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UniProtKB/Swiss-Prot entry P53045


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

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Entry information
Entry name ERG25_YEAST
Primary accession number P53045
Secondary accession number Q45U26
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 72)
Name and origin of the protein
Protein name C-4 methylsterol oxidase
Synonyms EC 1.14.13.72
Methylsterol monooxygenase
Gene name
Name: ERG25
Synonyms: FET6
OrderedLocusNames: YGR060W
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].
DOI=10.1073/pnas.93.1.186; PubMed=8552601 [NCBI, ExPASy, EBI, Israel, Japan]
Bard M., Bruner D.A., Pierson C.A., Lees N.D., Biermann B., Frye L., Koegel C., Barbuch R.;
"Cloning and characterization of ERG25, the Saccharomyces cerevisiae gene encoding C-4 sterol methyl oxidase.";
Proc. Natl. Acad. Sci. U.S.A. 93:186-190(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.271.28.16927; PubMed=8663358 [NCBI, ExPASy, EBI, Israel, Japan]
Li L., Kaplan J.;
"Characterization of yeast methyl sterol oxidase (ERG25) and identification of a human homologue.";
J. Biol. Chem. 271:16927-16933(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SK1;
DOI=10.1038/ng1674; PubMed=16273108 [NCBI, ExPASy, EBI, Israel, Japan]
Deutschbauer A.M., Davis R.W.;
"Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
Nat. Genet. 37:1333-1340(2005).
[4]
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).
[5]
SUBUNIT, INTERACTION WITH ERG27 AND ERG28, AND SUBCELLULAR LOCATION.
DOI=10.1073/pnas.112202799; PubMed=12119386 [NCBI, ExPASy, EBI, Israel, Japan]
Mo C., Valachovic M., Randall S.K., Nickels J.T., Bard M.;
"Protein-protein interactions among C-4 demethylation enzymes involved in yeast sterol biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 99:9739-9744(2002).
[6]
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).
[7]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-96, 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).
[8]
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).
[9]
SUBCELLULAR LOCATION.
DOI=10.1074/mcp.M400123-MCP200; PubMed=15716577 [NCBI, ExPASy, EBI, Israel, Japan]
Natter K., Leitner P., Faschinger A., Wolinski H., McCraith S., Fields S., Kohlwein S.D.;
"The spatial organization of lipid synthesis in the yeast Saccharomyces cerevisiae derived from large scale green fluorescent protein tagging and high resolution microscopy.";
Mol. Cell. Proteomics 4:662-672(2005).
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
U31885; AAC49139.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ115391; AAZ22473.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z72845; CAA97062.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S64354; S64354.
RefSeq NP_011574.1; -.
3D structure databases
ModBase P53045.
Protein-protein interaction databases
DIP DIP:2799N; -.
IntAct P53045; 45.
Organism-specific databases
CYGD YGR060w; -.
SGD S000003292; ERG25.
Yeast-GFP YGR060W.
Gene expression databases
GermOnline YGR060W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from direct assay from SGD).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from SGD).
GO:0000254; Molecular function: C-4 methylsterol oxidase activity (inferred from electronic annotation from EC).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006696; Biological process: ergosterol biosynthetic process (inferred from direct assay from SGD).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006088; Sterol_desatur.
Graphical view of domain structure.
Pfam PF01598; Sterol_desat; 1.
Pfam graphical view of domain structure.
Proteomic databases
PeptideAtlas P53045; -.
Proteomics databases
PRIDE P53045; -.
Genome annotation databases
Ensembl YGR060W; Saccharomyces cerevisiae. [Contig view]
GeneID 852951; -.
GenomeReviews Y13135_GR; YGR060W.
KEGG sce:YGR060W; -.
NMPDR fig|4932.3.peg.2690; -.
Phylogenomic databases
HOGENOM P53045; -.
Other
LinkHub P53045; -.
NextBio 972708; -.
ProtoNet P53045.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Endoplasmic reticulum; Iron; Lipid synthesis; Membrane; NAD; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis; Transmembrane; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   309  309     C-4 methylsterol oxidase. PRO_0000117039
TRANSMEM   56    76  21     Potential. 
MOTIF   160   164  5     Histidine box-1. 
MOTIF   173   177  5     Histidine box-2. 
MOTIF   257   263  7     Histidine box-3. 
CROSSLNK   96    96        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
Sequence information
Length: 309 AA [This is the length of the unprocessed precursor] Molecular weight: 36479 Da [This is the MW of the unprocessed precursor] CRC64: E0422C416DD17794 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSAVFNNATL SGLVQASTYS QTLQNVAHYQ PQLNFMEKYW AAWYSYMNND VLATGLMFFL 

        70         80         90        100        110        120 
LHEFMYFFRC LPWFIIDQIP YFRRWKLQPT KIPSAKEQLY CLKSVLLSHF LVEAIPIWTF 

       130        140        150        160        170        180 
HPMCEKLGIT VEVPFPSLKT MALEIGLFFV LEDTWHYWAH RLFHYGVFYK YIHKQHHRYA 

       190        200        210        220        230        240 
APFGLSAEYA HPAETLSLGF GTVGMPILYV MYTGKLHLFT LCVWITLRLF QAVDSHSGYD 

       250        260        270        280        290        300 
FPWSLNKIMP FWAGAEHHDL HHHYFIGNYA SSFRWWDYCL DTESGPEAKA SREERMKKRA 


ENNAQKKTN 

P53045 in FASTA format

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