Squalene monooxygenase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32476 (ERG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 127. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Squalene monooxygenase
EC=1.14.13.132

Alternative name(s):
Squalene epoxidase
Short name=SE

Gene names

Name:	ERG1
Ordered Locus Names:	YGR175C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	496 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane Transmembrane helix
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ergosterol biosynthetic process Inferred from mutant phenotype PubMed 200835. Source: SGD
Cellular_component	endoplasmic reticulum Inferred from direct assay PubMed 9450962. Source: SGD 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 PubMed 9450962. Source: SGD
Molecular_function	drug binding Inferred from mutant phenotype PubMed 14638499. Source: SGD flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro squalene monooxygenase activity Inferred from direct assay PubMed 9450962. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
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
YHR146W	P38845	1	EBI-6545,EBI-24770
YVH1	Q02256	1	EBI-6545,EBI-14322

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

Helical; Potential

Topological domain

38 – 474

437

Lumenal Potential

Transmembrane

475 – 495

Helical; 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.6

Cross-link

311

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

Natural variations

Natural variant

251

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

Sequences

Sequence

Length

Mass (Da)

Tools

P32476 [UniParc].

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

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

« Hide

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] [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. Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.
+	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.
PIR	S64489.
RefSeq	NP_011691.1. NM_001181304.1.
3D structure databases
ProteinModelPortal	P32476.
SMR	P32476. Positions 20-54, 327-364.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6325N.
IntAct	P32476. 16 interactions.
MINT	MINT-1324933.
STRING	4932.YGR175C.
Proteomic databases
PaxDb	P32476.
PeptideAtlas	P32476.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR175C; YGR175C; YGR175C.
GeneID	853086.
KEGG	sce:YGR175C.
Organism-specific databases
CYGD	YGR175c.
SGD	S000003407. ERG1.
Phylogenomic databases
eggNOG	COG0654.
GeneTree	ENSGT00390000011759.
HOGENOM	HOG000174713.
KO	K00511.
OMA	YSEMKYM.
OrthoDB	EOG47M56T.
Enzyme and pathway databases
BioCyc	MetaCyc:YGR175C-MONOMER. YEAST:YGR175C-MONOMER.
UniPathway	UPA00767; UER00752.
Gene expression databases
Genevestigator	P32476.
GermOnline	YGR175C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003042. Rng_hydrolase-like. IPR013698. Squalene_epoxidase. [Graphical view]
Pfam	PF08491. SE. 1 hit. [Graphical view]
PRINTS	PR00420. RNGMNOXGNASE.
ProtoNet	Search...
Other
ChEMBL	CHEMBL1888.
NextBio	973064.

Entry information

Entry name

ERG1_YEAST

Accession

Primary (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:	May 29, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome VII

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents