Reviewed, UniProtKB/Swiss-Prot P29704 (FDFT_YEAST)

Names and origin

Protein names

Recommended name:
    Squalene synthetase
      Short name=SQS
      Short name=SS
    EC=2.5.1.21
Alternative name(s):
    Farnesyl-diphosphate farnesyltransferase
    FPP:FPP farnesyltransferase

Gene names

Name:	ERG9
Ordered Locus Names:	YHR190W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May regulate the flux of isoprene intermediates through the sterol pathway. Squalene synthetase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. ERG9 is also essential for cell growth in yeast.
Catalytic activity	2 farnesyl diphosphate = diphosphate + presqualene diphosphate. Presqualene diphosphate + NAD(P)H = squalene + diphosphate + NAD(P)+.
Cofactor	Magnesium.
Pathway	Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Miscellaneous	Present with 10800 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the phytoene/squalene synthetase family.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Isoprene biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	Magnesium NADP
Molecular function	Oxidoreductase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membrane Inferred from direct assay. Source: SGD
Molecular function	farnesyl-diphosphate farnesyltransferase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ECM4	P36156	1	EBI-6865,EBI-2042717
RPB4	P20433	1	EBI-6865,EBI-15777

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 444	444	Squalene synthetase		PRO_0000067454
Regions
	Transmembrane	291 – 311	21	Potential
	Transmembrane	421 – 441	21	Potential
Experimental info
	Sequence conflict	48	1	L → F in CAA42583. Ref.1
	Sequence conflict	286	1	G → S in AAA34597. Ref.2
	Sequence conflict	320	1	N → D in CAA42583. Ref.1
	Sequence conflict	330	1	Y → C in CAA42583. Ref.1
	Sequence conflict	429	1	L → S in CAA42583. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P29704-1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 3DA00295B8DFDB16	FASTA	444	51,720
	10 20 30 40 50 60 MGKLLQLALH PVEMKAALKL KFCRTPLFSI YDQSTSPYLL HCFELLNLTS RSFAAVIREL 70 80 90 100 110 120 HPELRNCVTL FYLILRALDT IEDDMSIEHD LKIDLLRHFH EKLLLTKWSF DGNAPDVKDR 130 140 150 160 170 180 AVLTDFESIL IEFHKLKPEY QEVIKEITEK MGNGMADYIL DENYNLNGLQ TVHDYDVYCH 190 200 210 220 230 240 YVAGLVGDGL TRLIVIAKFA NESLYSNEQL YESMGLFLQK TNIIRDYNED LVDGRSFWPK 250 260 270 280 290 300 EIWSQYAPQL KDFMKPENEQ LGLDCINHLV LNALSHVIDV LTYLAGIHEQ STFQFCAIPQ 310 320 330 340 350 360 VMAIATLALV FNNREVLHGN VKIRKGTTCY LILKSRTLRG CVEIFDYYLR DIKSKLAVQD 370 380 390 400 410 420 PNFLKLNIQI SKIEQFMEEM YQDKLPPNVK PNETPIFLKV KERSRYDDEL VPTQQEEEYK 430 440 FNMVLSIILS VLLGFYYIYT LHRA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and primary structure of the ERG9 gene of Saccharomyces cerevisiae encoding squalene synthetase." Fegueur M., Richard L., Charles A.D., Karst F. Curr. Genet. 20:365-372(1991) [PubMed: 1807826] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Molecular cloning and characterization of the yeast gene for squalene synthetase." Jennings S.M., Tsay Y.H., Fisch T.M., Robinson G.W. Proc. Natl. Acad. Sci. U.S.A. 88:6038-6042(1991) [PubMed: 2068081] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M. Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M63979 Genomic DNA. Translation: AAA34597.1. X59959 Genomic DNA. Translation: CAA42583.1. U00030 Genomic DNA. Translation: AAB68360.1.
PIR	S46682.
RefSeq	NP_012060.1.
3D structure databases
HSSP	HSSP built from PDB template 1EZF based on UniProtKB P37268.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4576N.
IntAct	P29704. 13 interactions.
STRING	P29704.
Proteomic databases
PeptideAtlas	P29704.
Genome annotation databases
Ensembl	YHR190W; YHR190W; YHR190W; Saccharomyces cerevisiae. [Genome view]
GeneID	856597.
GenomeReviews	Gene locus YHR190W in contig U00093_GR.
KEGG	sce:YHR190W.
NMPDR	fig|4932.3.peg.3229.
Organism-specific databases
CYGD	YHR190w.
SGD	S000001233. ERG9.
Phylogenomic databases
HOGENOM	P29704.
OMA	GMAEFLE.
Enzyme and pathway databases
BioCyc	MetaCyc:YHR190W-MON.
BRENDA	2.5.1.21. 250.
Gene expression databases
ArrayExpress	P29704.
Genevestigator	P29704.
GermOnline	YHR190W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002060. Squ/phyt_synthse. IPR006449. Squal_synth. IPR019845. Squalene/phytoene_synthase_CS. IPR008949. Terpenoid_synth. [Graphical view]
Gene3D	G3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
Pfam	PF00494. SQS_PSY. 1 hit. [Graphical view]
TIGRFAMs	TIGR01559. squal_synth. 1 hit.
PROSITE	PS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit. PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	982487.

Entry information

Entry name

FDFT_YEAST

Accession

Primary (citable) accession number: P29704

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	February 1, 1995
Last modified:	November 3, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)