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P40581 (GPX3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:HYR1
Synonyms:GPX3, ORP1
Ordered Locus Names:YIR037W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length163 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH. Ref.17

Subunit structure

Interacts with YAP1 and probably YBP1. Ref.10

Subcellular location

Cytoplasm. Mitochondrion intermembrane space. Peroxisome matrix Ref.13 Ref.15 Ref.16.

Induction

In contrast to the other two peroxiredoxins, HYP1/GPX3 expression is constitutive, not stress-induced. Ref.5

Post-translational modification

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

Miscellaneous

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

Sequence similarities

Belongs to the glutathione peroxidase family.

Caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 163163Peroxiredoxin HYR1
PRO_0000066643

Sites

Active site361Cysteine sulfenic acid (-SOH) intermediate

Amino acid modifications

Disulfide bond36 ↔ 82Redox-active
Disulfide bond36Interchain (with C-598 in YAP1); transient

Experimental info

Mutagenesis821C → S: Loss of enzyme activity. Ref.17

Secondary structure

........................... 163
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40581 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 46C42B81E895C1A3

FASTA16318,641
        10         20         30         40         50         60 
MSEFYKLAPV DKKGQPFPFD QLKGKVVLIV NVASKCGFTP QYKELEALYK RYKDEGFTII 

        70         80         90        100        110        120 
GFPCNQFGHQ EPGSDEEIAQ FCQLNYGVTF PIMKKIDVNG GNEDPVYKFL KSQKSGMLGL 

       130        140        150        160 
RGIKWNFEKF LVDKKGKVYE RYSSLTKPSS LSETIEELLK EVE 

« Hide

References

« Hide 'large scale' references
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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, PROTEIN OXIDATION.
[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]"The yeast glutaredoxins are active as glutathione peroxidases."
Collinson E.J., Wheeler G.L., Garrido E.O., Avery A.M., Avery S.V., Grant C.M.
J. Biol. Chem. 277:16712-16717(2002) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[14]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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]"Intermembrane space proteome of yeast mitochondria."
Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J., Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.
Mol. Cell. Proteomics 11:1840-1852(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U22446 Genomic DNA. Translation: AAA64283.1.
Z38061 Genomic DNA. Translation: CAA86197.1.
BK006942 Genomic DNA. Translation: DAA08584.1.
PIRS48499.
RefSeqNP_012303.1. NM_001179559.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3CMIX-ray2.02A1-163[»]
ProteinModelPortalP40581.
SMRP40581. Positions 2-162.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35028. 44 interactions.
DIPDIP-1275N.
IntActP40581. 14 interactions.
MINTMINT-401428.
STRING4932.YIR037W.

Protein family/group databases

PeroxiBase3742. SceGPx03.

Proteomic databases

PaxDbP40581.
PeptideAtlasP40581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIR037W; YIR037W; YIR037W.
GeneID854855.
KEGGsce:YIR037W.

Organism-specific databases

CYGDYIR037w.
SGDS000001476. HYR1.

Phylogenomic databases

eggNOGCOG0386.
GeneTreeENSGT00740000115371.
HOGENOMHOG000277054.
KOK00432.
OMAVEYRPLA.
OrthoDBEOG7VHT8G.

Enzyme and pathway databases

BioCycYEAST:YIR037W-MONOMER.

Gene expression databases

GenevestigatorP40581.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR000889. Glutathione_peroxidase.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR11592. PTHR11592. 1 hit.
PfamPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFPIRSF000303. Glutathion_perox. 1 hit.
PRINTSPR01011. GLUTPROXDASE.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP40581.
NextBio977764.

Entry information

Entry nameGPX3_YEAST
AccessionPrimary (citable) accession number: P40581
Secondary accession number(s): D6VVW8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references