U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

ATX1 copper metallochaperone ATX1 [ Saccharomyces cerevisiae S288C ]

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

Summary

Go to the top of the page Help
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]
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
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

Go to the top of the page Help
Genomic Sequence:
NC_001146.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

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

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

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

Go to the top of the page Help
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)

Go to the top of the page Help

NEW Try the new Transcript table

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

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Other Literature Sources
Molecular Biology Databases
Research Materials
Tools