Q9UW98 · DPP5_TRIRU
- ProteinDipeptidyl-peptidase 5
- GeneDPPV
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids726 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 558 | Charge relay system | |||
Active site | 641 | Charge relay system | |||
Active site | 673 | Charge relay system | |||
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | aminopeptidase activity | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDipeptidyl-peptidase 5
- EC number
- Alternative names
- Allergen nameTri r 4
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Arthrodermataceae > Trichophyton
Accessions
- Primary accessionQ9UW98
- Secondary accessions
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Allergenic properties
Causes an allergic reaction in human. Binds to IgE and associated with delayed type hypersensitivity.
Keywords
- Disease
Protein family/group databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-19 | ||||
Chain | PRO_0000027225 | 20-726 | Dipeptidyl-peptidase 5 | ||
Glycosylation | 96 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 252 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 485 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 605 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 699 | N-linked (GlcNAc...) asparagine | |||
Keywords
- PTM
PTM databases
Expression
Induction
Expression is strongly increased during growth on protein-rich medium containing keratin.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length726
- Mass (Da)80,121
- Last updated2000-05-01 v1
- Checksum83609D55F06783A4
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |