProtoNet Q920E5.
Genome annotation databases
Ensembl ENSMUSG00000059743; Mus musculus. [Contig view]
GeneID 110196; -.
KEGG mmu:110196; -.
NMPDR fig|10090.3.peg.26163; -.
Phylogenomic databases
HOGENOM Q920E5; -.
HOVERGEN Q920E5; -.
Other
NextBio 363511; -.
SOURCE Fdps; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cholesterol biosynthesis; Cytoplasm; Isoprene biosynthesis; Lipid synthesis; Steroid biosynthesis; Sterol biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   353  353     Farnesyl pyrophosphate synthetase. PRO_0000123945
ACT_SITE   192   192        By similarity. 
Sequence information
Length: 353 AA [This is the length of the unprocessed precursor] Molecular weight: 40582 Da [This is the MW of the unprocessed precursor] CRC64: 9A3D7034ACAB576A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNGNQKLDAY NQEKQNFIQH FSQIVKVLTE KELGHPEIGD AIARLKEVLE YNALGGKYNR 

        70         80         90        100        110        120 
GLTVVQAFQE LVEPKKQDAE SLQRALTVGW CVELLQAFFL VSDDIMDSSL TRRGQICWYQ 

       130        140        150        160        170        180 
KPGIGLDAIN DALLLEASIY RLLKFYCREQ PYYLNLLELF LQSSYQTEIG QTLDLMTAPQ 

       190        200        210        220        230        240 
GHVDLGRYTE KRYKSIVKYK TAFYSFYLPI AAAMYMAGID GEKEHANALK ILMEMGEFFQ 

       250        260        270        280        290        300 
VQDDYLDLFG DPSVTGKVGT DIQDNKCSWL VVQCLLRASP QQRQILEENY GQKDPEKVAR 

       310        320        330        340        350 
VKALYEALDL QSAFFKYEED SYNRLKSLIE QCSAPLPPSI FMELANKIYK RRK 

Q920E5 in FASTA format

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View entry in raw text format (no links)
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