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    GRX7 glutathione-disulfide reductase GRX7 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852302, updated on 9-Dec-2024

    Summary

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    Official Symbol
    GRX7
    Official Full Name
    glutathione-disulfide reductase GRX7
    Primary source
    SGD:S000000218
    Locus tag
    YBR014C
    See related
    AllianceGenome:SGD:S000000218; FungiDB:YBR014C; VEuPathDB:YBR014C
    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 glutathione-disulfide reductase (NADPH) activity. Involved in cellular response to oxidative stress. Located in Golgi lumen; cis-Golgi network; and membrane. [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See GRX7 in Genome Data Viewer
    Location:
    chromosome: II
    Exon count:
    1
    Sequence:
    Chromosome: II; NC_001134.8 (266725..267336, complement)

    Chromosome II - NC_001134.8Genomic Context describing neighboring genes Neighboring gene uncharacterized protein Neighboring gene tRNA-Thr Neighboring gene alpha-1,2-mannosyltransferase MNN2 Neighboring gene cysteine-rich palmitoylated domain-containing protein CPP1

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001134.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Expression, characterization and regulation of a Saccharomyces cerevisiae monothiol glutaredoxin (Grx6) gene in Schizosaccharomyces pombe. Lee JH, et al. Mol Cells, 2007 Dec 31. PMID 18182845
    2. Saccharomyces cerevisiae Grx6 and Grx7 are monothiol glutaredoxins associated with the early secretory pathway. Izquierdo A, et al. Eukaryot Cell, 2008 Aug. PMID 18503006, Free PMC Article
    3. Two novel monothiol glutaredoxins from Saccharomyces cerevisiae provide further insight into iron-sulfur cluster binding, oligomerization, and enzymatic activity of glutaredoxins. Mesecke N, et al. Biochemistry, 2008 Feb 5. PMID 18171082
    4. Biochemical characterization of dithiol glutaredoxin 8 from Saccharomyces cerevisiae: the catalytic redox mechanism redux. Eckers E, et al. Biochemistry, 2009 Feb 17. PMID 19166312
    5. A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance. Mesecke N, et al. Mol Biol Cell, 2008 Jun. PMID 18400945, Free PMC Article

    See all (38) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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 2 iron, 2 sulfur cluster binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables glutathione disulfide oxidoreductase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables glutathione-disulfide reductase (NADPH) activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in cellular oxidant detoxification IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in cellular response to oxidative stress IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in cellular response to oxidative stress IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in Golgi apparatus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in Golgi lumen IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in Golgi lumen IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in cis-Golgi network IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cis-Golgi network IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in fungal-type vacuole HDA PubMed 
    is_active_in fungal-type vacuole IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    glutathione-disulfide reductase GRX7
    NP_009570.1
    • Cis-golgi localized monothiol glutaredoxin; more similar in activity to dithiol than other monothiol glutaredoxins; involved in the oxidative stress response; does not bind metal ions; GRX7 has a paralog, GRX6, 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_001134.8 Reference assembly

      Range
      266725..267336 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001178362.1 → NP_009570.1  TPA: glutathione-disulfide reductase GRX7 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_009570.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VQ16, P38068, Q1P9U2
      UniProtKB/TrEMBL
      A6ZKW0, C8Z408, G2W921, N1PAR0
      Conserved Domains (1) summary
      cd03419
      Location:99 → 181
      GRX_GRXh_1_2_like; Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P38068.1

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