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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

Gene LinkOut

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