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P27882

- ERV1_YEAST

UniProt

P27882 - ERV1_YEAST

Protein

Mitochondrial FAD-linked sulfhydryl oxidase ERV1

Gene

ERV1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    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.6 PublicationsPROSITE-ProRule annotation

    Catalytic activityi

    2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2.

    Cofactori

    FAD.1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. flavin-linked sulfhydryl oxidase activity Source: SGD
    2. protein binding Source: IntAct
    3. thiol oxidase activity Source: SGD

    GO - Biological processi

    1. cellular iron ion homeostasis Source: SGD
    2. cellular response to oxidative stress Source: SGD
    3. protein import into mitochondrial intermembrane space Source: SGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30753-MONOMER.
    ReactomeiREACT_189012. Mitochondrial protein import.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial FAD-linked sulfhydryl oxidase ERV1 (EC:1.8.3.2)
    Alternative name(s):
    14 kDa regulatory protein
    Essential for respiration and vegetative growth protein 1
    Gene namesi
    Name:ERV1
    Ordered Locus Names:YGR029W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR029w.
    SGDiS000003261. ERV1.

    Subcellular locationi

    Mitochondrion intermembrane space 2 Publications

    GO - Cellular componenti

    1. mitochondrial intermembrane space Source: SGD

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi30 – 301C → S: Reduces catalytic activity 3-fold. 1 Publication
    Mutagenesisi33 – 331C → S: Reduces catalytic activity 2-fold. 1 Publication
    Mutagenesisi130 – 1301C → S: Loss of function. 1 Publication
    Mutagenesisi133 – 1331C → S: Loss of function. 1 Publication
    Mutagenesisi159 – 1591C → S: Reduces catalytic activity 3.3-fold. 1 Publication
    Mutagenesisi176 – 1761C → S: Reduces catalytic activity 2.6-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 189189Mitochondrial FAD-linked sulfhydryl oxidase ERV1PRO_0000001187Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi130 ↔ 133Redox-activePROSITE-ProRule annotation
    Disulfide bondi159 ↔ 176PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiP27882.
    PaxDbiP27882.
    PeptideAtlasiP27882.

    Expressioni

    Gene expression databases

    GenevestigatoriP27882.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with MIA40, forming transient intermolecular disulfide bridges.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MIA40P360462EBI-6621,EBI-26978

    Protein-protein interaction databases

    BioGridi33273. 22 interactions.
    IntActiP27882. 5 interactions.
    STRINGi4932.YGR029W.

    Structurei

    Secondary structure

    1
    189
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 183
    Beta strandi26 – 294
    Helixi36 – 438
    Turni44 – 463
    Helixi87 – 10317
    Helixi111 – 12717
    Helixi131 – 14313
    Helixi151 – 16818
    Helixi176 – 1783
    Helixi179 – 1835

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3W4YX-ray2.00A/B/C73-189[»]
    4E0HX-ray2.00A86-189[»]
    4E0IX-ray3.00A/B/C1-189[»]
    ProteinModelPortaliP27882.
    SMRiP27882. Positions 14-188.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini83 – 183101ERV/ALR sulfhydryl oxidasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni166 – 18318FAD-bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ERV/ALR sulfhydryl oxidase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5054.
    GeneTreeiENSGT00390000001979.
    HOGENOMiHOG000195924.
    KOiK17783.
    OMAiYKEMASS.
    OrthoDBiEOG7WDNCT.

    Family and domain databases

    Gene3Di1.20.120.310. 1 hit.
    InterProiIPR017905. ERV/ALR_sulphydryl_oxidase.
    [Graphical view]
    PfamiPF04777. Evr1_Alr. 1 hit.
    [Graphical view]
    SUPFAMiSSF69000. SSF69000. 1 hit.
    PROSITEiPS51324. ERV_ALR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P27882-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKAIDKMTDN PPQEGLSGRK IIYDEDGKPC RSCNTLLDFQ YVTGKISNGL    50
    KNLSSNGKLA GTGALTGEAS ELMPGSRTYR KVDPPDVEQL GRSSWTLLHS 100
    VAASYPAQPT DQQKGEMKQF LNIFSHIYPC NWCAKDFEKY IRENAPQVES 150
    REELGRWMCE AHNKVNKKLR KPKFDCNFWE KRWKDGWDE 189
    Length:189
    Mass (Da):21,639
    Last modified:November 1, 1997 - v2
    Checksum:i83DADA0DB1DF17CC
    GO

    Sequence cautioni

    The sequence AAB48659.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAA43129.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAA48192.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60722 Genomic DNA. Translation: CAA43129.1. Sequence problems.
    M74772 Genomic DNA. Translation: AAB48659.1. Sequence problems.
    X68055 Genomic DNA. Translation: CAA48192.1. Sequence problems.
    Z72814 Genomic DNA. Translation: CAA97017.1.
    Z72813 Genomic DNA. Translation: CAA97016.1.
    BK006941 Genomic DNA. Translation: DAA08125.1.
    PIRiS20469.
    RefSeqiNP_011543.4. NM_001181158.3.

    Genome annotation databases

    EnsemblFungiiYGR029W; YGR029W; YGR029W.
    GeneIDi852916.
    KEGGisce:YGR029W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60722 Genomic DNA. Translation: CAA43129.1 . Sequence problems.
    M74772 Genomic DNA. Translation: AAB48659.1 . Sequence problems.
    X68055 Genomic DNA. Translation: CAA48192.1 . Sequence problems.
    Z72814 Genomic DNA. Translation: CAA97017.1 .
    Z72813 Genomic DNA. Translation: CAA97016.1 .
    BK006941 Genomic DNA. Translation: DAA08125.1 .
    PIRi S20469.
    RefSeqi NP_011543.4. NM_001181158.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3W4Y X-ray 2.00 A/B/C 73-189 [» ]
    4E0H X-ray 2.00 A 86-189 [» ]
    4E0I X-ray 3.00 A/B/C 1-189 [» ]
    ProteinModelPortali P27882.
    SMRi P27882. Positions 14-188.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33273. 22 interactions.
    IntActi P27882. 5 interactions.
    STRINGi 4932.YGR029W.

    Proteomic databases

    MaxQBi P27882.
    PaxDbi P27882.
    PeptideAtlasi P27882.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR029W ; YGR029W ; YGR029W .
    GeneIDi 852916.
    KEGGi sce:YGR029W.

    Organism-specific databases

    CYGDi YGR029w.
    SGDi S000003261. ERV1.

    Phylogenomic databases

    eggNOGi COG5054.
    GeneTreei ENSGT00390000001979.
    HOGENOMi HOG000195924.
    KOi K17783.
    OMAi YKEMASS.
    OrthoDBi EOG7WDNCT.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30753-MONOMER.
    Reactomei REACT_189012. Mitochondrial protein import.

    Miscellaneous databases

    NextBioi 972617.
    PROi P27882.

    Gene expression databases

    Genevestigatori P27882.

    Family and domain databases

    Gene3Di 1.20.120.310. 1 hit.
    InterProi IPR017905. ERV/ALR_sulphydryl_oxidase.
    [Graphical view ]
    Pfami PF04777. Evr1_Alr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69000. SSF69000. 1 hit.
    PROSITEi PS51324. ERV_ALR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Dual function of a new nuclear gene for oxidative phosphorylation and vegetative growth in yeast."
      Lisowsky T.
      Mol. Gen. Genet. 232:58-64(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: SC167.
    2. "Intramitochondrial protein sorting. Isolation and characterization of the yeast MSP1 gene which belongs to a novel family of putative ATPases."
      Nakai M., Endo T., Hase T., Matsubara H.
      J. Biol. Chem. 268:24262-24269(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: SF747-19D.
    3. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
      Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
      Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    4. "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.
      , 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.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "Removal of an intron with unique 3' branch site creates an amino-terminal protein sequence directing the scERV1 gene product to mitochondria."
      Lisowsky T.
      Yeast 12:1501-1510(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVISION OF GENE MODEL.
    7. "Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase."
      Lee J.-E., Hofhaus G., Lisowsky T.
      FEBS Lett. 477:62-66(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, FAD-BINDING.
    8. "The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre."
      Hofhaus G., Lee J.E., Tews I., Rosenberg B., Lisowsky T.
      Eur. J. Biochem. 270:1528-1535(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-30; CYS-33; CYS-130; CYS-133; CYS-159 AND CYS-176, SUBUNIT.
    9. "An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins."
      Lange H., Lisowsky T., Gerber J., Muhlenhoff U., Kispal G., Lill R.
      EMBO Rep. 2:715-720(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    11. "A disulfide relay system in the intermembrane space of mitochondria that mediates protein import."
      Mesecke N., Terziyska N., Kozany C., Baumann F., Neupert W., Hell K., Herrmann J.M.
      Cell 121:1059-1069(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MIA40.
    12. "The essential mitochondrial protein Erv1 cooperates with Mia40 in biogenesis of intermembrane space proteins."
      Rissler M., Wiedemann N., Pfannschmidt S., Gabriel K., Guiard B., Pfanner N., Chacinska A.
      J. Mol. Biol. 353:485-492(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MIA40.
    13. "Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c."
      Allen S., Balabanidou V., Sideris D.P., Lisowsky T., Tokatlidis K.
      J. Mol. Biol. 353:937-944(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiERV1_YEAST
    AccessioniPrimary (citable) accession number: P27882
    Secondary accession number(s): D6VUG4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3