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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

Gene LinkOut

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