IED ID | IndEnz0002016288 |
Enzyme Type ID | protease016288 |
Protein Name |
Dipeptidyl peptidase 4 EC 3.4.14.5 Dipeptidyl peptidase IV DPP IV DppIV |
Gene Name | DPP4 |
Organism | Trichophyton tonsurans (Scalp ringworm fungus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Trichophyton tonsurans (Scalp ringworm fungus) |
Enzyme Sequence | MKLLSLLMLAGIAQAIVPPREPRPPTGGGNKLLTYKECVPRATISPRSTSLAWINSDEDGQYISQSDDGALILQNIVTNTNKTLVAADKVPKGYYDYWFKPDLSAVLWATNYTKQYRHSYFANYFILDIEKGSLTPLAQDQAGDIQYAQWSPVDNSIAYVRGNDLYIWNNGTTKRITENGGPDIFNGVPDWVYEEEIFGDRFALWFSPDGEYLAYLRFNETGVPTYTIPYYKNKQKIAPAYPRELEIRYPKVSAKNPTVQFHLLNIASSQESTIPVTAFPENDLVIGEVAWLSSGHDSVAYRAFNRVQDREKIVSIKVESKESKVIRERDGTDGWIDNLLSMSYIGDVNGKEYYVDISDASGWAHIYLYPVDGGKEIALTKGEWEVVAILKVDTKKKLIYFTSTKYHSTTRHVYSVSYDTNVMTPLVNDKEAAYYTASFSAKGGYYILSYQGPNVPYQELYSTKDSKKPLKTITSNDALLEKLKEYKLPMVSFFEIKLPSGETLNVKQRLPPNFNPHKKYPVLFTPYGGPGAQEVSQAWNSLDFKSYITSDPELEYVTWTVDNRGTGYKGRKFRSAVAKRLGFLEAQDQVFAAKELLKNRWADKDHIGIWGWSYGGFLTAKTLETDSGVFTFGISTAPVSDFRLYDSMYTERYMKTVELNADGYSETAVHKVDGFKNLKGHYLIQHGTGDDNVHFQNAAVLSNTLMNGGVTADKLTTQWFTDSDHGIRYDMDSTYQYKQLAKMVYDQKQRRPERPPMHQWSKRVLAALFGERAEE |
Enzyme Length | 775 |
Uniprot Accession Number | B6V868 |
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 | 88,009 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |