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P36596

- FDFT_SCHPO

UniProt

P36596 - FDFT_SCHPO

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Protein
Squalene synthase
Gene
erg9, SPBC646.05c
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - 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

Magnesium By similarity.

Pathwayi

GO - Molecular functioni

  1. farnesyl-diphosphate farnesyltransferase activity Source: PomBase
  2. oxidoreductase activity Source: UniProtKB-KW
  3. protein binding Source: UniProtKB
  4. squalene synthase activity Source: UniProtKB-EC
Complete GO annotation...

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

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: Chromosome II

Organism-specific databases

PomBaseiSPBC646.05c.

Subcellular locationi

Endoplasmic reticulum membrane; Multi-pass membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei288 – 30821Helical; Reviewed prediction
Add
BLAST
Transmembranei425 – 44521Helical; Reviewed prediction
Add
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 synthase
PRO_0000067451Add
BLAST

Proteomic databases

MaxQBiP36596.

Interactioni

Subunit structurei

Monomer By similarity. Interacts with pof14.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi277625. 5 interactions.
IntActiP36596. 2 interactions.
MINTiMINT-3377067.
STRINGi4896.SPBC646.05c-1.

Structurei

3D structure databases

ProteinModelPortaliP36596.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1562.
HOGENOMiHOG000186940.
KOiK00801.
OMAiEMRHAVC.
OrthoDBiEOG7GJ6P5.
PhylomeDBiP36596.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR002060. Squ/phyt_synthse.
IPR006449. Squal_synth.
IPR019845. Squalene/phytoene_synthase_CS.
IPR008949. Terpenoid_synth.
[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

MSLANRIEEI RCLCQYKLWN DLPSYGEDEN VPQNIRRCYQ LLDMTSRSFA    50
VVIKELPNGI REAVMIFYLV LRGLDTVEDD MTLPLDKKLP ILRDFYKTIE 100
VEGWTFNESG PNEKDRQLLV EFDVVIKEYL NLSEGYRNVI SNITKEMGDG 150
MAYYASLAEK NDGFSVETIE DFNKYCHYVA GLVGIGLSRL FAQSKLEDPD 200
LAHSQAISNS LGLFLQKVNI IRDYREDFDD NRHFWPREIW SKYTSSFGDL 250
CLPDNSEKAL ECLSDMTANA LTHATDALVY LSQLKTQEIF NFCAIPQVMA 300
IATLAAVFRN PDVFQTNVKI RKGQAVQIIL HSVNLKNVCD LFLRYTRDIH 350
YKNTPKDPNF LKISIECGKI EQVSESLFPR RFREMYEKAY VSKLSEQKKG 400
NGTQKAILND EQKELYRKDL QKLGISILFV FFIILVCLAV IFYVFNIRIH 450
WSDFKELNLF 460
Length:460
Mass (Da):53,321
Last modified:June 1, 1994 - v1
Checksum:iBAEE7F24B6CE5D25
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
L06071 mRNA. Translation: AAA35343.1 .
CU329671 Genomic DNA. Translation: CAA22809.1 .
PIRi B48057.
T40581.
RefSeqi NP_595363.1. NM_001021271.2.

3D structure databases

ProteinModelPortali P36596.
ModBasei Search...

Protein-protein interaction databases

BioGridi 277625. 5 interactions.
IntActi P36596. 2 interactions.
MINTi MINT-3377067.
STRINGi 4896.SPBC646.05c-1.

Proteomic databases

MaxQBi P36596.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBC646.05c.1 ; SPBC646.05c.1:pep ; SPBC646.05c .
GeneIDi 2541110.
KEGGi spo:SPBC646.05c.

Organism-specific databases

PomBasei SPBC646.05c.

Phylogenomic databases

eggNOGi COG1562.
HOGENOMi HOG000186940.
KOi K00801.
OMAi EMRHAVC.
OrthoDBi EOG7GJ6P5.
PhylomeDBi P36596.

Enzyme and pathway databases

UniPathwayi UPA00767 ; UER00751 .

Miscellaneous databases

NextBioi 20802223.
PROi P36596.

Family and domain databases

Gene3Di 1.10.600.10. 1 hit.
InterProi IPR002060. Squ/phyt_synthse.
IPR006449. Squal_synth.
IPR019845. Squalene/phytoene_synthase_CS.
IPR008949. Terpenoid_synth.
[Graphical view ]
Pfami PF00494. SQS_PSY. 1 hit.
[Graphical view ]
SUPFAMi SSF48576. SSF48576. 1 hit.
TIGRFAMsi TIGR01559. squal_synth. 1 hit.
PROSITEi PS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 118 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

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