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P40581

- GPX3_YEAST

UniProt

P40581 - GPX3_YEAST

Protein

Peroxiredoxin HYR1

Gene

HYR1

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 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Involved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator YAP1, which is involved in transcription activation of genes of the oxidative stress response pathway. May also play a direct role in hydroperoxide scavenging, being the most active of three closely related S.cerevisiae peroxiredoxins (GPX1, GPX2, and HYP1/GPX3) with respect to peroxide and lipid hydroperoxide reduction. The three enzymes are not required for the glutaredoxin-mediated antioxidant function. In the presence of peroxides, HYP1 is directly oxidized at Cys-36 to form a cysteine sulfenic acid (-SOH). Cys-36-SOH then forms either an intramolecular disulfide bond (Cys-36 with Cys-82) or a transient, intermolecular disulfide bond with 'Cys-598' of YAP1, which is further resolved into a YAP1 intramolecular disulfide bond ('Cys-303' with 'Cys-598') and a reduced Cys-36 in HYP1/GPX3.8 Publications

    Catalytic activityi

    2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei36 – 361Cysteine sulfenic acid (-SOH) intermediate

    GO - Molecular functioni

    1. glutathione peroxidase activity Source: SGD
    2. peroxiredoxin activity Source: UniProtKB-EC
    3. phospholipid-hydroperoxide glutathione peroxidase activity Source: SGD

    GO - Biological processi

    1. cellular response to oxidative stress Source: SGD

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Enzyme and pathway databases

    BioCyciYEAST:YIR037W-MONOMER.

    Protein family/group databases

    PeroxiBasei3742. SceGPx03.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxiredoxin HYR1 (EC:1.11.1.15)
    Alternative name(s):
    Glutathione peroxidase 3
    Hydrogen peroxide resistance protein 1
    Oxidant receptor peroxidase 1
    Phospholipid hydroperoxide glutathione peroxidase 3
    Short name:
    PHGPx3
    Gene namesi
    Name:HYR1
    Synonyms:GPX3, ORP1
    Ordered Locus Names:YIR037W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IX

    Organism-specific databases

    CYGDiYIR037w.
    SGDiS000001476. HYR1.

    Subcellular locationi

    GO - Cellular componenti

    1. intracellular Source: SGD
    2. mitochondrial intermembrane space Source: SGD
    3. peroxisomal matrix Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Peroxisome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi82 – 821C → S: Loss of enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 163163Peroxiredoxin HYR1PRO_0000066643Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi36 ↔ 82Redox-active
    Disulfide bondi36 – 36Interchain (with C-598 in YAP1); transient

    Post-translational modificationi

    Reversible disulfide bond formation between Cys-36 and Cys-82 upon peroxide reduction; probably reverted by thioredoxin (TRX2).

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiP40581.
    PaxDbiP40581.
    PeptideAtlasiP40581.

    Expressioni

    Inductioni

    In contrast to the other two peroxiredoxins, HYP1/GPX3 expression is constitutive, not stress-induced.1 Publication

    Gene expression databases

    GenevestigatoriP40581.

    Interactioni

    Subunit structurei

    Interacts with YAP1 and probably YBP1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADE17P380091EBI-7869,EBI-14223
    ALO1P547831EBI-7869,EBI-2519
    CAR2P079911EBI-7869,EBI-12430
    ERG11P106141EBI-7869,EBI-5127
    GAP1P191451EBI-7869,EBI-7314
    GLN1P322881EBI-7869,EBI-7665
    HXT7P390041EBI-7869,EBI-8790
    PDR12Q027851EBI-7869,EBI-13065
    PEX11Q124621EBI-7869,EBI-13198
    PMP2P409751EBI-7869,EBI-2043041
    PMP3P872841EBI-7869,EBI-13555
    RNR2P099381EBI-7869,EBI-15240
    YBL039W-BP0C2681EBI-7869,EBI-2044092

    Protein-protein interaction databases

    BioGridi35028. 44 interactions.
    DIPiDIP-1275N.
    IntActiP40581. 14 interactions.
    MINTiMINT-401428.
    STRINGi4932.YIR037W.

    Structurei

    Secondary structure

    1
    163
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 64
    Helixi19 – 224
    Beta strandi26 – 3611
    Helixi39 – 5214
    Helixi53 – 553
    Beta strandi57 – 648
    Beta strandi97 – 1004
    Helixi105 – 1139
    Beta strandi117 – 1193
    Beta strandi129 – 1324
    Beta strandi134 – 1363
    Beta strandi138 – 1425
    Helixi148 – 1514
    Helixi152 – 1598

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CMIX-ray2.02A1-163[»]
    ProteinModelPortaliP40581.
    SMRiP40581. Positions 2-162.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40581.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutathione peroxidase family.Curated

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0386.
    GeneTreeiENSGT00740000115371.
    HOGENOMiHOG000277054.
    KOiK00432.
    OMAiPFTKPEK.
    OrthoDBiEOG7VHT8G.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR000889. Glutathione_peroxidase.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PANTHERiPTHR11592. PTHR11592. 1 hit.
    PfamiPF00255. GSHPx. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
    PRINTSiPR01011. GLUTPROXDASE.
    SUPFAMiSSF52833. SSF52833. 1 hit.
    PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
    PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
    PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P40581-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEFYKLAPV DKKGQPFPFD QLKGKVVLIV NVASKCGFTP QYKELEALYK    50
    RYKDEGFTII GFPCNQFGHQ EPGSDEEIAQ FCQLNYGVTF PIMKKIDVNG 100
    GNEDPVYKFL KSQKSGMLGL RGIKWNFEKF LVDKKGKVYE RYSSLTKPSS 150
    LSETIEELLK EVE 163
    Length:163
    Mass (Da):18,641
    Last modified:February 1, 1995 - v1
    Checksum:i46C42B81E895C1A3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22446 Genomic DNA. Translation: AAA64283.1.
    Z38061 Genomic DNA. Translation: CAA86197.1.
    BK006942 Genomic DNA. Translation: DAA08584.1.
    PIRiS48499.
    RefSeqiNP_012303.1. NM_001179559.1.

    Genome annotation databases

    EnsemblFungiiYIR037W; YIR037W; YIR037W.
    GeneIDi854855.
    KEGGisce:YIR037W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22446 Genomic DNA. Translation: AAA64283.1 .
    Z38061 Genomic DNA. Translation: CAA86197.1 .
    BK006942 Genomic DNA. Translation: DAA08584.1 .
    PIRi S48499.
    RefSeqi NP_012303.1. NM_001179559.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CMI X-ray 2.02 A 1-163 [» ]
    ProteinModelPortali P40581.
    SMRi P40581. Positions 2-162.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35028. 44 interactions.
    DIPi DIP-1275N.
    IntActi P40581. 14 interactions.
    MINTi MINT-401428.
    STRINGi 4932.YIR037W.

    Protein family/group databases

    PeroxiBasei 3742. SceGPx03.

    Proteomic databases

    MaxQBi P40581.
    PaxDbi P40581.
    PeptideAtlasi P40581.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YIR037W ; YIR037W ; YIR037W .
    GeneIDi 854855.
    KEGGi sce:YIR037W.

    Organism-specific databases

    CYGDi YIR037w.
    SGDi S000001476. HYR1.

    Phylogenomic databases

    eggNOGi COG0386.
    GeneTreei ENSGT00740000115371.
    HOGENOMi HOG000277054.
    KOi K00432.
    OMAi PFTKPEK.
    OrthoDBi EOG7VHT8G.

    Enzyme and pathway databases

    BioCyci YEAST:YIR037W-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P40581.
    NextBioi 977764.

    Gene expression databases

    Genevestigatori P40581.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR000889. Glutathione_peroxidase.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    PANTHERi PTHR11592. PTHR11592. 1 hit.
    Pfami PF00255. GSHPx. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000303. Glutathion_perox. 1 hit.
    PRINTSi PR01011. GLUTPROXDASE.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    PROSITEi PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
    PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
    PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and phenotypic characterization of a glutathione-peroxidase like gene involved in the oxidative stress response of Saccharomyces cerevisiae."
      Budde E., Stahl U.
      Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 38626 / AH22 / NRRL Y-12843.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Phospholipid hydroperoxide glutathione peroxidase (PHGPx): more than an antioxidant enzyme?"
      Ursini F., Maiorino M., Roveri A.
      Biomed. Environ. Sci. 10:327-332(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae."
      Inoue Y., Matsuda T., Sugiyama K., Izawa S., Kimura A.
      J. Biol. Chem. 274:27002-27009(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    6. "Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases."
      Avery A.M., Avery S.V.
      J. Biol. Chem. 276:33730-33735(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, FUNCTION AS A PHGPX.
    7. Cited for: FUNCTION AS A GLUTAREDOXIN.
    8. "A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation."
      Delaunay A., Pflieger D., Barrault M.-B., Vinh J., Toledano M.B.
      Cell 111:471-481(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, OXIDATION OF YAP1.
    9. "Structure, mechanism and regulation of peroxiredoxins."
      Wood Z.A., Schroder E., Robin Harris J., Poole L.B.
      Trends Biochem. Sci. 28:32-40(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A PEROXIREDOXIN.
    10. "Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor."
      Veal E.A., Ross S.J., Malakasi P., Peacock E., Morgan B.A.
      J. Biol. Chem. 278:30896-30904(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH YBP1.
    11. "Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling."
      Azevedo D., Tacnet F., Delaunay A., Rodrigues-Pousada C., Toledano M.B.
      Free Radic. Biol. Med. 35:889-900(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ACTIVATING SUBSTANCES.
    12. "Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress."
      Carmel-Harel O., Storz G.
      Annu. Rev. Microbiol. 54:439-461(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    14. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    15. "Involvement of glutathione peroxidase 1 in growth and peroxisome formation in Saccharomyces cerevisiae in oleic acid medium."
      Ohdate T., Inoue Y.
      Biochim. Biophys. Acta 1821:1295-1305(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    16. Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "Crystal structure of glutathione-dependent phospholipid peroxidase Hyr1 from the yeast Saccharomyces cerevisiae."
      Zhang W.J., He Y.-X., Yang Z., Yu J., Chen Y., Zhou C.-Z.
      Proteins 73:1058-1062(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS), CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-82.

    Entry informationi

    Entry nameiGPX3_YEAST
    AccessioniPrimary (citable) accession number: P40581
    Secondary accession number(s): D6VVW8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 8000 molecules/cell in log phase SD medium.1 Publication

    Caution

    Was originally thought to be a glutathione peroxidase or a phospholipid hydroperoxide glutathione peroxidase. HYP1 does not require glutathione for hydroperoxide reduction.Curated

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

    External Data

    Dasty 3