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    IMP2 endopeptidase catalytic subunit [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855051, updated on 3-Nov-2024

    Summary

    Official Symbol
    IMP2
    Official Full Name
    endopeptidase catalytic subunit
    Primary source
    SGD:S000004638
    Locus tag
    YMR035W
    See related
    AllianceGenome:SGD:S000004638; FungiDB:YMR035W; VEuPathDB:YMR035W
    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 endopeptidase activity. Involved in protein processing involved in protein targeting to mitochondrion. Part of mitochondrial inner membrane peptidase complex. Orthologous to human IMMP2L (inner mitochondrial membrane peptidase subunit 2). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

    See IMP2 in Genome Data Viewer
    Location:
    chromosome: XIII
    Exon count:
    1
    Sequence:
    Chromosome: XIII; NC_001145.3 (341142..341675)

    Chromosome XIII - NC_001145.3Genomic Context describing neighboring genes Neighboring gene Arp9p Neighboring gene Rch1p Neighboring gene putative tyrosine protein phosphatase MIH1 Neighboring gene stress-responsive transcriptional activator MSN2

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables endopeptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables endopeptidase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    enables endopeptidase activity IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    enables peptidase activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables serine-type endopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
     
    Component Evidence Code Pubs
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
     
    located_in mitochondrial inner membrane IEA
    Inferred from Electronic Annotation
    more info
     
    part_of mitochondrial inner membrane peptidase complex IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    part_of mitochondrial inner membrane peptidase complex IEA
    Inferred from Electronic Annotation
    more info
     
    part_of mitochondrial inner membrane peptidase complex IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
     

    General protein information

    Preferred Names
    endopeptidase catalytic subunit
    NP_013749.1
    • Catalytic subunit of mitochondrial inner membrane peptidase complex; required for maturation of mitochondrial proteins of the intermembrane space; complex contains two catalytic subunits (Imp1p and Imp2p that differ in substrate specificity), and Som1p

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

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

    Reference assembly

    Genomic

    1. NC_001145.3 Reference assembly

      Range
      341142..341675
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182532.1NP_013749.1  TPA: endopeptidase catalytic subunit [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013749.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VZL0, P46972
      UniProtKB/TrEMBL
      A6ZM97, B3LLT4, B5VPG4, C7GL84, C8ZEP2, G2WK88, N1NYM8
      Conserved Domains (1) summary
      cd06530
      Location:34147
      S26_SPase_I; The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4.21.89) family members are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are ...