| IED ID | IndEnz0002018473 |
| Enzyme Type ID | protease018473 |
| Protein Name |
Dipeptidyl peptidase 4 EC 3.4.14.5 Dipeptidyl peptidase IV DPP IV DppIV |
| Gene Name | DPP4 |
| 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 | MKFLSLLLLAGIAQAIVPPREPRPPTGGGNKLLTYKECVPRATISPRSTSLAWINSDEDGQYISQSDDGALILQNIVTNTNKTLVAADKVPKGYYDYWFKPDLSAVLWATNYTKQYRHSYFANYFILDIEKGSLTPLAQDQAGDIQYAQWSPVDNSIAYVRGNDLYIWNNGTTKRTTENGGPDIFNGVPDWVYEEEIFGDRFALWFSPDGEYLAYLRFNETGVPTYTIPYYKNKQKIAPAYPRELEIRYPKVSAKNPTVQFHLLNIASSQESTIPVTAFPENDLVIGEVAWLSSGHDSVAYRAFNRVQDREKIVSIKVESKESKVIRERDGTDGWIDNLLSMSYIGDVNGKEYYVDISDASGWAHIYLYPVDGGKEIALTKGEWEVVAILKVDTKKKLIYFTSTKYHSTTRHVYSVSYDTNVMTPLVNDKEAAYYTASFSAKGGYYILSYQGPNVPYQELYSTKDSKKPLKTITSNDALLEKLKEYKLPKVSFFEIKLPSGETLNVKQRLPPNFNPHKKYPVLFTPYGGPGAQEVSQAWNSLDFKSYITSDPELEYVTWTVDNRGTGYKGRKFRSAVAKRLGFLEAQDQVFAAKELLKNRWADKDHIGIWGWSYGGFLTAKTLETDSGVFTFGISTAPVSDFRLYDSMYTERYMKTVELNADGYSETAVHKVDGFKNLKGHYLIQHGTGDDNVHFQNAAVLSNTLMNGGVTADKLTTQWFTDSDHGIRYDMDSTYQYKQLAKMVYDQKQRRPERPPMHQWSKRVLAALFGERAEE |
| Enzyme Length | 775 |
| Uniprot Accession Number | A7UKV8 |
| Absorption | |
| Active Site | ACT_SITE 613; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 690; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 725; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.; EC=3.4.14.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10084}; |
| DNA Binding | |
| EC Number | 3.4.14.5 |
| Enzyme Function | FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Contributes to pathogenicity (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Glycosylation (4); 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..15; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 88,010 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |