| IED ID | IndEnz0002005217 |
| Enzyme Type ID | protease005217 |
| Protein Name |
Dipeptidyl-peptidase 5 EC 3.4.14.- Dipeptidyl-peptidase V DPP V DppV |
| Gene Name | DPP5 |
| Organism | Trichophyton equinum (Horse ringworm fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Trichophyton equinum (Horse ringworm fungus) |
| Enzyme Sequence | MAAAKWLIASLAFASSGLAFTPEDFISAPRRGEAIPDPKGELAVFHVSKYNFDKKDRPSGWNLLNLKNGDISVLTTDSDISEITWLGDGTKIVYVNGTDSVKGGVGIWISDAKNFGNAYKAGSVNGAFSGLKLAKSGDKINFVGYGQSTTKGDLYNEAAAKEAVSSARIYDSLFVRHWDTYVGTQFNAVFSGALTKSGDKYSFDGKLKNLVHPVKYAESPYPPFGGSGDYDLSSDGKTVAFMSKAPELPKANLTTTYIFVVPHDGSRVAEPINKRNGPRTPQAIEGASSSPVFSPDGKRIAYLQMATKNYESDRRVIHIAEVGSNKPVQRIASNWDRSPEVVKWSSDGRTLYVTAEDHATGKLFTLPADARDSHKPAVVKHDGSVSSFYFVGSSKSVLISGNSLWSNALFQVATPGRPNRKLFYANEHDPELKGLGPNDIEPLWVDGARTKIHSWIVKPTGFDKNKVYPLAFLIHGGPQGSWGDSWSTRWNPRVWADQGYVVVAPNPTGSTGFGQKLTDDITNDWGGAPYKDLVKIWEHVRDHIKYIDTDNGIAAGASFGGFMVNWIQGHDLGRKFKALVSHDGTFVGSSKIGTDELFFIEHDFNGTFFEARQNYDRWDCSKPELVAKWSTPQLVIHNDFDFRLSVAEGVGLFNVLQEKGIPSRFLNFPDETHWVTKPENSLVWHQQVLGWINKWSGINKSNPKSIKLSDCPIEVVDHEAHSYFDY |
| Enzyme Length | 726 |
| Uniprot Accession Number | A7UKV4 |
| Absorption | |
| Active Site | ACT_SITE 558; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 641; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 673; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.14.- |
| Enzyme Function | FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini. Contributes to pathogenicity (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Glycosylation (4); Region (1); Signal peptide (1) |
| Keywords | Aminopeptidase;Glycoprotein;Hydrolase;Protease;Secreted;Serine protease;Signal;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 80,073 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |