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P32476 (ERG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 monooxygenase

EC=1.14.13.132
Alternative name(s):
Squalene epoxidase
Short name=SE
Gene names
Name:ERG1
Ordered Locus Names:YGR175C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Squalene + NADPH + O2 = (3S)-2,3-epoxy-2,3-dihydrosqualene + NADP+ + H2O.

Cofactor

FAD.

Enzyme regulation

Inhibited by the allylamine antimycotic drugs.

Pathway

Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 2/3.

Subunit structure

Interacts with ERG28. Ref.7

Subcellular location

Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.

Miscellaneous

Present with 65400 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the squalene monooxygenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 496496Squalene monooxygenase
PRO_0000209851

Regions

Topological domain1 – 1616Cytoplasmic Potential
Transmembrane17 – 3721Helical; Potential
Topological domain38 – 474437Lumenal Potential
Transmembrane475 – 49521Helical; Potential
Topological domain4961Cytoplasmic Potential
Nucleotide binding21 – 4828FAD Potential

Amino acid modifications

Cross-link284Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
Cross-link311Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Natural variations

Natural variant2511L → F in strain: A2-M8; confers resistance to the allylamine antifungal terbinafine.

Sequences

Sequence LengthMass (Da)Tools
P32476 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: BBEFD766634855E8

FASTA49655,126
        10         20         30         40         50         60 
MSAVNVAPEL INADNTITYD AIVIGAGVIG PCVATGLARK GKKVLIVERD WAMPDRIVGE 

        70         80         90        100        110        120 
LMQPGGVRAL RSLGMIQSIN NIEAYPVTGY TVFFNGEQVD IPYPYKADIP KVEKLKDLVK 

       130        140        150        160        170        180 
DGNDKVLEDS TIHIKDYEDD ERERGVAFVH GRFLNNLRNI TAQEPNVTRV QGNCIEILKD 

       190        200        210        220        230        240 
EKNEVVGAKV DIDGRGKVEF KAHLTFICDG IFSRFRKELH PDHVPTVGSS FVGMSLFNAK 

       250        260        270        280        290        300 
NPAPMHGHVI LGSDHMPILV YQISPEETRI LCAYNSPKVP ADIKSWMIKD VQPFIPKSLR 

       310        320        330        340        350        360 
PSFDEAVSQG KFRAMPNSYL PARQNDVTGM CVIGDALNMR HPLTGGGMTV GLHDVVLLIK 

       370        380        390        400        410        420 
KIGDLDFSDR EKVLDELLDY HFERKSYDSV INVLSVALYS LFAADSDNLK ALQKGCFKYF 

       430        440        450        460        470        480 
QRGGDCVNKP VEFLSGVLPK PLQLTRVFFA VAFYTIYLNM EERGFLGLPM ALLEGIMILI 

       490 
TAIRVFTPFL FGELIG 

« Hide

References

« Hide 'large scale' references
[1]"The gene encoding squalene epoxidase from Saccharomyces cerevisiae: cloning and characterization."
Jandrositz A., Turnowsky F., Hoegenauer G.
Gene 107:155-160(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A2-M8.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-311.
Strain: SUB592.
[6]"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-284.
[7]"Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex."
Mo C., Bard M.
J. Lipid Res. 46:1991-1998(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERG28.
[8]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[9]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64994 Genomic DNA. Translation: AAA34592.1.
Z72960 Genomic DNA. Translation: CAA97201.1.
BK006941 Genomic DNA. Translation: DAA08271.1.
PIRS64489.
RefSeqNP_011691.1. NM_001181304.1.

3D structure databases

ProteinModelPortalP32476.
SMRP32476. Positions 18-52, 147-214.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33428. 40 interactions.
DIPDIP-6325N.
IntActP32476. 16 interactions.
MINTMINT-1324933.
STRING4932.YGR175C.

Proteomic databases

PaxDbP32476.
PeptideAtlasP32476.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR175C; YGR175C; YGR175C.
GeneID853086.
KEGGsce:YGR175C.

Organism-specific databases

CYGDYGR175c.
SGDS000003407. ERG1.

Phylogenomic databases

eggNOGCOG0654.
GeneTreeENSGT00390000011759.
HOGENOMHOG000174713.
KOK00511.
OMAVMGVQYK.
OrthoDBEOG7KM62S.

Enzyme and pathway databases

BioCycMetaCyc:YGR175C-MONOMER.
YEAST:YGR175C-MONOMER.
UniPathwayUPA00767; UER00752.

Gene expression databases

GenevestigatorP32476.

Family and domain databases

InterProIPR003042. Rng_hydrolase-like.
IPR013698. Squalene_epoxidase.
[Graphical view]
PfamPF08491. SE. 1 hit.
[Graphical view]
PRINTSPR00420. RNGMNOXGNASE.
ProtoNetSearch...

Other

NextBio973064.
PROP32476.

Entry information

Entry nameERG1_YEAST
AccessionPrimary (citable) accession number: P32476
Secondary accession number(s): D6VUW0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: March 19, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways