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Protein

Probable squalene monooxygenase

Gene

erg1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway.By similarity

Catalytic activityi

Squalene + [reduced NADPH--hemoprotein reductase] + O2 = (3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH--hemoprotein reductase] + H2O.By similarity

Cofactori

FADBy similarity

Pathwayi: lanosterol biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes lanosterol from farnesyl diphosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Squalene synthase (erg9)
  2. Probable squalene monooxygenase (erg1)
  3. Lanosterol synthase (erg7)
This subpathway is part of the pathway lanosterol biosynthesis, which is itself part of Terpene metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes lanosterol from farnesyl diphosphate, the pathway lanosterol biosynthesis and in Terpene metabolism.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 3528FADSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

ReactomeiR-SPO-191273. Cholesterol biosynthesis.
R-SPO-2426168. Activation of gene expression by SREBF (SREBP).
UniPathwayiUPA00767; UER00752.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable squalene monooxygenase (EC:1.14.14.17By similarity)
Alternative name(s):
Squalene epoxidase
Short name:
SE
Gene namesi
Name:erg1
ORF Names:SPBC713.12
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC713.12.
PomBaseiSPBC713.12. erg1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei347 – 36418HelicalSequence analysisAdd
BLAST
Transmembranei409 – 42921HelicalSequence analysisAdd
BLAST
Transmembranei433 – 45321HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • endoplasmic reticulum Source: PomBase
  • endoplasmic reticulum membrane Source: PomBase
  • fungal-type vacuole membrane Source: PomBase
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457Probable squalene monooxygenasePRO_0000209850Add
BLAST

Proteomic databases

MaxQBiQ9C1W3.

Interactioni

Protein-protein interaction databases

MINTiMINT-4702304.

Structurei

3D structure databases

ProteinModelPortaliQ9C1W3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the squalene monooxygenase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000174713.
InParanoidiQ9C1W3.
KOiK00511.
OMAiQFIMGLR.
OrthoDBiEOG7KM62S.
PhylomeDBiQ9C1W3.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR013698. Squalene_epoxidase.
[Graphical view]
PfamiPF08491. SE. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9C1W3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATQDADIII IGAGITGCAL GAALGRQGRK VLVLERDMSE PDRIVGELLQ
60 70 80 90 100
PGGIEALEKI GIADAVEGID GQWTSGYQIF YGDSNVSVPY PSKPNGGAYQ
110 120 130 140 150
GIGFHYGRFV MNLRKALTST PNVTVTEATV NELLRDETGE VITGVVTSSK
160 170 180 190 200
KSESPVEYKA PLTIVCDGCF SKFRKAFIDH PIQVTDHFLG LILTNPDYIA
210 220 230 240 250
PGRGHVILSK VAPMVLYPIS STEARILINY PGKNLPPMET LKKYVLESCV
260 270 280 290 300
PNMPEKLRPS LKAAVYNDRL RSMPNQFLPP TVNRTKGMIL VGDSNNMRHP
310 320 330 340 350
LTGGGMTVCF HDAYLLSRFI SPSAVPDLLD YERILNQMNK FHWKRKGYSF
360 370 380 390 400
VINVLSIALY KLFTPKNRYM KALESGCIDY FKRGGNCVEG PIRLLGGLDH
410 420 430 440 450
SPSHLIGHFY AVCLYGIYQY VLSGPALLMP VRIIESLLIF LQASLVIIPY

ILSEMSS
Length:457
Mass (Da):50,339
Last modified:June 1, 2001 - v1
Checksum:i67D1B26BBD8CA527
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAC22613.1.
RefSeqiNP_595351.1. NM_001021259.2.

Genome annotation databases

EnsemblFungiiSPBC713.12.1; SPBC713.12.1:pep; SPBC713.12.
GeneIDi2541106.
KEGGispo:SPBC713.12.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAC22613.1.
RefSeqiNP_595351.1. NM_001021259.2.

3D structure databases

ProteinModelPortaliQ9C1W3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4702304.

Proteomic databases

MaxQBiQ9C1W3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC713.12.1; SPBC713.12.1:pep; SPBC713.12.
GeneIDi2541106.
KEGGispo:SPBC713.12.

Organism-specific databases

EuPathDBiFungiDB:SPBC713.12.
PomBaseiSPBC713.12. erg1.

Phylogenomic databases

HOGENOMiHOG000174713.
InParanoidiQ9C1W3.
KOiK00511.
OMAiQFIMGLR.
OrthoDBiEOG7KM62S.
PhylomeDBiQ9C1W3.

Enzyme and pathway databases

UniPathwayiUPA00767; UER00752.
ReactomeiR-SPO-191273. Cholesterol biosynthesis.
R-SPO-2426168. Activation of gene expression by SREBF (SREBP).

Miscellaneous databases

NextBioi20802219.
PROiQ9C1W3.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR013698. Squalene_epoxidase.
[Graphical view]
PfamiPF08491. SE. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "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.
  2. "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 nameiERG1_SCHPO
AccessioniPrimary (citable) accession number: Q9C1W3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 1, 2001
Last modified: January 20, 2016
This is version 96 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, 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

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 one 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.