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    LOC102362334 serpin I2 [ Latimeria chalumnae (coelacanth) ]

    Gene ID: 102362334, updated on 26-Apr-2024

    Summary

    Gene symbol
    LOC102362334
    Gene description
    serpin I2
    See related
    Ensembl:ENSLACG00000011728
    Gene type
    protein coding
    RefSeq status
    MODEL
    Organism
    Latimeria chalumnae
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Coelacanthiformes; Coelacanthidae; Latimeria
    Also known as
    SERPINI2
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    Genomic context

    See LOC102362334 in Genome Data Viewer
    Location:
    chromosome: 8
    Exon count:
    8
    Annotation release Status Assembly Chr Location
    RS_2024_04 current fLatCha1.pri (GCF_037176945.1) 8 NC_088146.1 (6086546..6105448, complement)
    101 previous assembly LatCha1 (GCF_000225785.1) Unplaced Scaffold NW_005819819.1 (629956..648765, complement)

    Chromosome 8 - NC_088146.1Genomic Context describing neighboring genes Neighboring gene 5S ribosomal RNA Neighboring gene zinc finger, B-box domain containing Neighboring gene 5S ribosomal RNA Neighboring gene WD repeat-containing protein 49 Neighboring gene 5S ribosomal RNA Neighboring gene programmed cell death 10a

    Genomic regions, transcripts, and products

    General protein information

    Preferred Names
    serpin I2
    Names
    serpin family I member 2

    NCBI Reference Sequences (RefSeq)

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    RefSeqs of Annotated Genomes: GCF_037176945.1-RS_2024_04

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference fLatCha1.pri

    Genomic

    1. NC_088146.1 Reference fLatCha1.pri

      Range
      6086546..6105448 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_006002484.1XP_006002546.1  serpin I2

      UniProtKB/TrEMBL
      H3AUJ8
      Related
      ENSLACP00000013319.1, ENSLACT00000013415.1
      Conserved Domains (1) summary
      cl00137
      Location:33411
      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 ...