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    DAP2 dipeptidyl aminopeptidase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856423, updated on 9-Dec-2024

    Summary

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    Official Symbol
    DAP2
    Official Full Name
    dipeptidyl aminopeptidase
    Primary source
    SGD:S000001070
    Locus tag
    YHR028C
    See related
    AllianceGenome:SGD:S000001070; FungiDB:YHR028C; VEuPathDB:YHR028C
    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
    DPP2
    Summary
    Enables dipeptidyl-peptidase activity. Predicted to be involved in protein processing. Located in fungal-type vacuole membrane. Human ortholog(s) of this gene implicated in Middle East respiratory syndrome and type 2 diabetes mellitus. Orthologous to human DPP4 (dipeptidyl peptidase 4). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See DAP2 in Genome Data Viewer
    Location:
    chromosome: VIII
    Exon count:
    1
    Sequence:
    Chromosome: VIII; NC_001140.6 (164978..167434, complement)

    Chromosome VIII - NC_001140.6Genomic Context describing neighboring genes Neighboring gene H(+)-transporting V0 sector ATPase subunit c'' Neighboring gene proteasome regulatory particle base subunit RPN1 Neighboring gene Yhi9p Neighboring gene mitogen-activated serine/threonine-protein kinase SLT2

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001140.6

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Structure, biosynthesis, and localization of dipeptidyl aminopeptidase B, an integral membrane glycoprotein of the yeast vacuole. Roberts CJ, et al. J Cell Biol, 1989 Apr. PMID 2647766, Free PMC Article
    2. Identification of the structural gene for dipeptidyl aminopeptidase yscV (DAP2) of Saccharomyces cerevisiae. Suárez Rendueles P, et al. J Bacteriol, 1987 Sep. PMID 3305478, Free PMC Article
    3. Localization of the thermosensitive X-prolyl dipeptidyl aminopeptidase in the vacuolar membrane of Saccharomyces cerevisiae. Bordallo C, et al. FEBS Lett, 1984 Jul 23. PMID 6378661
    4. Membrane protein sorting in the yeast secretory pathway: evidence that the vacuole may be the default compartment. Roberts CJ, et al. J Cell Biol, 1992 Oct. PMID 1527174, Free PMC Article
    5. Sec61p is required for ERAD-L: genetic dissection of the translocation and ERAD-L functions of Sec61P using novel derivatives of CPY. Willer M, et al. J Biol Chem, 2008 Dec 5. PMID 18819915, Free PMC Article

    See all (35) 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 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 serine-type endopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables serine-type peptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in protein processing ISS
    Inferred from Sequence or Structural Similarity
    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 fungal-type vacuole membrane HDA PubMed 
    located_in fungal-type vacuole membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in plasma membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in vacuolar membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in vacuole IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    dipeptidyl aminopeptidase
    NP_011893.1
    • Dipeptidyl aminopeptidase; synthesized as a glycosylated precursor; localizes to the vacuolar membrane; similar to Ste13p

    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_001140.6 Reference assembly

      Range
      164978..167434 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179158.1 → NP_011893.1  TPA: dipeptidyl aminopeptidase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_011893.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D3DKX5, E9P957, P18962
      UniProtKB/TrEMBL
      B3LSE9, C7GTV2, N1P2T7
      Conserved Domains (2) summary
      pfam00326
      Location:608 → 815
      Peptidase_S9; Prolyl oligopeptidase family
      pfam00930
      Location:148 → 508
      DPPIV_N; Dipeptidyl peptidase IV (DPP IV) N-terminal region
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P18962.2

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