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    Jon65Ai Jonah 65Ai [ Drosophila melanogaster (fruit fly) ]

    Gene ID: 38685, updated on 9-Dec-2024

    Summary

    Official Symbol
    Jon65Aiprovided by FlyBase
    Official Full Name
    Jonah 65Aiprovided by FlyBase
    Primary source
    FLYBASE:FBgn0035667
    Locus tag
    Dmel_CG10475
    See related
    AllianceGenome:FB:FBgn0035667
    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
    CG10475; CT29408; Dmel\CG10475; Jon65; Jon65A; SP145
    Summary
    Enables serine hydrolase activity. Predicted to be involved in innate immune response and proteolysis. Predicted to be active in extracellular space. [provided by Alliance of Genome Resources, Dec 2024]
    Orthologs
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    Genomic context

    See Jon65Ai in Genome Data Viewer
    Location:
    65A4-65A4; 3-16 cM
    Exon count:
    1
    Annotation release Status Assembly Chr Location
    Release 6.54 current Release 6 plus ISO1 MT (GCF_000001215.4) 3L NT_037436.4 (6053493..6054443, complement)
    Release 5.57 previous assembly Release 5 (GCF_000001215.2) 3L NT_037436.3 (6046593..6047543, complement)

    Chromosome 3L - NT_037436.4Genomic Context describing neighboring genes Neighboring gene Jonah 65Aiii Neighboring gene Jonah 65Aii Neighboring gene tantalus Neighboring gene long non-coding RNA:CR45441

    Genomic regions, transcripts, and products

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Gene Ontology Provided by FlyBase

    Process Evidence Code Pubs
    involved_in innate immune response IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
     
    involved_in proteolysis ISM
    Inferred from Sequence Model
    more info
    PubMed 
    Component Evidence Code Pubs
    is_active_in extracellular space IBA
    Inferred from Biological aspect of Ancestor
    more info
     

    General protein information

    Preferred Names
    jonah 65Ai
    Names
    CG10475-PA
    CG10475-PB
    Jon65Ai-PA
    Jon65Ai-PB
    jonah 65A
    NP_001286951.1
    NP_648015.1

    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
      6053493..6054443 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001300022.1NP_001286951.1  jonah 65Ai, isoform B [Drosophila melanogaster]

      See identical proteins and their annotated locations for NP_001286951.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      Q9VRS9
      Conserved Domains (2) summary
      smart00020
      Location:37254
      Tryp_SPc; Trypsin-like serine protease
      cd00190
      Location:41257
      Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...
    2. NM_139758.2NP_648015.1  jonah 65Ai, isoform A [Drosophila melanogaster]

      See identical proteins and their annotated locations for NP_648015.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      Q9VRS9
      Related
      FBpp0076775
      Conserved Domains (2) summary
      smart00020
      Location:37254
      Tryp_SPc; Trypsin-like serine protease
      cd00190
      Location:41257
      Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...