Reviewed, UniProtKB/Swiss-Prot P36596 (FDFT_SCHPO)

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
ORF Names:	SPBC646.05c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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.
Subunit structure	Monomer By similarity. Interacts with pof14.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Ref.3 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 ergosterol biosynthetic process Ref.1 Inferred from genetic interaction. Source: GeneDB_SPombe isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Ref.3 Inferred from direct assay. Source: GeneDB_SPombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	farnesyl-diphosphate farnesyltransferase activity Ref.1 Inferred from genetic interaction. Source: GeneDB_SPombe magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.3 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
pof14	Q10223	3	EBI-1794119,EBI-1793014
skp1	Q9Y709	1	EBI-1794119,EBI-1172248

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 460	460	Squalene synthetase		PRO_0000067451
Regions
	Transmembrane	288 – 308	21	Potential
	Transmembrane	425 – 445	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	P36596-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: BAEE7F24B6CE5D25	FASTA	460	53,321
	10 20 30 40 50 60 MSLANRIEEI RCLCQYKLWN DLPSYGEDEN VPQNIRRCYQ LLDMTSRSFA VVIKELPNGI 70 80 90 100 110 120 REAVMIFYLV LRGLDTVEDD MTLPLDKKLP ILRDFYKTIE VEGWTFNESG PNEKDRQLLV 130 140 150 160 170 180 EFDVVIKEYL NLSEGYRNVI SNITKEMGDG MAYYASLAEK NDGFSVETIE DFNKYCHYVA 190 200 210 220 230 240 GLVGIGLSRL FAQSKLEDPD LAHSQAISNS LGLFLQKVNI IRDYREDFDD NRHFWPREIW 250 260 270 280 290 300 SKYTSSFGDL CLPDNSEKAL ECLSDMTANA LTHATDALVY LSQLKTQEIF NFCAIPQVMA 310 320 330 340 350 360 IATLAAVFRN PDVFQTNVKI RKGQAVQIIL HSVNLKNVCD LFLRYTRDIH YKNTPKDPNF 370 380 390 400 410 420 LKISIECGKI EQVSESLFPR RFREMYEKAY VSKLSEQKKG NGTQKAILND EQKELYRKDL 430 440 450 460 QKLGISILFV FFIILVCLAV IFYVFNIRIH WSDFKELNLF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Conservation between human and fungal squalene synthetases: similarities in structure, function, and regulation." Robinson G.W., Tsay Y.H., Kienzle B.K., Smith-Monroy C.A., Bishop R.W. Mol. Cell. Biol. 13:2706-2717(1993) [PubMed: 8474436] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ATCC 38366 / 972.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"Repression of ergosterol level during oxidative stress by fission yeast F-box protein Pof14 independently of SCF." Tafforeau L., Le Blastier S., Bamps S., Dewez M., Vandenhaute J., Hermand D. EMBO J. 25:4547-4556(2006) [PubMed: 17016471] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH POF14.
[4]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	L06071 mRNA. Translation: AAA35343.1. CU329671 Genomic DNA. Translation: CAA22809.1.
PIR	B48057. T40581.
RefSeq	NP_595363.1.
3D structure databases
HSSP	HSSP built from PDB template 1EZF based on UniProtKB P37268.
ModBase	Search...
Protein-protein interaction databases
IntAct	P36596. 2 interactions.
STRING	P36596.
Genome annotation databases
GeneID	2541110.
GenomeReviews	Gene locus erg9 in contig CU329671_GR.
KEGG	spo:SPBC646.05c.
NMPDR	fig|4896.1.peg.1229.
Organism-specific databases
GeneDB_Spombe	SPBC646.05c.
Phylogenomic databases
OMA	GMAEFLE.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003439-MON.
BRENDA	2.5.1.21. 653.
Gene expression databases
ArrayExpress	P36596.
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...

Entry information

Entry name

FDFT_SCHPO

Accession

Primary (citable) accession number: P36596

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	November 3, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)