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    Atox1 Antioxidant 1 copper chaperone [ Drosophila melanogaster (fruit fly) ]

    Gene ID: 326216, updated on 9-Dec-2024

    Summary

    Official Symbol
    Atox1provided by FlyBase
    Official Full Name
    Antioxidant 1 copper chaperoneprovided by FlyBase
    Primary source
    FLYBASE:FBgn0052446
    Locus tag
    Dmel_CG32446
    See related
    AllianceGenome:FB:FBgn0052446
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Drosophila melanogaster
    Lineage
    Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora
    Also known as
    CG12562; CG32446; DmAtox1; Dmel\CG32446
    Summary
    Predicted to enable copper chaperone activity. Involved in copper ion homeostasis. Predicted to be active in cytosol. Is expressed in embryonic/larval crystal cell; organism; and procrystal cell. Orthologous to human ATOX1 (antioxidant 1 copper chaperone). [provided by Alliance of Genome Resources, Dec 2024]
    Orthologs
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    Genomic context

    See Atox1 in Genome Data Viewer
    Location:
    78E2-78E2; 3-47 cM
    Exon count:
    3
    Annotation release Status Assembly Chr Location
    Release 6.54 current Release 6 plus ISO1 MT (GCF_000001215.4) 3L NT_037436.4 (21640995..21642599)
    Release 5.57 previous assembly Release 5 (GCF_000001215.2) 3L NT_037436.3 (21634095..21635699)

    Chromosome 3L - NT_037436.4Genomic Context describing neighboring genes Neighboring gene antisense RNA:CR45955 Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene long non-coding RNA:CR45956 Neighboring gene uncharacterized protein

    Genomic regions, transcripts, and products

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Gene Ontology Provided by FlyBase

    Function Evidence Code Pubs
    enables copper chaperone activity IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    Process Evidence Code Pubs
    involved_in copper ion homeostasis IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    involved_in copper ion transport IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    Component Evidence Code Pubs
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
     

    General protein information

    Preferred Names
    antioxidant 1 copper chaperone
    Names
    Atox1-PA
    Atox1-PB
    CG32446-PA
    CG32446-PB

    NCBI Reference Sequences (RefSeq)

    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. NT_037436.4 Reference assembly

      Range
      21640995..21642599
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_168932.2NP_730672.1  antioxidant 1 copper chaperone, isoform A [Drosophila melanogaster]

      See identical proteins and their annotated locations for NP_730672.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      Q95RR1
      Related
      FBpp0078080
      Conserved Domains (1) summary
      cd00371
      Location:562
      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 ...
    2. NM_001275255.1NP_001262184.1  antioxidant 1 copper chaperone, isoform B [Drosophila melanogaster]

      See identical proteins and their annotated locations for NP_001262184.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      M9PD88
      Conserved Domains (1) summary
      cd00371
      Location:562
      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 ...