ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P05369


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name FPPS_RAT
Primary accession number P05369
Secondary accession number Q6GT82
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on February 1, 1991 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 74)
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
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=3670308 [NCBI, ExPASy, EBI, Israel, Japan]
Clarke C.F., Tanaka R.D., Svenson K., Wamsley M., Fogelman A.M., Edwards P.A.;
"Molecular cloning and sequence of a cholesterol-repressible enzyme related to prenyltransferase in the isoprene biosynthetic pathway.";
Mol. Cell. Biol. 7:3138-3146(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION.
STRAIN=Sprague-Dawley;
TISSUE=Testis;
PubMed=2325654 [NCBI, ExPASy, EBI, Israel, Japan]
Teruya J.H., Kutsunai S.Y., Spear D.H., Edwards P.A., Clarke C.F.;
"Testis-specific transcription initiation sites of rat farnesyl pyrophosphate synthetase mRNA.";
Mol. Cell. Biol. 10:2315-2326(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-110.
TISSUE=Pituitary;
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
M34477; AAA41143.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17300; AAA40960.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC059125; AAH59125.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A34713; A34713.
B34713; B34713.
RefSeq NP_114028.1; -.
UniGene Rn.2848
3D structure databases
HSSP P08836; 1UBY. [HSSP ENTRY / PDB]
SMR P05369; 8-353.
ModBase P05369.
Organism-specific databases
RGD 68953; Fdps.
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.
BLOCKS P05369.
Genome annotation databases
GeneID 83791; -.
KEGG rno:83791; -.
Phylogenomic databases
HOVERGEN P05369; -.
Other
LinkHub P05369; -.
ProtoNet P05369.
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_0000123946
ACT_SITE   192   192        By similarity. 
VARIANT   110   110  1     Y -> H. 
Sequence information
Length: 353 AA [This is the length of the unprocessed precursor] Molecular weight: 40830 Da [This is the MW of the unprocessed precursor] CRC64: 27FD7E0DD6FEA001 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNGDQKLDVH NQEKQNFIQH FSQIVKVLTE DELGHPEKGD AITRIKEVLE YNTVGGKYNR 

        70         80         90        100        110        120 
GLTVVQTFQE LVEPRKQDAE SLQRALTVGW CVELLQAFFL VLDDIMDSSY TRRGQICWYQ 

       130        140        150        160        170        180 
KPGIGLDAIN DALLLEAAIY RLLKFYCREQ PYYLNLLELF LQSSYQTEIG QTLDLITAPQ 

       190        200        210        220        230        240 
GQVDLGRYTE KRYKSIVKYK TAFYSFYLPI AAAMYMAGID GEKEHANALK ILLEMGEFFQ 

       250        260        270        280        290        300 
IQDDYLDLFG DPSVTGKVGT DIQDNKCSWL VVQCLLRATP QQRQILEENY GQKDPEKVAR 

       310        320        330        340        350 
VKALYEELDL RSVFFKYEED SYNRLKSLIE QCSAPLPPSI FLELANKIYK RRK 

P05369 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!