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    dipeptidyl-peptidase III [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854097, updated on 2-Nov-2024

    Summary

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    Official Full Name
    dipeptidyl-peptidase III
    Primary source
    SGD:S000005418
    Locus tag
    YOL057W
    See related
    AllianceGenome:SGD:S000005418; FungiDB:YOL057W; VEuPathDB:YOL057W
    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 dipeptidyl-peptidase activity. Predicted to be involved in proteolysis. Located in cytoplasm and nucleus. Orthologous to human DPP3 (dipeptidyl peptidase 3). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    Location:
    chromosome: XV
    Exon count:
    1
    Sequence:
    Chromosome: XV; NC_001147.6 (220767..222902)

    Chromosome XV - NC_001147.6Genomic Context describing neighboring genes Neighboring gene glycerol-3-phosphate dehydrogenase (NAD(+)) GPD2 Neighboring gene argininosuccinate synthase Neighboring gene phosphoglycerate mutase family protein GPM3 Neighboring gene trifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase/thiaminase

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001147.6

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The first structure of dipeptidyl-peptidase III provides insight into the catalytic mechanism and mode of substrate binding. Baral PK, et al. J Biol Chem, 2008 Aug 8. PMID 18550518
    2. Identification of the reactive cysteine residues in yeast dipeptidyl peptidase III. Jajcanin-Jozić N, et al. Biochimie, 2010 Jan. PMID 19825391
    3. Importance of the three basic residues in the vicinity of the zinc-binding motifs for the activity of the yeast dipeptidyl peptidase III. Jajčanin-Jozić N, et al. J Biochem, 2014 Jan. PMID 24136327
    4. Hydrolysis of dipeptide derivatives reveals the diversity in the M49 family. Jajčanin-Jozić N, et al. Biol Chem, 2013 Jun. PMID 23362197
    5. Redox-dependent Regulation of Gluconeogenesis by a Novel Mechanism Mediated by a Peroxidatic Cysteine of Peroxiredoxin. Irokawa H, et al. Sci Rep, 2016 Sep 16. PMID 27634403, Free PMC Article

    See all (27) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. the 1.95-A crystal structure of yeast DPP III representing the prototype for the M49 family of metallopeptidases [dipeptidyl-peptidase III ]
      Title: The first structure of dipeptidyl-peptidase III provides insight into the catalytic mechanism and mode of substrate binding.
    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 IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables dipeptidyl-peptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables dipeptidyl-peptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables dipeptidyl-peptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables dipeptidyl-peptidase activity ISS
    Inferred from Sequence or Structural Similarity
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metalloexopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metallopeptidase activity 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 proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in proteolysis ISS
    Inferred from Sequence or Structural Similarity
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA 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 nucleus HDA PubMed 

    General protein information

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    Preferred Names
    dipeptidyl-peptidase III
    NP_014584.1
    • Dipeptidyl-peptidase III; cleaves dipeptides from the amino terminus of target proteins; highly active on synthetic substrate Arg-Arg-2-naphthylamide; mammalian ortholog may be a biomarker for some cancers

    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_001147.6 Reference assembly

      Range
      220767..222902
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183312.1 → NP_014584.1  TPA: dipeptidyl-peptidase III [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014584.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      O94146, Q05663, Q08225
      UniProtKB/TrEMBL
      B3LJ02, C8ZHQ6, N1NWQ2
      Conserved Domains (1) summary
      pfam03571
      Location:156 → 709
      Peptidase_M49; Peptidase family M49
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q08225.1

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