UniProtKB - P34760 (TSA1_YEAST)
Peroxiredoxin TSA1
TSA1
Functioni
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (PubMed:2895105, PubMed:7961686, PubMed:10681558, PubMed:15210711, PubMed:19106090).
Protects the cell against the oxidative stress caused by nascent-protein misfolding and aggregation (PubMed:24424024).
Relays hydrogen peroxide as a signal to the transcription factor YAP1 by inducing the formation of intramolecular disulfide bonds in YAP1, which causes its nuclear accumulation and activation (PubMed:15706081, PubMed:19106090).
Can act alternatively as peroxidase and molecular chaperone. Oxidative stress and heat shock exposure cause a reversible shift of the protein structure from low MW species to high MW complexes, triggering a peroxidase-to-chaperone functional switch. The chaperone function of the protein enhances resistance to heat shock (PubMed:15163410).
8 PublicationsMiscellaneous
Catalytic activityi
- EC:1.11.1.241 Publication
Kineticsi
- KM=3 µM for H2O21 Publication
- KM=4 µM for cumene hydroperoxide1 Publication
- KM=10 µM for tert-butyl hydroperoxide1 Publication
- KM=2 µM for TRX11 Publication
- KM=3 µM for TRX21 Publication
- KM=12 µM for H2O21 Publication
- KM=17.1 µM for cumene hydroperoxide1 Publication
- KM=7.9 µM for tert-butyl hydroperoxide1 Publication
- Vmax=4.8 µmol/min/mg enzyme for H2O21 Publication
- Vmax=2.2 µmol/min/mg enzyme for cumene hydroperoxide1 Publication
- Vmax=2.4 µmol/min/mg enzyme for tert-butyl hydroperoxide1 Publication
- Vmax=5.5 µmol/min/mg enzyme for TRX11 Publication
- Vmax=5.5 µmol/min/mg enzyme for TRX21 Publication
- Vmax=0.66 µM/sec/mg enzyme for H2O21 Publication
- Vmax=0.56 µM/sec/mg enzyme for cumene hydroperoxide1 Publication
- Vmax=0.61 µM/sec/mg enzyme for tert-butyl hydroperoxide1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 45 | Important for catalytic activity, helps activating the peroxidatic cysteine through H-bonding | 1 | |
Active sitei | 48 | Cysteine sulfenic acid (-SOH) intermediate1 Publication | 1 | |
Binding sitei | 124 | SubstrateCombined sources1 Publication | 1 |
GO - Molecular functioni
- identical protein binding Source: CAFA
- kinase regulator activity Source: SGD
- peroxiredoxin activity Source: SGD
- ribosome binding Source: SGD
- thioredoxin peroxidase activity Source: SGD
- unfolded protein binding Source: SGD
GO - Biological processi
- cell redox homeostasis Source: SGD
- cellular response to heat Source: CAFA
- cellular response to hydroperoxide Source: CAFA
- cellular response to oxidative stress Source: SGD
- chaperone-mediated protein folding Source: CAFA
- DNA damage checkpoint signaling Source: SGD
- DNA protection Source: SGD
- negative regulation of cell aging Source: SGD
- negative regulation of cell death Source: CAFA
- negative regulation of hydrogen peroxide-induced cell death Source: CAFA
- protein folding Source: SGD
- protein polymerization Source: CAFA
- protein stabilization Source: CAFA
- regulation of gluconeogenesis Source: SGD
- response to hydroperoxide Source: SGD
Keywordsi
Molecular function | Antioxidant, Oxidoreductase, Peroxidase |
Enzyme and pathway databases
Reactomei | R-SCE-5628897, TP53 Regulates Metabolic Genes R-SCE-6798695, Neutrophil degranulation |
Protein family/group databases
MoonProti | P34760 |
PeroxiBasei | 4465, Sce2CysPrx01 |
Names & Taxonomyi
Protein namesi | Recommended name: Peroxiredoxin TSA1Curated (EC:1.11.1.241 Publication)Short name: Prx Alternative name(s): Cytoplasmic thiol peroxidase 11 Publication Short name: cTPx 11 Publication Protector protein1 Publication Short name: PRP Thiol-specific antioxidant protein 11 Publication Thioredoxin peroxidase type Ia1 Publication Short name: TPx type Ia Thioredoxin-dependent peroxide reductase1 Publication Thioredoxin-dependent peroxiredoxin TSA1Curated |
Gene namesi | Ordered Locus Names:YML028WImported |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000004490, TSA1 |
VEuPathDBi | FungiDB:YML028W |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 48 | C → S: Exists mainly as monomer. Has no peroxiredoxin activity. Fails to protect glutamine synthetase against damage by DTT oxidation. 2 Publications | 1 | |
Mutagenesisi | 171 | C → S: Exists mainly as monomer. Has no peroxiredoxin activity. 2 Publications | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000135095 | 2 – 196 | Peroxiredoxin TSA1Add BLAST | 195 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Cross-linki | 14 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources | ||
Disulfide bondi | 48 | Interchain (with C-171); in linked form1 Publication | ||
Disulfide bondi | 48 | Interchain (with C-84 in SRX1); transient1 Publication | ||
Cross-linki | 89 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources | ||
Cross-linki | 132 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources | ||
Disulfide bondi | 171 | Interchain (with C-48); in linked form1 Publication | ||
Modified residuei | 174 | PhosphothreonineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
MaxQBi | P34760 |
PaxDbi | P34760 |
PRIDEi | P34760 |
TopDownProteomicsi | P34760 |
2D gel databases
SWISS-2DPAGEi | P34760 |
PTM databases
CarbonylDBi | P34760 |
iPTMneti | P34760 |
Interactioni
Subunit structurei
GO - Molecular functioni
- identical protein binding Source: CAFA
- unfolded protein binding Source: SGD
Protein-protein interaction databases
BioGRIDi | 35141, 625 interactors |
DIPi | DIP-1667N |
IntActi | P34760, 38 interactors |
MINTi | P34760 |
STRINGi | 4932.YML028W |
Miscellaneous databases
RNActi | P34760, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P34760 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 3 – 161 | ThioredoxinPROSITE-ProRule annotationAdd BLAST | 159 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 45 – 47 | Substrate bindingCombined sources1 Publication | 3 |
Sequence similaritiesi
Keywords - Domaini
Redox-active centerPhylogenomic databases
eggNOGi | KOG0852, Eukaryota |
GeneTreei | ENSGT00940000153430 |
HOGENOMi | CLU_042529_21_1_1 |
InParanoidi | P34760 |
OMAi | FWYPKDF |
Family and domain databases
InterProi | View protein in InterPro IPR000866, AhpC/TSA IPR024706, Peroxiredoxin_AhpC-typ IPR019479, Peroxiredoxin_C IPR036249, Thioredoxin-like_sf IPR013766, Thioredoxin_domain |
Pfami | View protein in Pfam PF10417, 1-cysPrx_C, 1 hit PF00578, AhpC-TSA, 1 hit |
PIRSFi | PIRSF000239, AHPC, 1 hit |
SUPFAMi | SSF52833, SSF52833, 1 hit |
PROSITEi | View protein in PROSITE PS51352, THIOREDOXIN_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MVAQVQKQAP TFKKTAVVDG VFDEVSLDKY KGKYVVLAFI PLAFTFVCPT
60 70 80 90 100
EIIAFSEAAK KFEEQGAQVL FASTDSEYSL LAWTNIPRKE GGLGPINIPL
110 120 130 140 150
LADTNHSLSR DYGVLIEEEG VALRGLFIID PKGVIRHITI NDLPVGRNVD
160 170 180 190
EALRLVEAFQ WTDKNGTVLP CNWTPGAATI KPTVEDSKEY FEAANK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L14640 Unassigned DNA Translation: AAA16374.1 Z46659 Genomic DNA Translation: CAA86627.1 BK006946 Genomic DNA Translation: DAA09870.1 |
PIRi | A47362 |
RefSeqi | NP_013684.1, NM_001182386.1 |
Genome annotation databases
EnsemblFungii | YML028W_mRNA; YML028W; YML028W |
GeneIDi | 854980 |
KEGGi | sce:YML028W |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L14640 Unassigned DNA Translation: AAA16374.1 Z46659 Genomic DNA Translation: CAA86627.1 BK006946 Genomic DNA Translation: DAA09870.1 |
PIRi | A47362 |
RefSeqi | NP_013684.1, NM_001182386.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3SBC | X-ray | 2.80 | A/B/C/D/E/F/G/H/I/J | 1-196 | [»] | |
SMRi | P34760 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 35141, 625 interactors |
DIPi | DIP-1667N |
IntActi | P34760, 38 interactors |
MINTi | P34760 |
STRINGi | 4932.YML028W |
Protein family/group databases
MoonProti | P34760 |
PeroxiBasei | 4465, Sce2CysPrx01 |
PTM databases
CarbonylDBi | P34760 |
iPTMneti | P34760 |
2D gel databases
SWISS-2DPAGEi | P34760 |
Proteomic databases
MaxQBi | P34760 |
PaxDbi | P34760 |
PRIDEi | P34760 |
TopDownProteomicsi | P34760 |
Genome annotation databases
EnsemblFungii | YML028W_mRNA; YML028W; YML028W |
GeneIDi | 854980 |
KEGGi | sce:YML028W |
Organism-specific databases
SGDi | S000004490, TSA1 |
VEuPathDBi | FungiDB:YML028W |
Phylogenomic databases
eggNOGi | KOG0852, Eukaryota |
GeneTreei | ENSGT00940000153430 |
HOGENOMi | CLU_042529_21_1_1 |
InParanoidi | P34760 |
OMAi | FWYPKDF |
Enzyme and pathway databases
Reactomei | R-SCE-5628897, TP53 Regulates Metabolic Genes R-SCE-6798695, Neutrophil degranulation |
Miscellaneous databases
PROi | PR:P34760 |
RNActi | P34760, protein |
Family and domain databases
InterProi | View protein in InterPro IPR000866, AhpC/TSA IPR024706, Peroxiredoxin_AhpC-typ IPR019479, Peroxiredoxin_C IPR036249, Thioredoxin-like_sf IPR013766, Thioredoxin_domain |
Pfami | View protein in Pfam PF10417, 1-cysPrx_C, 1 hit PF00578, AhpC-TSA, 1 hit |
PIRSFi | PIRSF000239, AHPC, 1 hit |
SUPFAMi | SSF52833, SSF52833, 1 hit |
PROSITEi | View protein in PROSITE PS51352, THIOREDOXIN_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | TSA1_YEAST | |
Accessioni | P34760Primary (citable) accession number: P34760 Secondary accession number(s): D6VZE6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1994 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 193 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome XIII
Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families