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DAP2 dipeptidyl aminopeptidase [ Saccharomyces cerevisiae S288C ]

Gene ID: 856423, updated on 2-Nov-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, Nov 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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