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UniProtKB/Swiss-Prot entry P27882


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

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Entry information
Entry name ERV1_YEAST
Primary accession number P27882
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 73)
Name and origin of the protein
Protein name Mitochondrial FAD-linked sulfhydryl oxidase ERV1
Synonyms EC 1.8.3.2
Essential for respiration and vegetative growth protein 1
14 kDa regulatory protein
Gene name
Name: ERV1
OrderedLocusNames: YGR029W
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=SC167;
DOI=10.1007/BF00299137; PubMed=1552903 [NCBI, ExPASy, EBI, Israel, Japan]
Lisowsky T.;
"Dual function of a new nuclear gene for oxidative phosphorylation and vegetative growth in yeast.";
Mol. Gen. Genet. 232:58-64(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SF747-19D;
PubMed=8226973 [NCBI, ExPASy, EBI, Israel, Japan]
Nakai M., Endo T., Hase T., Matsubara H.;
"Intramitochondrial protein sorting. Isolation and characterization of the yeast MSP1 gene which belongs to a novel family of putative ATPases.";
J. Biol. Chem. 268:24262-24269(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1002/(SICI)1097-0061(19970915)13:11<1077::AID-YEA152>3.3.CO;2-P; PubMed=9290212 [NCBI, ExPASy, EBI, Israel, Japan]
Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII.";
Yeast 13:1077-1090(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
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]
REVISION OF GENE MODEL.
DOI=10.1002/(SICI)1097-0061(199612)12:15<1501::AID-YEA40>3.0.CO;2-H; PubMed=8972573 [NCBI, ExPASy, EBI, Israel, Japan]
Lisowsky T.;
"Removal of an intron with unique 3' branch site creates an amino-terminal protein sequence directing the scERV1 gene product to mitochondria.";
Yeast 12:1501-1510(1996).
[6]
FUNCTION, AND FAD-BINDING.
DOI=10.1016/S0014-5793(00)01767-1; PubMed=10899311 [NCBI, ExPASy, EBI, Israel, Japan]
Lee J.-E., Hofhaus G., Lisowsky T.;
"Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase.";
FEBS Lett. 477:62-66(2000).
[7]
FUNCTION, MUTAGENESIS OF CYS-30; CYS-33; CYS-130; CYS-133; CYS-159 AND CYS-176, AND SUBUNIT.
DOI=10.1046/j.1432-1033.2003.03519.x; PubMed=12654008 [NCBI, ExPASy, EBI, Israel, Japan]
Hofhaus G., Lee J.E., Tews I., Rosenberg B., Lisowsky T.;
"The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre.";
Eur. J. Biochem. 270:1528-1535(2003).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1093/embo-reports/kve161; PubMed=11493598 [NCBI, ExPASy, EBI, Israel, Japan]
Lange H., Lisowsky T., Gerber J., Muhlenhoff U., Kispal G., Lill R.;
"An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins.";
EMBO Rep. 2:715-720(2001).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2135385100; PubMed=14576278 [NCBI, ExPASy, EBI, Israel, Japan]
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[10]
FUNCTION, AND INTERACTION WITH MIA40.
DOI=10.1016/j.cell.2005.04.011; PubMed=15989955 [NCBI, ExPASy, EBI, Israel, Japan]
Mesecke N., Terziyska N., Kozany C., Baumann F., Neupert W., Hell K., Herrmann J.M.;
"A disulfide relay system in the intermembrane space of mitochondria that mediates protein import.";
Cell 121:1059-1069(2005).
[11]
FUNCTION, AND INTERACTION WITH MIA40.
DOI=10.1016/j.jmb.2005.08.051; PubMed=16181637 [NCBI, ExPASy, EBI, Israel, Japan]
Rissler M., Wiedemann N., Pfannschmidt S., Gabriel K., Guiard B., Pfanner N., Chacinska A.;
"The essential mitochondrial protein Erv1 cooperates with Mia40 in biogenesis of intermembrane space proteins.";
J. Mol. Biol. 353:485-492(2005).
[12]
FUNCTION.
DOI=10.1016/j.jmb.2005.08.049; PubMed=16185707 [NCBI, ExPASy, EBI, Israel, Japan]
Allen S., Balabanidou V., Sideris D.P., Lisowsky T., Tokatlidis K.;
"Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c.";
J. Mol. Biol. 353:937-944(2005).
Comments
  • FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS). Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine residues in MIA40 in an oxidized state. Reduced ERV1 is reoxidized by cytochrome c. Required for the maturation of cytoplasmic, but not of mitochondrial Fe/S proteins.
  • CATALYTIC ACTIVITY: 4 R'C(R)SH + O2 = 2 R'C(R)S-S(R)CR' + 2 H2O.
  • COFACTOR: FAD.
  • SUBUNIT: Homodimer. Interacts with MIA40, forming transient intermolecular disulfide bridges.
  • SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
  • SIMILARITY: Contains 1 ERV/ALR sulfhydryl oxidase domain.
  • SEQUENCE CAUTION:
    • Sequence=AAB48659.1; Type=Erroneous gene model prediction;
    • Sequence=CAA43129.1; Type=Erroneous gene model prediction;
    • Sequence=CAA48192.1; Type=Erroneous gene model prediction;
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
X60722; CAA43129.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M74772; AAB48659.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X68055; CAA48192.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z72814; CAA97017.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z72813; CAA97016.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S20469; S20469.
RefSeq NP_011543.2; -.
3D structure databases
HSSP Q63042; 1OQC. [HSSP ENTRY / PDB]
ModBase P27882.
Protein-protein interaction databases
IntAct P27882; -.
Organism-specific databases
CYGD YGR029w; -.
SGD S000003261; ERV1.
Yeast-GFP YGR029W.
Gene expression databases
GermOnline YGR029W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005758; Cellular component: mitochondrial intermembrane space (inferred from direct assay from SGD).
GO:0016971; Molecular function: flavin-linked sulfhydryl oxidase activity (inferred from direct assay from SGD).
GO:0006879; Biological process: cellular iron ion homeostasis (inferred from direct assay from SGD).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
GO:0045041; Biological process: protein import into mitochondrial intermembrane space (inferred from mutant phenotype from SGD).
GO:0006979; Biological process: response to oxidative stress (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR006863; Evr1_Alr.
Graphical view of domain structure.
Gene3D G3DSA:1.20.120.310; Evr1_Alr; 1.
Pfam PF04777; Evr1_Alr; 1.
Pfam graphical view of domain structure.
PROSITE PS51324; ERV_ALR; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P27882.
Proteomic databases
PeptideAtlas P27882; -.
Genome annotation databases
Ensembl YGR029W; Saccharomyces cerevisiae. [Contig view]
GeneID 852916; -.
GenomeReviews Y13135_GR; YGR029W.
KEGG sce:YGR029W; -.
NMPDR fig|4932.3.peg.2655; -.
Phylogenomic databases
HOGENOM P27882; -.
Other
LinkHub P27882; -.
NextBio 972617; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   189  189     Mitochondrial FAD-linked sulfhydryl oxidase ERV1. PRO_0000001187
DOMAIN   83   183  101     ERV/ALR sulfhydryl oxidase. 
REGION   166   183  18     FAD-binding (By similarity). 
DISULFID   130   133        Redox-active (By similarity). 
DISULFID   159   176        By similarity. 
MUTAGEN   30    30        C->S: Reduces catalytic activity 3-fold. 
MUTAGEN   33    33        C->S: Reduces catalytic activity 2-fold. 
MUTAGEN   130   130        C->S: Loss of function. 
MUTAGEN   133   133        C->S: Loss of function. 
MUTAGEN   159   159        C->S: Reduces catalytic activity 3.3-fold. 
MUTAGEN   176   176        C->S: Reduces catalytic activity 2.6-fold. 
Sequence information
Length: 189 AA [This is the length of the unprocessed precursor] Molecular weight: 21639 Da [This is the MW of the unprocessed precursor] CRC64: 83DADA0DB1DF17CC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKAIDKMTDN PPQEGLSGRK IIYDEDGKPC RSCNTLLDFQ YVTGKISNGL KNLSSNGKLA 

        70         80         90        100        110        120 
GTGALTGEAS ELMPGSRTYR KVDPPDVEQL GRSSWTLLHS VAASYPAQPT DQQKGEMKQF 

       130        140        150        160        170        180 
LNIFSHIYPC NWCAKDFEKY IRENAPQVES REELGRWMCE AHNKVNKKLR KPKFDCNFWE 


KRWKDGWDE 

P27882 in FASTA format

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