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P36596 (FDFT_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Squalene synthase

Short name=SQS
Short name=SS
EC=2.5.1.21
Alternative name(s):
FPP:FPP farnesyltransferase
Farnesyl-diphosphate farnesyltransferase
Gene names
Name:erg9
ORF Names:SPBC646.05c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the condensation of 2 two farnesyl pyrophosphate moieties to form squalene. It is the first committed enzyme of the sterol biosynthesis pathway. Required for the biosynthesis of ergosterol. Ref.1

Catalytic activity

2 farnesyl diphosphate + NAD(P)H = squalene + 2 diphosphate + NAD(P)+.

Cofactor

Magnesium By similarity.

Pathway

Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3.

Subunit structure

Monomer By similarity. Interacts with pof14. Ref.3

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.3 Ref.4.

Sequence similarities

Belongs to the phytoene/squalene synthase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

pof14Q102235EBI-1794119,EBI-1793014

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 460460Squalene synthase
PRO_0000067451

Regions

Transmembrane288 – 30821Helical; Potential
Transmembrane425 – 44521Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
P36596 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: BAEE7F24B6CE5D25

FASTA46053,321
        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 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Strain: 972 / ATCC 24843.
[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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06071 mRNA. Translation: AAA35343.1.
CU329671 Genomic DNA. Translation: CAA22809.1.
PIRB48057.
T40581.
RefSeqNP_595363.1. NM_001021271.2.

3D structure databases

ProteinModelPortalP36596.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid277625. 5 interactions.
IntActP36596. 2 interactions.
MINTMINT-3377067.
STRING4896.SPBC646.05c-1.

Proteomic databases

MaxQBP36596.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC646.05c.1; SPBC646.05c.1:pep; SPBC646.05c.
GeneID2541110.
KEGGspo:SPBC646.05c.

Organism-specific databases

PomBaseSPBC646.05c.

Phylogenomic databases

eggNOGCOG1562.
HOGENOMHOG000186940.
KOK00801.
OMAEMRHAVC.
OrthoDBEOG7GJ6P5.
PhylomeDBP36596.

Enzyme and pathway databases

UniPathwayUPA00767; UER00751.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
InterProIPR002060. Squ/phyt_synthse.
IPR006449. Squal_synth.
IPR019845. Squalene/phytoene_synthase_CS.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamPF00494. SQS_PSY. 1 hit.
[Graphical view]
SUPFAMSSF48576. SSF48576. 1 hit.
TIGRFAMsTIGR01559. squal_synth. 1 hit.
PROSITEPS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802223.
PROP36596.

Entry information

Entry nameFDFT_SCHPO
AccessionPrimary (citable) accession number: P36596
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 11, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways