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Protein

Peroxiredoxin TSA1

Gene

TSA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Physiologically important antioxidant which constitutes an enzymatic defense against sulfur-containing radicals. Can provide protection against a thiol-containing oxidation system but not against an oxidation system without thiol.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei48 – 481Cysteine sulfenic acid (-SOH) intermediateBy similarity

GO - Molecular functioni

  • 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 oxidant detoxification Source: GOC
  • cellular response to oxidative stress Source: SGD
  • chaperone-mediated protein folding Source: SGD
  • DNA damage checkpoint Source: SGD
  • DNA protection Source: SGD
  • protein folding Source: SGD
  • replicative cell aging Source: SGD
  • response to hydroperoxide Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

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

Protein family/group databases

MoonProtiP34760.
PeroxiBasei4465. Sce2CysPrx01.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin TSA1 (EC:1.11.1.15)
Alternative name(s):
Cytoplasmic thiol peroxidase 1
Short name:
cTPx 1
PRP
Thiol-specific antioxidant protein 1
Thioredoxin peroxidase
Gene namesi
Name:TSA1
Synonyms:TPX1, TSA, ZRG14
Ordered Locus Names:YML028W
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

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytosol Source: SGD
  • polysome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 196195Peroxiredoxin TSA1PRO_0000135095Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi48 – 48Interchain (with C-171); alternate; in linked formBy similarity
Disulfide bondi48 – 48Interchain (with C-84 in SRX1); transient1 Publication
Disulfide bondi171 – 171Interchain (with C-48); in linked formBy similarity
Modified residuei174 – 1741PhosphothreonineCombined sources

Post-translational modificationi

The Cys-48-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-48 (probably Cys-SOH) rapidly reacts with Cys-171-SH of the other subunit to form an intermolecular disulfide. This disulfide is subsequently reduced by thioredoxin.
Forms a transient disulfide bond with SRX1 during the reduction of cysteine sulfinic acid (-SO2H).

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP34760.
PeptideAtlasiP34760.
TopDownProteomicsiP34760.

2D gel databases

SWISS-2DPAGEP34760.

PTM databases

iPTMnetiP34760.

Expressioni

Inductioni

By H2O2.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation.1 Publication

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi35141. 237 interactions.
DIPiDIP-1667N.
IntActiP34760. 29 interactions.
MINTiMINT-408012.

Structurei

Secondary structure

1
196
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 185Combined sources
Beta strandi21 – 255Combined sources
Helixi27 – 304Combined sources
Beta strandi33 – 397Combined sources
Helixi47 – 6418Combined sources
Beta strandi67 – 759Combined sources
Helixi77 – 848Combined sources
Helixi88 – 903Combined sources
Beta strandi100 – 1023Combined sources
Helixi107 – 1126Combined sources
Turni117 – 1193Combined sources
Beta strandi124 – 1296Combined sources
Beta strandi133 – 1419Combined sources
Helixi149 – 16517Combined sources
Turni184 – 1863Combined sources
Helixi187 – 1948Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SBCX-ray2.80A/B/C/D/E/F/G/H/I/J1-196[»]
ProteinModelPortaliP34760.
SMRiP34760. Positions 1-196.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 161159ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
InParanoidiP34760.
KOiK03386.
OMAiWVETSPR.
OrthoDBiEOG7B8SG7.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

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.

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.
PIRiA47362.
RefSeqiNP_013684.1. NM_001182386.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SBCX-ray2.80A/B/C/D/E/F/G/H/I/J1-196[»]
ProteinModelPortaliP34760.
SMRiP34760. Positions 1-196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35141. 237 interactions.
DIPiDIP-1667N.
IntActiP34760. 29 interactions.
MINTiMINT-408012.

Protein family/group databases

MoonProtiP34760.
PeroxiBasei4465. Sce2CysPrx01.

PTM databases

iPTMnetiP34760.

2D gel databases

SWISS-2DPAGEP34760.

Proteomic databases

MaxQBiP34760.
PeptideAtlasiP34760.
TopDownProteomicsiP34760.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML028W; YML028W; YML028W.
GeneIDi854980.
KEGGisce:YML028W.

Organism-specific databases

EuPathDBiFungiDB:YML028W.
SGDiS000004490. TSA1.

Phylogenomic databases

GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
InParanoidiP34760.
KOiK03386.
OMAiWVETSPR.
OrthoDBiEOG7B8SG7.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi978097.
PROiP34760.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae."
    Chae H.Z., Kim I.-H., Kim K., Rhee S.G.
    J. Biol. Chem. 268:16815-16821(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE, PARTIAL PROTEIN SEQUENCE OF 2-13; 62-66; 79-87; 90-94; 137-143; 148-153; 155-161 AND 192-196, CLEAVAGE OF INITIATOR METHIONINE.
    Strain: JD7-7C.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae."
    Park S.G., Cha M.-K., Jeong W., Kim I.-H.
    J. Biol. Chem. 275:5723-5732(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin."
    Biteau B., Labarre J., Toledano M.B.
    Nature 425:980-984(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND WITH SRX1.
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Crystal structure of Saccharomyces cerevisiae TSA1C47S mutant protein."
    Tairum C.A. Jr., Horta B.B., Zara F.J., Netto L.E.S., Oliveira M.A.
    Submitted (JUN-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF MUTANT SER-48.

Entry informationi

Entry nameiTSA1_YEAST
AccessioniPrimary (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: May 11, 2016
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 378000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.