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    APE2 metallo-aminopeptidase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 853699, updated on 4-Aug-2024

    Summary

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    Gene symbol
    APE2
    Gene description
    metallo-aminopeptidase
    Primary source
    FungiDB:YKL157W
    Locus tag
    YKL157W
    See related
    SGD:S000001640; AllianceGenome:SGD:S000001640; VEuPathDB:YKL157W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Also known as
    LAP1; YKL158W
    Summary
    Enables metalloaminopeptidase activity. Involved in peptide catabolic process. Located in cell wall-bounded periplasmic space and extracellular region. Human ortholog(s) of this gene implicated in cervix carcinoma. Orthologous to several human genes including NPEPPS (aminopeptidase puromycin sensitive). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See APE2 in Genome Data Viewer
    Location:
    chromosome: XI
    Exon count:
    2
    Sequence:
    Chromosome: XI; NC_001143.9 (154991..158232)

    Chromosome XI - NC_001143.9Genomic Context describing neighboring genes Neighboring gene Elf1p Neighboring gene Rcn1p Neighboring gene ribosomal 40S subunit protein S27A Neighboring gene tRNA methyltransferase RSM22

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001143.9

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Aminopeptidase yscII of yeast. Isolation of mutants and their biochemical and genetic analysis. Hirsch HH, et al. Eur J Biochem, 1988 May 2. PMID 3286257
    2. Molecular cloning of soluble aminopeptidases from Saccharomyces cerevisiae. Sequence analysis of aminopeptidase yscII, a putative zinc-metallopeptidase. García-Alvarez N, et al. Eur J Biochem, 1991 Dec 18. PMID 1765107
    3. External and internal forms of yeast aminopeptidase II. Frey J, et al. Eur J Biochem, 1979 Jun. PMID 383482
    4. Identification and characterization of CaApe2--a neutral arginine/alanine/leucine-specific metallo-aminopeptidase from Candida albicans. Klinke T, et al. FEMS Yeast Res, 2008 Sep. PMID 18637841
    5. Isolation and characterization of aminopeptidase mutants of Saccharomyces cerevisiae. Trumbly RJ, et al. J Bacteriol, 1983 Oct. PMID 6352682, Free PMC Article

    See all (47) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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 IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metalloaminopeptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables metalloaminopeptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metallopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables peptide binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables zinc ion binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables zinc ion binding RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in peptide catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in peptide catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in peptide catabolic process 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 cell wall-bounded periplasmic space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in extracellular region IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in extracellular space IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    is_active_in membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in mitochondrion HDA PubMed 
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleus HDA PubMed 
    located_in periplasmic space IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    metallo-aminopeptidase
    NP_012765.3
    • Aminopeptidase yscII; may have role in obtaining leucine from dipeptide substrates; targeted to vacuole via Vps10p-dependent endosomal vacuolar protein sorting pathway; APE2 has a paralog, AAP1, that arose from the whole genome duplication

    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_001143.9 Reference assembly

      Range
      154991..158232
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179723.2 → NP_012765.3  TPA: metallo-aminopeptidase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012765.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VX41, P32454, P36055
      UniProtKB/TrEMBL
      C8ZC17, N1P147
      Conserved Domains (1) summary
      COG0308
      Location:90 → 941
      PepN; Aminopeptidase N [Amino acid transport and metabolism]
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P32454.4

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