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Protein

Squalene synthase

Gene

erg9

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Mg2+By similarity

Pathwayi

GO - Molecular functioni

  1. farnesyl-diphosphate farnesyltransferase activity Source: PomBase
  2. oxidoreductase activity Source: UniProtKB-KW
  3. squalene synthase activity Source: PomBase

GO - Biological processi

  1. ergosterol biosynthetic process Source: PomBase
  2. isoprenoid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Isoprene biosynthesis, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

Magnesium, NADP

Enzyme and pathway databases

ReactomeiREACT_272874. Cholesterol biosynthesis.
UniPathwayiUPA00767; UER00751.

Names & Taxonomyi

Protein namesi
Recommended name:
Squalene synthase (EC:2.5.1.21)
Short name:
SQS
Short name:
SS
Alternative name(s):
FPP:FPP farnesyltransferase
Farnesyl-diphosphate farnesyltransferase
Gene namesi
Name:erg9
ORF Names:SPBC646.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC646.05c.
PomBaseiSPBC646.05c.

Subcellular locationi

  1. Endoplasmic reticulum membrane 2 Publications; Multi-pass membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei288 – 30821HelicalSequence AnalysisAdd
BLAST
Transmembranei425 – 44521HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: PomBase
  2. endoplasmic reticulum membrane Source: PomBase
  3. integral component of membrane Source: UniProtKB-KW
  4. nuclear outer membrane-endoplasmic reticulum membrane network Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 460460Squalene synthasePRO_0000067451Add
BLAST

Proteomic databases

MaxQBiP36596.

Interactioni

Subunit structurei

Monomer (By similarity). Interacts with pof14.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
pof14Q102235EBI-1794119,EBI-1793014

Protein-protein interaction databases

BioGridi277625. 4 interactions.
IntActiP36596. 2 interactions.
MINTiMINT-3377067.
STRINGi4896.SPBC646.05c-1.

Structurei

3D structure databases

ProteinModelPortaliP36596.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phytoene/squalene synthase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1562.
HOGENOMiHOG000186940.
InParanoidiP36596.
KOiK00801.
OMAiFHTYLYQ.
OrthoDBiEOG7GJ6P5.
PhylomeDBiP36596.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR002060. Squ/phyt_synthse.
IPR006449. Squal_synth.
IPR019845. Squalene/phytoene_synthase_CS.
[Graphical view]
PfamiPF00494. SQS_PSY. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
TIGRFAMsiTIGR01559. squal_synth. 1 hit.
PROSITEiPS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36596-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLANRIEEI RCLCQYKLWN DLPSYGEDEN VPQNIRRCYQ LLDMTSRSFA
60 70 80 90 100
VVIKELPNGI REAVMIFYLV LRGLDTVEDD MTLPLDKKLP ILRDFYKTIE
110 120 130 140 150
VEGWTFNESG PNEKDRQLLV EFDVVIKEYL NLSEGYRNVI SNITKEMGDG
160 170 180 190 200
MAYYASLAEK NDGFSVETIE DFNKYCHYVA GLVGIGLSRL FAQSKLEDPD
210 220 230 240 250
LAHSQAISNS LGLFLQKVNI IRDYREDFDD NRHFWPREIW SKYTSSFGDL
260 270 280 290 300
CLPDNSEKAL ECLSDMTANA LTHATDALVY LSQLKTQEIF NFCAIPQVMA
310 320 330 340 350
IATLAAVFRN PDVFQTNVKI RKGQAVQIIL HSVNLKNVCD LFLRYTRDIH
360 370 380 390 400
YKNTPKDPNF LKISIECGKI EQVSESLFPR RFREMYEKAY VSKLSEQKKG
410 420 430 440 450
NGTQKAILND EQKELYRKDL QKLGISILFV FFIILVCLAV IFYVFNIRIH
460
WSDFKELNLF
Length:460
Mass (Da):53,321
Last modified:June 1, 1994 - v1
Checksum:iBAEE7F24B6CE5D25
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06071 mRNA. Translation: AAA35343.1.
CU329671 Genomic DNA. Translation: CAA22809.1.
PIRiB48057.
T40581.
RefSeqiNP_595363.1. NM_001021271.2.

Genome annotation databases

EnsemblFungiiSPBC646.05c.1; SPBC646.05c.1:pep; SPBC646.05c.
GeneIDi2541110.
KEGGispo:SPBC646.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06071 mRNA. Translation: AAA35343.1.
CU329671 Genomic DNA. Translation: CAA22809.1.
PIRiB48057.
T40581.
RefSeqiNP_595363.1. NM_001021271.2.

3D structure databases

ProteinModelPortaliP36596.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277625. 4 interactions.
IntActiP36596. 2 interactions.
MINTiMINT-3377067.
STRINGi4896.SPBC646.05c-1.

Proteomic databases

MaxQBiP36596.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC646.05c.1; SPBC646.05c.1:pep; SPBC646.05c.
GeneIDi2541110.
KEGGispo:SPBC646.05c.

Organism-specific databases

EuPathDBiFungiDB:SPBC646.05c.
PomBaseiSPBC646.05c.

Phylogenomic databases

eggNOGiCOG1562.
HOGENOMiHOG000186940.
InParanoidiP36596.
KOiK00801.
OMAiFHTYLYQ.
OrthoDBiEOG7GJ6P5.
PhylomeDBiP36596.

Enzyme and pathway databases

UniPathwayiUPA00767; UER00751.
ReactomeiREACT_272874. Cholesterol biosynthesis.

Miscellaneous databases

NextBioi20802223.
PROiP36596.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR002060. Squ/phyt_synthse.
IPR006449. Squal_synth.
IPR019845. Squalene/phytoene_synthase_CS.
[Graphical view]
PfamiPF00494. SQS_PSY. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
TIGRFAMsiTIGR01559. squal_synth. 1 hit.
PROSITEiPS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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].

Entry informationi

Entry nameiFDFT_SCHPO
AccessioniPrimary (citable) accession number: P36596
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 29, 2015
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.