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    ATX1 copper metallochaperone ATX1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855462, updated on 2-Nov-2024

    Summary

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    Official Symbol
    ATX1
    Official Full Name
    copper metallochaperone ATX1
    Primary source
    SGD:S000005203
    Locus tag
    YNL259C
    See related
    AllianceGenome:SGD:S000005203; FungiDB:YNL259C; VEuPathDB:YNL259C
    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 copper chaperone activity. Involved in cellular response to oxidative stress; copper ion transport; and intracellular iron ion homeostasis. Located in cytosol. Orthologous to human ATOX1 (antioxidant 1 copper chaperone). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See ATX1 in Genome Data Viewer
    Location:
    chromosome: XIV
    Exon count:
    1
    Sequence:
    Chromosome: XIV; NC_001146.8 (157644..157865, complement)

    Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene origin recognition complex subunit 5 Neighboring gene ribosome biosynthesis protein LTO1 Neighboring gene Dsl1p Neighboring gene Sip3p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001146.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Computer simulation of the interaction of Cu(I) with cys residues at the binding site of the yeast metallochaperone Cu(I)-Atx1. Dalosto SD. J Phys Chem B, 2007 Mar 22. PMID 17388422
    2. The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity. Lin SJ, et al. Proc Natl Acad Sci U S A, 1995 Apr 25. PMID 7731983, Free PMC Article
    3. Intracellular pathways of copper trafficking in yeast and humans. Culotta VC, et al. Adv Exp Med Biol, 1999. PMID 10079832
    4. Structure-function analyses of the ATX1 metallochaperone. Portnoy ME, et al. J Biol Chem, 1999 May 21. PMID 10329707
    5. Solution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1. Arnesano F, et al. Biochemistry, 2001 Feb 13. PMID 11327811

    See all (58) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. different effects of ATX1 unfolding on Cu(I) affinity
      Title: The influence of protein folding on the copper affinities of trafficking and target sites.
    2. evidence of a dual role for the Ccc2 N-terminus, namely to receive copper from Atx1 and to convey copper to another domain of Ccc2, thereby activating the ATPase
      Title: Dissecting the role of the N-terminal metal-binding domains in activating the yeast copper ATPase in vivo.
    3. results suggest that in vivo the high GSH concentration favors Atx1 dimerization and that Cu (2) (I) (GS(-))(2)(Atx1)(2) is the major conformation of Atx1 in the cytosol
      Title: Interplay between glutathione, Atx1 and copper. 1. Copper(I) glutathionate induced dimerization of Atx1.
    4. structurally characterized the adduct between the copper chaperone Atx1 and the first copper(I)-binding domain of the Ccc2 ATPase
      Title: The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction.
    5. The possible role of electrostatic potential surfaces in the docking of Ccc2 with these Atx1-homologues is discussed
      Title: Cd2+- or Hg2+-binding proteins can replace the Cu+-chaperone Atx1 in delivering Cu+ to the secretory pathway 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 copper chaperone activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables copper chaperone activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in cellular response to oxidative stress IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in copper ion transport IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in copper ion transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in copper ion transport IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in intracellular iron ion homeostasis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    copper metallochaperone ATX1
    NP_014140.1
    • Cytosolic copper metallochaperone; transports copper to the secretory vesicle copper transporter Ccc2p for eventual insertion into Fet3p, which is a multicopper oxidase required for high-affinity iron uptake; human homolog ATOX1 can complement yeast atx1 mutant; overexpression of human ATOX1 suppresses lysine auxotrophy of the yeast sod1 null mutant, as does overexpression of yeast ATX1

    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_001146.8 Reference assembly

      Range
      157644..157865 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183097.1 → NP_014140.1  TPA: copper metallochaperone ATX1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014140.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W0T4, E9P8W0, P38636
      UniProtKB/TrEMBL
      A6ZRI4, B3LPA2, C7GPA2, C8ZFX8, G2WLK7, N1NXZ5
      Conserved Domains (1) summary
      cd00371
      Location:13 → 68
      HMA; Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P38636.1

    Gene LinkOut

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