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    TSA2 thioredoxin peroxidase TSA2 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852064, updated on 9-Dec-2024

    Summary

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    Official Symbol
    TSA2
    Official Full Name
    thioredoxin peroxidase TSA2
    Primary source
    SGD:S000002861
    Locus tag
    YDR453C
    See related
    AllianceGenome:SGD:S000002861; FungiDB:YDR453C; VEuPathDB:YDR453C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables thioredoxin peroxidase activity. Involved in several processes, including cell redox homeostasis; cellular response to heat; and protein folding. Located in cytoplasm. Human ortholog(s) of this gene implicated in autosomal recessive spinocerebellar ataxia 32 and methylmalonic aciduria and homocystinuria type cblC. Orthologous to several human genes including PRDX1 (peroxiredoxin 1); PRDX2 (peroxiredoxin 2); and PRDX4 (peroxiredoxin 4). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See TSA2 in Genome Data Viewer
    Location:
    chromosome: IV
    Exon count:
    1
    Sequence:
    Chromosome: IV; NC_001136.10 (1365072..1365662, complement)

    Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene Yhp1p Neighboring gene endopolyphosphatase Neighboring gene guanylate kinase Neighboring gene bifunctional K:H/Na:H antiporter NHX1

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001136.10

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Structure of TSA2 reveals novel features of the active-site loop of peroxiredoxins. Nielsen MH, et al. Acta Crystallogr D Struct Biol, 2016 Jan. PMID 26894543
    2. Site-specific mutagenesis of yeast 2-Cys peroxiredoxin improves heat or oxidative stress tolerance by enhancing its chaperone or peroxidase function. Hong SH, et al. Protoplasma, 2017 Jan. PMID 26843371
    3. Catalytic Thr or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms. Tairum CA, et al. Sci Rep, 2016 Sep 15. PMID 27629822, Free PMC Article
    4. Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function. Jang HH, et al. Cell, 2004 May 28. PMID 15163410
    5. Cytosolic thioredoxin peroxidase I and II are important defenses of yeast against organic hydroperoxide insult: catalases and peroxiredoxins cooperate in the decomposition of H2O2 by yeast. Munhoz DC, et al. J Biol Chem, 2004 Aug 20. PMID 15210711

    See all (74) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. a novel function for Tsa2p as a negative regulator of Aft1p-driven transcription, which is induced in V-ATPase mutants to limit transcription of the iron regulon.
      Title: Loss of vacuolar H+-ATPase (V-ATPase) activity in yeast generates an iron deprivation signal that is moderated by induction of the peroxiredoxin TSA2.
    2. show that the yeast Tsa1/Tsa2 peroxiredoxins colocalize to ribosomes and function to protect the Sup35 translation termination factor against oxidative stress-induced formation of its heritable [PSI(+)] prion conformation.
      Title: Ribosome-associated peroxiredoxins suppress oxidative stress-induced de novo formation of the [PSI+] prion in yeast.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables peroxidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables peroxiredoxin activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables peroxiredoxin activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables thioredoxin peroxidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables thioredoxin peroxidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables thioredoxin peroxidase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables thioredoxin-dependent peroxiredoxin activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in cell redox homeostasis IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in cell redox homeostasis IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in cell redox homeostasis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in cellular oxidant detoxification IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in cellular response to heat IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in cellular response to oxidative stress IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in cellular response to oxidative stress IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in hydrogen peroxide catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in response to oxidative stress IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in response to oxidative stress IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    thioredoxin peroxidase TSA2
    NP_010741.1
    • Stress inducible cytoplasmic thioredoxin peroxidase; cooperates with Tsa1p in the removal of reactive oxygen, nitrogen and sulfur species using thioredoxin as hydrogen donor; deletion enhances the mutator phenotype of tsa1 mutants; protein abundance increases in response to DNA replication stress; TSA2 has a paralog, TSA1, that arose from the whole genome duplication

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_001136.10 Reference assembly

      Range
      1365072..1365662 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001180761.1 → NP_010741.1  TPA: thioredoxin peroxidase TSA2 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_010741.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VT78, Q04120
      UniProtKB/TrEMBL
      A6ZZ44, B5VGY3, C7GKP5, C8Z611, G2WBI4, N1P7J0
      Conserved Domains (1) summary
      cd03015
      Location:5 → 176
      PRX_Typ2cys; Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q04120.3

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