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UniProtKB/Swiss-Prot entry P32476


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ERG1_YEAST
Primary accession number P32476
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on October 1, 1996 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 82)
Name and origin of the protein
Protein name Squalene monooxygenase
Synonyms EC 1.14.99.7
Squalene epoxidase
SE
Gene name
Name: ERG1
OrderedLocusNames: YGR175C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=A2-M8;
DOI=10.1016/0378-1119(91)90310-8; PubMed=1743514 [NCBI, ExPASy, EBI, Israel, Japan]
Jandrositz A., Turnowsky F., Hoegenauer G.;
"The gene encoding squalene epoxidase from Saccharomyces cerevisiae: cloning and characterization.";
Gene 107:155-160(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169869 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[3]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[4]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-311, AND MASS SPECTROMETRY.
DOI=10.1038/nbt849; PubMed=12872131 [NCBI, ExPASy, EBI, Israel, Japan]
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.;
"A proteomics approach to understanding protein ubiquitination.";
Nat. Biotechnol. 21:921-926(2003).
[5]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-284, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2135500100; PubMed=14557538 [NCBI, ExPASy, EBI, Israel, Japan]
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery.";
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
[6]
INTERACTION WITH ERG28.
DOI=10.1194/jlr.M500153-JLR200; PubMed=15995173 [NCBI, ExPASy, EBI, Israel, Japan]
Mo C., Bard M.;
"Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex.";
J. Lipid Res. 46:1991-1998(2005).
[7]
TOPOLOGY [LARGE SCALE ANALYSIS].
DOI=10.1073/pnas.0604075103; PubMed=16847258 [NCBI, ExPASy, EBI, Israel, Japan]
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M64994; AAA34592.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z72960; CAA97201.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S64489; S64489.
RefSeq NP_011691.1; -.
3D structure databases
ModBase P32476.
Protein-protein interaction databases
DIP DIP:6325N; -.
IntAct P32476; -.
Enzyme and pathway databases
BioCyc MetaCyc:YGR175C-MON; -.
Organism-specific databases
CYGD YGR175c; -.
SGD S000003407; ERG1.
Yeast-GFP YGR175C.
Gene expression databases
GermOnline YGR175C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005811; Cellular component: lipid particle (inferred from direct assay from SGD).
GO:0005792; Cellular component: microsome (inferred from electronic annotation from UniProtKB-KW).
GO:0008144; Molecular function: drug binding (inferred from mutant phenotype from SGD).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004506; Molecular function: squalene monooxygenase activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0046246; Biological process: terpene biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR006076; FAD-dep_OxRdtase.
IPR003042; Rng_hydrolase.
IPR013698; Squalene_epoxidase.
Graphical view of domain structure.
Pfam PF01266; DAO; 1.
PF08491; SE; 1.
Pfam graphical view of domain structure.
PRINTS PR00420; RNGMNOXGNASE.
ProtoNet P32476.
Proteomic databases
PeptideAtlas P32476; -.
Genome annotation databases
Ensembl YGR175C; Saccharomyces cerevisiae. [Contig view]
GeneID 853086; -.
GenomeReviews Y13135_GR; YGR175C.
KEGG sce:YGR175C; -.
NMPDR fig|4932.3.peg.2818; -.
Phylogenomic databases
HOGENOM P32476; -.
Other
LinkHub P32476; -.
NextBio 973064; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome; Oxidoreductase; Transmembrane; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   496  496     Squalene monooxygenase. PRO_0000209851
TOPO_DOM   1    16  16     Cytoplasmic (Potential). 
TRANSMEM   17    37  21     Potential. 
TOPO_DOM   38   474  437     Lumenal (Potential). 
TRANSMEM   475   495  21     Potential. 
TOPO_DOM   496   496  1     Cytoplasmic (Potential). 
NP_BIND   21    48  28     FAD (Potential). 
CROSSLNK   284   284        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   311   311        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
VARIANT   251   251  1     L -> F (in strain: A2-M8; confers resistance to the allylamine antifungal terbinafine). 
Sequence information
Length: 496 AA [This is the length of the unprocessed precursor] Molecular weight: 55126 Da [This is the MW of the unprocessed precursor] CRC64: BBEFD766634855E8 [This is a checksum on the sequence]
        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 

P32476 in FASTA format

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View entry in raw text format (no links)
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