Squalene monooxygenase - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P32476 (ERG1_YEAST)

Last modified June 16, 2009. Version 88. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Squalene monooxygenase
    EC=1.14.99.7
Alternative name(s):
    Squalene epoxidase
      Short name=SE

Gene names

Name:	ERG1
Ordered Locus Names:	YGR175C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	496 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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 + AH₂ + O₂ = (S)-squalene-2,3-epoxide + A + H₂O.
Cofactor	FAD.
Enzyme regulation	Inhibited by the allylamine antimycotic drugs.
Pathway	Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl-PP: step 2/3.
Subunit structure	Interacts with ERG28. Ref.6
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. Ref.3
Sequence similarities	Belongs to the squalene monooxygenase family.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lipid particle Inferred from direct assay. Source: SGD microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro drug binding Inferred from mutant phenotype. Source: SGD protein binding Inferred from physical interaction. Source: IntAct squalene monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
	P38845	1	EBI-6545,EBI-24770
CSG2	P35206	1	EBI-6545,EBI-2051140
ERG25	P53045	1	EBI-6545,EBI-6506
ERG4	P25340	1	EBI-6545,EBI-6558
ERP1	Q05359	1	EBI-6545,EBI-6581
ERP4	Q12450	1	EBI-6545,EBI-6598
ERV25	P54837	1	EBI-6545,EBI-6642
ERV29	P53337	1	EBI-6545,EBI-23662
GOT1	Q03554	1	EBI-6545,EBI-2057821
PIS1	P06197	1	EBI-6545,EBI-13458
SNA3	P14359	1	EBI-6545,EBI-26122
SWP1	Q02795	1	EBI-6545,EBI-12666
YVH1	Q02256	1	EBI-6545,EBI-14322

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 496

496

Squalene monooxygenase

PRO_0000209851

Regions

Topological domain

1 – 16

Cytoplasmic Potential

Transmembrane

17 – 37

Potential

Topological domain

38 – 474

437

Lumenal Potential

Transmembrane

475 – 495

Potential

Topological domain

496

Cytoplasmic Potential

Nucleotide binding

21 – 48

FAD Potential

Amino acid modifications

Cross-link

284

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Cross-link

311

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.4

Natural variations

Natural variant

251

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

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Sequences

Sequence

Length

Mass (Da)

Tools

P32476-1 [UniParc].

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

496

55,126

        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

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References

	« Hide 'large scale' referencesShow '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: 1743514] [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. Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]	"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: 12872131] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-311, MASS SPECTROMETRY.
[5]	"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: 14557538] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-284, MASS SPECTROMETRY.
[6]	"Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex." Mo C., Bard M. J. Lipid Res. 46:1991-1998(2005) [PubMed: 15995173] [Abstract] Cited for: INTERACTION WITH ERG28.
[7]	"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: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M64994 Genomic DNA. Translation: AAA34592.1. Z72960 Genomic DNA. Translation: CAA97201.1.
PIR	S64489.
RefSeq	NP_011691.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6325N.
IntAct	P32476. 34 interactions.
Proteomic databases
PeptideAtlas	P32476.
Genome annotation databases
Ensembl	YGR175C. Saccharomyces cerevisiae. [Contig view]
GeneID	853086.
GenomeReviews	Gene locus YGR175C in contig Y13135_GR.
KEGG	sce:YGR175C.
NMPDR	fig\|4932.3.peg.2818.
Organism-specific databases
CYGD	YGR175c.
SGD	S000003407. ERG1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P32476.
OMA	P32476. IPYPLSE.
Enzyme and pathway databases
BioCyc	MetaCyc:YGR175C-MON.
BRENDA	1.14.99.7. 250.
Gene expression databases
GermOnline	YGR175C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006076. FAD-dep_OxRdtase. IPR003042. Rng_hydrolase-like. IPR013698. Squalene_epoxidase. [Graphical view]
Pfam	PF01266. DAO. 1 hit. PF08491. SE. 1 hit. [Graphical view]
PRINTS	PR00420. RNGMNOXGNASE.
ProtoNet	Search...
Other Resources
NextBio	973064.

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Entry information

Entry name

ERG1_YEAST

Accession

Primary (citable) accession number: P32476

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome VII

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents