Reviewed, UniProtKB/Swiss-Prot Q8WMY2 (FPPS_BOVIN)

Names and origin

Protein names

Recommended name:
    Farnesyl pyrophosphate synthetase
      Short name=FPP synthetase
      Short name=FPS
Alternative name(s):
    Farnesyl diphosphate synthetase
Including the following 2 domains:
    1- Recommended name:
            Dimethylallyltranstransferase
              EC=2.5.1.1
    2- Recommended name:
            Geranyltranstransferase
              EC=2.5.1.10

Gene names

Name:

FDPS

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. 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. Isoprenoid biosynthesis; geranyl-PP biosynthesis; geranyl-PP from dimethylallyl-PP and isopentenyl-PP: step 1/1.
Subunit structure	Homodimer. Interacts with RSAD2 By similarity. Interacts with bovine leukemia virus (BLV) protein G4.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the FPP/GGPP synthetase family.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Host-virus interaction Isoprene biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Cytoplasm
Molecular function	Transferase
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dimethylallyltranstransferase activity Inferred from electronic annotation. Source: EC geranyltranstransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 353	353	Farnesyl pyrophosphate synthetase		PRO_0000237610
Sites
	Active site	192	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8WMY2-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 6FCAA8526E0826BE	FASTA	353	40,510
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Oncoviral bovine leukemia virus G4 and human T-cell leukemia virus type 1 p13(II) accessory proteins interact with farnesyl pyrophosphate synthetase." Lefebvre L., Vanderplasschen A., Ciminale V., Heremans H., Dangoisse O., Jauniaux J.-C., Toussaint J.-F., Zelnik V., Burny A., Kettmann R., Willems L. J. Virol. 76:1400-1414(2002) [PubMed: 11773414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH BLV G4.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF461050 mRNA. Translation: AAL58886.1. BC149572 mRNA. Translation: AAI49573.1.
IPI	IPI00839514.
RefSeq	NP_803463.1.
UniGene	Bt.23182
3D structure databases
HSSP	HSSP built from PDB template 1UBX based on UniProtKB P08836.
SMR	Q8WMY2. Positions 8-353.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000003948. Bos taurus. [Contig view]
GeneID	281156.
KEGG	bta:281156.
Phylogenomic databases
HOVERGEN	Q8WMY2.
Enzyme and pathway databases
BRENDA	2.5.1.1. 251. 2.5.1.10. 251.
Family and domain databases
InterPro	IPR000092. Polyprenyl_synt. IPR008949. Terpenoid_synth. [Graphical view]
Gene3D	G3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
Pfam	PF00348. polyprenyl_synt. 1 hit. [Graphical view]
PROSITE	PS00723. POLYPRENYL_SYNTHET_1. 1 hit. PS00444. POLYPRENYL_SYNTHET_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FPPS_BOVIN

Accession

Primary (citable) accession number: Q8WMY2
Secondary accession number(s): A6QPZ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	March 1, 2002
Last modified:	June 16, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)