NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH BLV G4.
PubMed=11773414 [NCBI, ExPASy, EBI, Israel, Japan]
Lefebvre L., Vanderplasschen A., Ciminale V., Heremans H., Dangoisse O., Jauniaux J.-C., Toussaint J.-F., Zelnik V., Burny A., Kettmann R., Willems L.;
"Oncoviral bovine leukemia virus G4 and human T-cell leukemia virus type 1 p13(II) accessory proteins interact with farnesyl pyrophosphate synthetase.";
J. Virol. 76:1400-1414(2002).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford;
TISSUE=Fetal liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (By similarity).
CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate.
CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate.
ENZYME REGULATION: Inactivated by interferon-induced RSAD2. This inactivation may result of disruption of lipid rafts at the plasma membrane, and thus have an antiviral effect since many envelopped viruses need lipid rafts to bud efficiently out of the cell (By similarity).
PATHWAY: Isoprenoid biosynthesis; farnesyl-PP biosynthesis; farnesyl-PP from geranyl-PP and isopentenyl-PP: step 1/1 .
PATHWAY: Isoprenoid biosynthesis; geranyl-PP biosynthesis; geranyl-PP from dimethylallyl-PP and isopentenyl-PP: step 1/1 .
SUBUNIT: Homodimer. Interacts with RSAD2 (By similarity). Interacts with bovine leukemia virus (BLV) protein G4.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the FPP/GGPP synthetase family.

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

AF461050; AAL58886.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC149572; AAI49573.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_803463.1; -.

UniGene

Bt.23182

3D structure databases

HSSP

P08836; 1UBX. [HSSP ENTRY / PDB]

SMR

Q8WMY2; 8-353.

ModBase

Q8WMY2.

Ontologies

GO:0004161;	Molecular function: dimethylallyltranstransferase activity (inferred from electronic annotation from EC).
GO:0004337;	Molecular function: geranyltranstransferase activity (inferred from electronic annotation from EC).
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.

BLOCKS

Q8WMY2.

Genome annotation databases

Ensembl

ENSBTAG00000007050; Bos taurus. [Contig view]

GeneID

281156; -.

KEGG

bta:281156; -.

Phylogenomic databases

HOVERGEN

Q8WMY2; -.

Other

ProtoNet

Q8WMY2.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cholesterol biosynthesis; Cytoplasm; Host-virus interaction; Isoprene biosynthesis; Lipid synthesis; Steroid biosynthesis; Sterol biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 353`	`353`	`Farnesyl pyrophosphate synthetase.`	`PRO_0000237610`
`ACT_SITE`	`192 192`		`By similarity.`

Sequence information

Length: 353 AA [This is the length of the unprocessed precursor]

Molecular weight: 40510 Da [This is the MW of the unprocessed precursor]

CRC64: 6FCAA8526E0826BE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNGDQKLDAY AQERQDFIQH FSQIVKVLTE EDIGHPEIGD AITRLKEVLE YNAIGGKYNR 

        70         80         90        100        110        120 
GLTVVITFRE LVEPGKQDPD SLQRALTVGW CVELLQAFFL VSDDIMDSSL TRRGQTCWYQ 

       130        140        150        160        170        180 
KPGIGLDAIN DAFLLESSIY RLLKLYCREQ PYYLDLIELF LQSSYQTEIG QTLDLITAPQ 

       190        200        210        220        230        240 
GNVDLGRFTE KRYKSIVKYK TAFYSFYLPV AAAMYMAGID GEKEHAHAKK ILLEMGEFFQ 

       250        260        270        280        290        300 
IQDDYLDLFG DPSMTGKIGT DIQDNKCSWL VVQCLQRASP EQRQILQENY GQKEAEKVAR 

       310        320        330        340        350 
VKALYEEMNL SAVYMQYEED SYNHIMGLIE QYAAPLPPAI FLGLAQKIYK RKK

Q8WMY2 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools