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P40581

- GPX3_YEAST

UniProt

P40581 - GPX3_YEAST

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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

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
Complete GO annotation...

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
Complete GO annotation...

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. 45 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.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277054.
InParanoidiP40581.
KOiK00432.
OMAiPFTKPEK.
OrthoDBiEOG7VHT8G.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
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

        10         20         30         40         50
MSEFYKLAPV DKKGQPFPFD QLKGKVVLIV NVASKCGFTP QYKELEALYK
60 70 80 90 100
RYKDEGFTII GFPCNQFGHQ EPGSDEEIAQ FCQLNYGVTF PIMKKIDVNG
110 120 130 140 150
GNEDPVYKFL KSQKSGMLGL RGIKWNFEKF LVDKKGKVYE RYSSLTKPSS
160
LSETIEELLK EVE
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. 45 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 ENSGT00760000119230.
HOGENOMi HOG000277054.
InParanoidi P40581.
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.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 126 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