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    Spn42Db Serpin 42Db [ Drosophila melanogaster (fruit fly) ]

    Gene ID: 35599, updated on 9-Dec-2024

    Summary

    Official Symbol
    Spn42Dbprovided by FlyBase
    Official Full Name
    Serpin 42Dbprovided by FlyBase
    Primary source
    FLYBASE:FBgn0033112
    Locus tag
    Dmel_CG9454
    See related
    AllianceGenome:FB:FBgn0033112
    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
    CG9454; Dmel\CG9454
    Summary
    Predicted to enable serine-type endopeptidase inhibitor activity. Predicted to be involved in negative regulation of proteolysis. Predicted to be active in extracellular space. Human ortholog(s) of this gene implicated in familial encephalopathy with neuroserpin inclusion bodies. Orthologous to human SERPINI1 (serpin family I member 1) and SERPINI2 (serpin family I member 2). [provided by Alliance of Genome Resources, Dec 2024]
    Orthologs
    NEW
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    Genomic context

    See Spn42Db in Genome Data Viewer
    Location:
    42D6-42D6; 2-55 cM
    Exon count:
    3
    Annotation release Status Assembly Chr Location
    Release 6.54 current Release 6 plus ISO1 MT (GCF_000001215.4) 2R NT_033778.4 (6879285..6880770, complement)
    Release 5.57 previous assembly Release 5 (GCF_000001215.2) 2R NT_033778.3 (2766790..2768275, complement)

    Chromosome 2R - NT_033778.4Genomic Context describing neighboring genes Neighboring gene antisense RNA:CR44169 Neighboring gene uncharacterized protein Neighboring gene Serpin 42Da Neighboring gene Serpin 42Dc Neighboring gene Serpin 42Dd Neighboring gene Serpin 42De

    Genomic regions, transcripts, and products

    General gene information

    Gene Ontology Provided by FlyBase

    Function Evidence Code Pubs
    enables serine-type endopeptidase inhibitor activity IEA
    Inferred from Electronic Annotation
    more info
     
    Process Evidence Code Pubs
    involved_in negative regulation of 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
     
    located_in extracellular space IEA
    Inferred from Electronic Annotation
    more info
     

    General protein information

    Preferred Names
    serpin 42Db
    Names
    CG9454-PC
    CG9454-PD
    Spn42Db-PC
    Spn42Db-PD

    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_033778.4 Reference assembly

      Range
      6879285..6880770 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_136400.3NP_610244.2  serpin 42Db, isoform C [Drosophila melanogaster]

      See identical proteins and their annotated locations for NP_610244.2

      Status: REVIEWED

      UniProtKB/TrEMBL
      A1Z6R3, F3YDI3
      Conserved Domains (1) summary
      cd00172
      Location:12373
      SERPIN; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate ...
    2. NM_001273817.1NP_001260746.1  serpin 42Db, isoform D [Drosophila melanogaster]

      See identical proteins and their annotated locations for NP_001260746.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      A0A0B4KF64, Q4V6M2
      Conserved Domains (1) summary
      cd00172
      Location:12283
      SERPIN; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate ...