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 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

Sites

Feature key	Position(s)	DescriptionActions	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
Inferred from mutant phenotypeⁱ
- 15163410
kinase regulator activity
Source: SGD
Inferred from mutant phenotypeⁱ
- 27634403
peroxiredoxin activity
Source: SGD
Inferred from direct assayⁱ
- 17210445
ribosome binding
Source: SGD
Inferred from direct assayⁱ
- 18271751
thioredoxin peroxidase activity
Source: SGD
Inferred from direct assayⁱ
- 7961686
- 9799566
unfolded protein binding
Source: SGD
Inferred from direct assayⁱ
- 15163410

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell redox homeostasis
Source: SGD
Inferred from direct assayⁱ
- 8344960
cellular response to heat
Source: CAFA
Inferred from mutant phenotypeⁱ
- 15163410
cellular response to hydroperoxide
Source: CAFA
Inferred from mutant phenotypeⁱ
- 15163410
cellular response to oxidative stress
Source: SGD
Inferred from direct assayⁱ
- 8344960
chaperone-mediated protein folding
Source: CAFA
Inferred from mutant phenotypeⁱ
- 15163410
DNA damage checkpoint
Source: SGD
Inferred from genetic interactionⁱ
- 19851444
DNA protection
Source: SGD
Inferred from mutant phenotypeⁱ
- 19543365
hydrogen peroxide catabolic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
negative regulation of cell aging
Source: SGD
Inferred from mutant phenotypeⁱ
- 27264606
negative regulation of cell death
Source: CAFA
Inferred from mutant phenotypeⁱ
- 15163410
negative regulation of hydrogen peroxide-induced cell death
Source: CAFA
Inferred from mutant phenotypeⁱ
- 15163410
protein folding
Source: SGD
Inferred from direct assayⁱ
- 15163410
protein polymerization
Source: CAFA
Inferred from mutant phenotypeⁱ
- 15163410
protein stabilization
Source: CAFA
Inferred from mutant phenotypeⁱ
- 15163410
regulation of gluconeogenesis
Source: SGD
Inferred from mutant phenotypeⁱ
- 27634403
replicative cell aging
Source: SGD
Inferred from mutant phenotypeⁱ
- 20729566
response to hydroperoxide
Source: SGD
Inferred from mutant phenotypeⁱ
- 15210711
response to oxidative stress
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Antioxidant, Oxidoreductase, Peroxidase

Molecular function

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCycⁱ	YEAST:YML028W-MONOMER
Reactomeⁱ	R-SCE-3299685 Detoxification of Reactive Oxygen Species 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:1.11.1.151 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
Organismⁱ	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifierⁱ	559292 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae
Proteomesⁱ	UP000002311 Componentⁱ: Chromosome XIII

Organism-specific databases

Saccharomyces Genome Database More...SGDⁱ	S000004490 TSA1

SGDⁱ

S000004490 TSA1

Keywords - Cellular componentⁱ

Cytoplasm

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	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

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

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P34760
PaxDbⁱ	P34760
PRIDEⁱ	P34760
TopDownProteomicsⁱ	P34760

2D gel databases

SWISS-2DPAGEⁱ	P34760

SWISS-2DPAGEⁱ

P34760

PTM databases

CarbonylDBⁱ	P34760
iPTMnetⁱ	P34760

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
Inferred from mutant phenotypeⁱ
- 15163410
unfolded protein binding
Source: SGD
Inferred from direct assayⁱ
- 15163410

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	35141, 590 interactors
Database of interacting proteins More...DIPⁱ	DIP-1667N
IntActⁱ	P34760, 38 interactors
Molecular INTeraction database More...MINTⁱ	P34760
STRINGⁱ	4932.YML028W

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	14 – 18	Combined sources	5
Beta strandⁱ	21 – 25	Combined sources	5
Helixⁱ	27 – 30	Combined sources	4
Beta strandⁱ	33 – 39	Combined sources	7
Helixⁱ	47 – 64	Combined sources	18
Beta strandⁱ	67 – 75	Combined sources	9
Helixⁱ	77 – 84	Combined sources	8
Helixⁱ	88 – 90	Combined sources	3
Beta strandⁱ	100 – 102	Combined sources	3
Helixⁱ	107 – 112	Combined sources	6
Turnⁱ	117 – 119	Combined sources	3
Beta strandⁱ	124 – 129	Combined sources	6
Beta strandⁱ	133 – 141	Combined sources	9
Helixⁱ	149 – 165	Combined sources	17
Turnⁱ	184 – 186	Combined sources	3
Helixⁱ	187 – 194	Combined sources	8

Show more details

3D structure databases

ProteinModelPortalⁱ	P34760
SMRⁱ	P34760
ModBaseⁱ	Search...
MobiDBⁱ	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

Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.Curated

Keywords - Domainⁱ

Redox-active center

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000004653
HOGENOMⁱ	HOG000022343
InParanoidⁱ	P34760
KEGG Orthology (KO) More...KOⁱ	K03386
OMAⁱ	WYPKDFT
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C53IH

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
Pfam protein domain database More...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

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P34760-1 [UniParc]FASTA Add 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
PIRⁱ	A47362
NCBI Reference Sequences More...RefSeqⁱ	NP_013684.1, NM_001182386.1

Genome annotation databases

EnsemblFungiⁱ	YML028W; YML028W; YML028W
GeneIDⁱ	854980
KEGGⁱ	sce:YML028W

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P34760	Peroxiredoxin TSA1		YEAS1		196	UniRef100_P34760
K7_Tsa1p		YEASK		196
Tsa1p		YEASA		196
Tsa1p		YEAS8		196
TSA1p Thioredoxin peroxidase		Saccharomyces sp. 'boulardii'		196
+6

Protein	Similar proteins		Species	Score	Length	Source
P34760	Peroxiredoxin TSA1		YEAS1		196	UniRef90_P34760
K7_Tsa1p		YEASK		196
Tsa1p		YEASA		196
Tsa1p		YEAS8		196
TSA1p Thioredoxin peroxidase		Saccharomyces sp. 'boulardii'		196
+18

Protein	Similar proteins		Species	Score	Length	Source
P34760	Peroxiredoxin TSA1-B		CANAL		196	UniRef50_P34760
Peroxiredoxin TSA2	)	YEAST		196
Thioredoxin peroxidase		ECHGR		193
Thioredoxin peroxidase		TRYBR		199
Peroxiredoxin TSA1		YEAS1		196
+536

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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	[»]
ProteinModelPortalⁱ	P34760
SMRⁱ	P34760
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	35141, 590 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

SWISS-2DPAGEⁱ

P34760

Proteomic databases

MaxQBⁱ	P34760
PaxDbⁱ	P34760
PRIDEⁱ	P34760
TopDownProteomicsⁱ	P34760

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblFungiⁱ	YML028W; YML028W; YML028W
GeneIDⁱ	854980
KEGGⁱ	sce:YML028W

Organism-specific databases

SGDⁱ	S000004490 TSA1

Phylogenomic databases

GeneTreeⁱ	ENSGT00390000004653
HOGENOMⁱ	HOG000022343
InParanoidⁱ	P34760
KOⁱ	K03386
OMAⁱ	WYPKDFT
OrthoDBⁱ	EOG092C53IH

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P34760

PROⁱ

PR:P34760

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
ProtoNetⁱ	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:	November 7, 2018
	This is version 174 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Yeast chromosome XIII
Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

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UniProtKB - P34760 (TSA1_YEAST)

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Peroxiredoxin TSA1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Other locations

Cytosol

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ