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    ICP55 aminopeptidase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856811, updated on 2-Nov-2024

    Summary

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    Official Symbol
    ICP55
    Official Full Name
    aminopeptidase
    Primary source
    SGD:S000000880
    Locus tag
    YER078C
    See related
    AllianceGenome:SGD:S000000880; FungiDB:YER078C; VEuPathDB:YER078C
    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 aminopeptidase activity. Involved in protein processing and protein stabilization. Located in mitochondrion and nucleus. Used to study nephronophthisis-like nephropathy 1. Human ortholog(s) of this gene implicated in nephronophthisis-like nephropathy 1. Orthologous to human XPNPEP3 (X-prolyl aminopeptidase 3). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See ICP55 in Genome Data Viewer
    Location:
    chromosome: V
    Exon count:
    1
    Sequence:
    Chromosome: V; NC_001137.3 (316807..318342, complement)

    Chromosome V - NC_001137.3Genomic Context describing neighboring genes Neighboring gene uncharacterized protein Neighboring gene Mrx1p Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001137.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Novel highly sensitive, specific, and straightforward strategy for comprehensive N-terminal proteomics reveals unknown substrates of the mitochondrial peptidase Icp55. Venne AS, et al. J Proteome Res, 2013 Sep 6. PMID 23964590
    2. Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55. Naamati A, et al. J Biol Chem, 2009 Oct 30. PMID 19720832, Free PMC Article
    3. Mitochondrial protein turnover: role of the precursor intermediate peptidase Oct1 in protein stabilization. Vögtle FN, et al. Mol Biol Cell, 2011 Jul 1. PMID 21525245, Free PMC Article
    4. Mitochondrial aminopeptidase deletion increases chronological lifespan and oxidative stress resistance while decreasing respiratory metabolism in S. cerevisiae. Stames EM, et al. PLoS One, 2013. PMID 24116217, Free PMC Article
    5. Role of the novel metallopeptidase Mop112 and saccharolysin for the complete degradation of proteins residing in different subcompartments of mitochondria. Kambacheld M, et al. J Biol Chem, 2005 May 20. PMID 15772085

    See all (39) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Data report the crystal structures of Icp55 including one bound to the apstatin inhibitor. Apart from icp activity, the enzyme was found to exhibit Xaa-Pro aminopeptidase activity in vitro. Furthermore, the enzyme seems to exist in a rapid equilibrium between monomers and dimers. The latter was found to be the active species with loop dynamics at the dimer interface playing an important role in activity.
      Title: Crystal structures and biochemical analyses of intermediate cleavage peptidase: role of dynamics in enzymatic function.
    2. The icp55 deletion strain demonstrated an increased chronological lifespan and decreased reactive oxygen species.
      Title: Mitochondrial aminopeptidase deletion increases chronological lifespan and oxidative stress resistance while decreasing respiratory metabolism in S. cerevisiae.
    3. A novel substrate, Isa2, is likely processed by Icp55 in two consecutive steps and thus might represent the first example of a triple processing event in a mitochondrial precursor protein.
      Title: Novel highly sensitive, specific, and straightforward strategy for comprehensive N-terminal proteomics reveals unknown substrates of the mitochondrial peptidase Icp55.
    4. Icp55 protease and its substrate Nfs1 appear to be dual distributed between the nucleus and mitochondria
      Title: Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables aminopeptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables aminopeptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables aminopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables aminopeptidase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables manganese ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metalloaminopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metallopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in protein processing IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in protein processing IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein stabilization IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proteolysis IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in mitochondrial inner membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrion HDA PubMed 
    is_active_in mitochondrion IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in mitochondrion IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    aminopeptidase
    NP_011001.1
    • Mitochondrial aminopeptidase; cleaves N termini of at least 38 imported proteins after cleavage by the mitochondrial processing peptidase (MPP), thereby increasing their stability; member of aminopeptidase P family; exists in rapid equilibrium between monomer and dimer, with dimer being active species; ortholog of human gene XPNPEP3, which is mutated in rare hereditary kidney disease similar to nephronophthisis

    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_001137.3 Reference assembly

      Range
      316807..318342 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001178969.1 → NP_011001.1  TPA: aminopeptidase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_011001.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D3DLY4, P40051
      UniProtKB/TrEMBL
      A6ZR33, B3LRJ5, C7GRR0, C8Z788, N1PA46
      Conserved Domains (2) summary
      cd01087
      Location:250 → 481
      Prolidase; E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline dipeptidase., imidodipeptidase, peptidase D, gamma-peptidase. Catalyses hydrolysis of Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro.
      pfam05195
      Location:70 → 192
      AMP_N; Aminopeptidase P, N-terminal domain
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P40051.1

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