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Protein

Peroxiredoxin TSA1

Gene

TSA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 Publications

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.1 Publication
Present with 378000 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=3 µM for H2O21 Publication
  2. KM=4 µM for cumene hydroperoxide1 Publication
  3. KM=10 µM for tert-butyl hydroperoxide1 Publication
  4. KM=2 µM for TRX11 Publication
  5. KM=3 µM for TRX21 Publication
  6. KM=12 µM for H2O21 Publication
  7. KM=17.1 µM for cumene hydroperoxide1 Publication
  8. KM=7.9 µM for tert-butyl hydroperoxide1 Publication
  1. Vmax=4.8 µmol/min/mg enzyme for H2O21 Publication
  2. Vmax=2.2 µmol/min/mg enzyme for cumene hydroperoxide1 Publication
  3. Vmax=2.4 µmol/min/mg enzyme for tert-butyl hydroperoxide1 Publication
  4. Vmax=5.5 µmol/min/mg enzyme for TRX11 Publication
  5. Vmax=5.5 µmol/min/mg enzyme for TRX21 Publication
  6. Vmax=0.66 µM/sec/mg enzyme for H2O21 Publication
  7. Vmax=0.56 µM/sec/mg enzyme for cumene hydroperoxide1 Publication
  8. Vmax=0.61 µM/sec/mg enzyme for tert-butyl hydroperoxide1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei45Important for catalytic activity, helps activating the peroxidatic cysteine through H-bonding1
Active sitei48Cysteine sulfenic acid (-SOH) intermediate1 Publication1
Binding sitei124SubstrateCombined sources1 Publication1

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 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
  • replicative cell aging Source: SGD
  • response to hydroperoxide Source: SGD

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciYEAST:YML028W-MONOMER
ReactomeiR-SCE-3299685 Detoxification of Reactive Oxygen Species
R-SCE-5628897 TP53 Regulates Metabolic Genes
R-SCE-6798695 Neutrophil degranulation

Protein family/group databases

MoonProtiP34760
PeroxiBasei4465 Sce2CysPrx01

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin TSA1Curated (EC:1.11.1.151 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
Gene namesi
Name:TSA11 Publication
Synonyms:TPX1, TSA, ZRG14
Ordered Locus Names:YML028WImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML028W
SGDiS000004490 TSA1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi48C → S: Exists mainly as monomer. Has no peroxiredoxin activity. Fails to protect glutamine synthetase against damage by DTT oxidation. 2 Publications1
Mutagenesisi171C → S: Exists mainly as monomer. Has no peroxiredoxin activity. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001350952 – 196Peroxiredoxin TSA1Add BLAST195

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Disulfide bondi48Interchain (with C-171); in linked form1 Publication
Disulfide bondi48Interchain (with C-84 in SRX1); transient1 Publication
Cross-linki89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki132Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Disulfide bondi171Interchain (with C-48); in linked form1 Publication
Modified residuei174PhosphothreonineCombined sources1

Post-translational modificationi

The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRX1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner.1 Publication

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP34760
PaxDbiP34760
PRIDEiP34760
TopDownProteomicsiP34760

2D gel databases

SWISS-2DPAGEP34760

PTM databases

CarbonylDBiP34760
iPTMnetiP34760

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation (PubMed:8041739). Interacts with YAP1 via transient disulfide linkages (PubMed:19106090).2 Publications

GO - Molecular functioni

  • identical protein binding Source: CAFA
  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi35141, 564 interactors
DIPiDIP-1667N
IntActiP34760, 38 interactors
MINTiP34760
STRINGi4932.YML028W

Structurei

Secondary structure

1196
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 18Combined sources5
Beta strandi21 – 25Combined sources5
Helixi27 – 30Combined sources4
Beta strandi33 – 39Combined sources7
Helixi47 – 64Combined sources18
Beta strandi67 – 75Combined sources9
Helixi77 – 84Combined sources8
Helixi88 – 90Combined sources3
Beta strandi100 – 102Combined sources3
Helixi107 – 112Combined sources6
Turni117 – 119Combined sources3
Beta strandi124 – 129Combined sources6
Beta strandi133 – 141Combined sources9
Helixi149 – 165Combined sources17
Turni184 – 186Combined sources3
Helixi187 – 194Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SBCX-ray2.80A/B/C/D/E/F/G/H/I/J1-196[»]
ProteinModelPortaliP34760
SMRiP34760
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 161ThioredoxinPROSITE-ProRule annotationAdd BLAST159

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni45 – 47Substrate bindingCombined sources1 Publication3

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

GeneTreeiENSGT00390000004653
HOGENOMiHOG000022343
InParanoidiP34760
KOiK03386
OMAiTAVHNGE
OrthoDBiEOG092C53IH

Family and domain databases

InterProiView protein in InterPro
IPR000866 AhpC/TSA
IPR024706 Peroxiredoxin_AhpC-typ
IPR019479 Peroxiredoxin_C
IPR036249 Thioredoxin-like_sf
IPR013766 Thioredoxin_domain
PfamiView protein in Pfam
PF10417 1-cysPrx_C, 1 hit
PF00578 AhpC-TSA, 1 hit
PIRSFiPIRSF000239 AHPC, 1 hit
SUPFAMiSSF52833 SSF52833, 1 hit
PROSITEiView protein in PROSITE
PS51352 THIOREDOXIN_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P34760-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:196
Mass (Da):21,590
Last modified:January 23, 2007 - v3
Checksum:i9ACF40E410F2C04A
GO

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
PIRiA47362
RefSeqiNP_013684.1, NM_001182386.1

Genome annotation databases

EnsemblFungiiYML028W; YML028W; YML028W
GeneIDi854980
KEGGisce:YML028W

Similar proteinsi

Entry informationi

Entry nameiTSA1_YEAST
AccessioniPrimary (citable) accession number: P34760
Secondary accession number(s): D6VZE6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 170 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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