Reviewed, UniProtKB/Swiss-Prot P05369 (FPPS_RAT)

Names and origin

Protein names

Recommended name:
    Farnesyl pyrophosphate synthetase
      Short name=FPP synthetase
      Short name=FPS
Alternative name(s):
    Farnesyl diphosphate synthetase
    Cholesterol-regulated 39 kDa protein
      Short name=CR 39
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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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.
Subcellular location	Cytoplasm.
Tissue specificity	Testis, liver, kidney, brain and adrenal gland.
Sequence similarities	Belongs to the FPP/GGPP synthetase family.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Isoprene biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Cytoplasm
Molecular function	Transferase
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Traceable author statement. Source: RGD 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 farnesyltranstransferase activity Inferred from genetic interaction. Source: RGD geranyltranstransferase activity Traceable author statement. Source: RGD
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_0000123946
Sites
	Active site	192	1	By similarity
Natural variations
	Natural variant	110	1	Y → H Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P05369-1 [UniParc]. Last modified February 1, 1991. Version 2. Checksum: 27FD7E0DD6FEA001	FASTA	353	40,830
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequence of a cholesterol-repressible enzyme related to prenyltransferase in the isoprene biosynthetic pathway." Clarke C.F., Tanaka R.D., Svenson K., Wamsley M., Fogelman A.M., Edwards P.A. Mol. Cell. Biol. 7:3138-3146(1987) [PubMed: 3670308] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Testis-specific transcription initiation sites of rat farnesyl pyrophosphate synthetase mRNA." Teruya J.H., Kutsunai S.Y., Spear D.H., Edwards P.A., Clarke C.F. Mol. Cell. Biol. 10:2315-2326(1990) [PubMed: 2325654] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION. Strain: Sprague-Dawley. Tissue: Testis.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-110. Tissue: Pituitary.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M34477 mRNA. Translation: AAA41143.1. M17300 mRNA. Translation: AAA40960.1. Sequence problems. BC059125 mRNA. Translation: AAH59125.1.
IPI	IPI00325147.
PIR	A34713. B34713.
RefSeq	NP_114028.1.
UniGene	Rn.2848
3D structure databases
HSSP	HSSP built from PDB template 1UBY based on UniProtKB P08836.
SMR	P05369. Positions 8-353.
ModBase	Search...
Proteomic databases
PRIDE	P05369.
Genome annotation databases
GeneID	83791.
KEGG	rno:83791.
Organism-specific databases
RGD	68953. Fdps.
Phylogenomic databases
HOVERGEN	P05369.
Enzyme and pathway databases
BRENDA	2.5.1.1. 248. 2.5.1.10. 248.
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...
Other Resources
NextBio	616373.

Entry information

Entry name

FPPS_RAT

Accession

Primary (citable) accession number: P05369
Secondary accession number(s): Q6GT82

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)