Q9UW98 · DPP5_TRIRU

Function

function

Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini. Contributes to pathogenicity (By similarity).

Features

Showing features for active site.

1726100200300400500600700
TypeIDPosition(s)Description
Active site558Charge relay system
Active site641Charge relay system
Active site673Charge relay system

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Molecular Functionaminopeptidase activity
Molecular Functionserine-type endopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Dipeptidyl-peptidase 5
  • EC number
  • Alternative names
    • Dipeptidyl-peptidase V (DPP V; DppV)
  • Allergen name
    Tri r 4

Gene names

    • Name
      DPPV

Organism names

Accessions

  • Primary accession
    Q9UW98
  • Secondary accessions
    • Q6E7G5

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Allergenic properties

Causes an allergic reaction in human. Binds to IgE and associated with delayed type hypersensitivity.

Keywords

Protein family/group databases

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

Type
IDPosition(s)Description
Signal1-19
ChainPRO_000002722520-726Dipeptidyl-peptidase 5
Glycosylation96N-linked (GlcNAc...) asparagine
Glycosylation252N-linked (GlcNAc...) asparagine
Glycosylation485N-linked (GlcNAc...) asparagine
Glycosylation605N-linked (GlcNAc...) asparagine
Glycosylation699N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Expression

Induction

Expression is strongly increased during growth on protein-rich medium containing keratin.

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region269-291Disordered

Sequence similarities

Belongs to the peptidase S9C family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    726
  • Mass (Da)
    80,121
  • Last updated
    2000-05-01 v1
  • Checksum
    83609D55F06783A4
MAAAKWLIASLAFASSGLAFTPEDFISAPRRGEAIPDPKGELAVFHVSKYNFDKKDRPSGWNLLNLKNGDINVLTTDSDVSEITWLGDGTKVVYINGTDSVKGGVGIWISDAKNFGNAYKAGSVNGAFSGLKLAKSGDKINFVGYGQSTTKGDLYNEAAAKEAVSSARIYDSLFVRHWDTYVGTQFNAVFSGTLTKSGDKYSFDGKLKNLVQPVKYAESPYPPFGGSGDYDLSSDGKTVAFMSKAPELPKANLTTSYIFLVPHDGSRVAEPINKRNGPRTPQGIEGASSSPVFSPDGKRIAYLQMAAKNYESDRRVIHIAEVGTNKPVQRIASNWDRSPEAVKWSSDGRTLYVTAEDHATGKLFTLPADARDNHKPAVVKHDGSVSSFYFIGSSKSVLISGNSLWSNALYQVATPDRPNRKLFYANEHDPELKGLGPNDIEPLWVDGARTKIHSWIVKPTGFDKNKVYPLAFLIHGGPQGSWGDNWSTRWNPRVWADQGYVVVAPNPTGSTGFGQKLTDDITNDWGGAPYKDLVKIWEHVHDHIKYIDTDNGIAAGASFGGFMVNWIQGQDLGRKFKALVSHDGTFVGSSKIGTDELFFIEHDFNGTFFEARQNYDRWDCSKPELVAKWSTPQLVVHNDFDFRLSVAEGVGLFNVLQEKGVPSRFLNFPDETHWVTKPENSLVWHQQVLGWVNKWSGINKSNPKSIKLSDCPIEVVDHEAHSYFDY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF082514
EMBL· GenBank· DDBJ
AAD52012.1
EMBL· GenBank· DDBJ
mRNA
AY525331
EMBL· GenBank· DDBJ
AAS19461.1
EMBL· GenBank· DDBJ
Genomic DNA
AF407232
EMBL· GenBank· DDBJ
AAN03632.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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