Detail Information for IndEnz0002016288
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