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Protein

Peroxiredoxin TSA2

Gene

TSA2

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

Reduces peroxides. May play an important role in eliminating peroxides generated during metabolism (By similarity).By similarity

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
  • thioredoxin peroxidase activity Source: SGD

GO - Biological processi

  • cell redox homeostasis Source: SGD
  • cellular oxidant detoxification Source: GOC
  • cellular response to oxidative stress Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciYEAST:YDR453C-MONOMER.
ReactomeiR-SCE-3299685. Detoxification of Reactive Oxygen Species.
R-SCE-5628897. TP53 Regulates Metabolic Genes.

Protein family/group databases

MoonProtiQ04120.
PeroxiBasei4467. Sce2CysPrx02.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin TSA2 (EC:1.11.1.15)
Alternative name(s):
Cytoplasmic thiol peroxidase 2
Short name:
cTPx 2
Thiol-specific antioxidant protein 2
Thioredoxin peroxidase 2
Gene namesi
Name:TSA2
Ordered Locus Names:YDR453C
ORF Names:D9461.38
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR453C.
SGDiS000002861. TSA2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi48 – 481C → S: No activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 196196Peroxiredoxin TSA2PRO_0000135096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi48 – 48Interchain (with C-171); in linked formBy similarity
Disulfide bondi171 – 171Interchain (with C-48); in linked formBy similarity

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.

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ04120.
PeptideAtlasiQ04120.
PRIDEiQ04120.
TopDownProteomicsiQ04120.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation.By similarity

Protein-protein interaction databases

BioGridi32508. 46 interactions.
DIPiDIP-4317N.
IntActiQ04120. 5 interactions.
MINTiMINT-535451.

Structurei

Secondary structure

1
196
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 186Combined sources
Beta strandi21 – 277Combined sources
Helixi28 – 303Combined sources
Beta strandi33 – 397Combined sources
Beta strandi45 – 473Combined sources
Helixi48 – 5710Combined sources
Helixi59 – 646Combined sources
Beta strandi67 – 759Combined sources
Helixi77 – 859Combined sources
Turni88 – 914Combined sources
Beta strandi100 – 1023Combined sources
Helixi107 – 1115Combined sources
Turni117 – 1193Combined sources
Beta strandi124 – 1296Combined sources
Beta strandi133 – 1419Combined sources
Helixi149 – 16517Combined sources
Turni184 – 1863Combined sources
Helixi187 – 1937Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5DVBX-ray2.20A/B/C/D/E/F/G/H/I/J1-196[»]
5EPTX-ray5.00A/B/C/D/E/F/G/H/I/J1-196[»]
ProteinModelPortaliQ04120.
SMRiQ04120. Positions 1-195.
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.
InParanoidiQ04120.
KOiK03386.
OMAiDINMNDY.
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.

Q04120-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAEVQKQAP PFKKTAVVDG IFEEISLEKY KGKYVVLAFV PLAFSFVCPT
60 70 80 90 100
EIVAFSDAAK KFEDQGAQVL FASTDSEYSL LAWTNLPRKD GGLGPVKVPL
110 120 130 140 150
LADKNHSLSR DYGVLIEKEG IALRGLFIID PKGIIRHITI NDLSVGRNVN
160 170 180 190
EALRLVEGFQ WTDKNGTVLP CNWTPGAATI KPDVKDSKEY FKNANN
Length:196
Mass (Da):21,615
Last modified:January 23, 2007 - v3
Checksum:i43CC57C92081D745
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64886.1.
BK006938 Genomic DNA. Translation: DAA12288.1.
PIRiS69732.
RefSeqiNP_010741.1. NM_001180761.1.

Genome annotation databases

EnsemblFungiiYDR453C; YDR453C; YDR453C.
GeneIDi852064.
KEGGisce:YDR453C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64886.1.
BK006938 Genomic DNA. Translation: DAA12288.1.
PIRiS69732.
RefSeqiNP_010741.1. NM_001180761.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5DVBX-ray2.20A/B/C/D/E/F/G/H/I/J1-196[»]
5EPTX-ray5.00A/B/C/D/E/F/G/H/I/J1-196[»]
ProteinModelPortaliQ04120.
SMRiQ04120. Positions 1-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32508. 46 interactions.
DIPiDIP-4317N.
IntActiQ04120. 5 interactions.
MINTiMINT-535451.

Protein family/group databases

MoonProtiQ04120.
PeroxiBasei4467. Sce2CysPrx02.

Proteomic databases

MaxQBiQ04120.
PeptideAtlasiQ04120.
PRIDEiQ04120.
TopDownProteomicsiQ04120.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR453C; YDR453C; YDR453C.
GeneIDi852064.
KEGGisce:YDR453C.

Organism-specific databases

EuPathDBiFungiDB:YDR453C.
SGDiS000002861. TSA2.

Phylogenomic databases

GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
InParanoidiQ04120.
KOiK03386.
OMAiDINMNDY.
OrthoDBiEOG7B8SG7.

Enzyme and pathway databases

BioCyciYEAST:YDR453C-MONOMER.
ReactomeiR-SCE-3299685. Detoxification of Reactive Oxygen Species.
R-SCE-5628897. TP53 Regulates Metabolic Genes.

Miscellaneous databases

PROiQ04120.

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. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "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, MUTAGENESIS OF CYS-48.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTSA2_YEAST
AccessioniPrimary (citable) accession number: Q04120
Secondary accession number(s): D6VT78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 133 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 4820 molecules/cell in log phase SD medium.1 Publication

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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.