| IED ID | IndEnz0002001075 |
| Enzyme Type ID | protease001075 |
| Protein Name |
Venom dipeptidyl peptidase 4 EC 3.4.14.5 Venom dipeptidyl peptidase IV allergen Ves v 3 |
| Gene Name | |
| Organism | Vespula vulgaris (Yellow jacket) (Wasp) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Hymenoptera Apocrita (wasps ants and bees) Aculeata Vespoidea Vespidae (wasps) Vespinae (hornets and yellowjackets) Vespula Vespula vulgaris (Yellow jacket) (Wasp) |
| Enzyme Sequence | MVPLRSFVLLNSLFLVLLAARTVVTRVIDKDNSDRIVKTQNDQNLSKVPFNLEETYTADFLAYVFNGTWTSDTTIVYTDRRTGDILQFDVIKQRSTLIVDSSVMDAYIVSNYVLSPKGRYLLIGYDLKKGYRYSTFMRYVIYDIEHRAYHKIGNDMHIALAKWAPLTDDLIYILDNDIYYMRFSNNGFNDVQRVTYDGISGIVYNGVPDWVYEEEVLQDSSAIWFSPDGNHLAYASFDDRNVQEILYLHYGEPGNLDDQYPTEVKIKYPKVGTLNPVVSLTLVDLHDPTLNKIDLKAPHYAVGTDNLLYNVQWKDFDHVVVTWSNRVQNKTEIVWYNMYGEIVKTLHVVEHKGWLDIKHLFFYKGSVYIRKLQPSGTKAGRFHHVTRYDETFKQSPTQMDLTPDAIEVQNICTIDQSNGRIYYLASGLGKPSQKNLYSVPADGSEKPTCISCNVLTPEGNVCTYADAIFSPLGQYYVLVCHGPDPAFVSIFNNAHQKVYSWENNLSLRKKLAKRHLPLVKDLDVRANGYESKVRLFLPHNFDESKSYPMLVNVYAGPNTLKIIDAASYGHQVYMTTNRSVIYAYIDGRGSSNKGSKMLFSIYRKLGTVEVEDQITVTRQLQEMFPWIDSKRTGVWGWSYGGFSTAMILAKDTSFVFKCGIAIAPVSSWIYYDSIYTERFMGFPTPEDNLSGYNETDVSRRVEDIRGKKFMLIHGSGDDNVHYQQSLALAKALEKADVMFEQITYTDEAHALFGVLPHLYHTMDRFWSDCFSLSHAH |
| Enzyme Length | 776 |
| Uniprot Accession Number | B1A4F7 |
| Absorption | |
| Active Site | ACT_SITE 638; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 717; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 749; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by diprotin A. {ECO:0000269|PubMed:20348419}. |
| 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:0000269|PubMed:20348419}; |
| DNA Binding | |
| EC Number | 3.4.14.5 |
| Enzyme Function | FUNCTION: Venom dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. May process venom proteins into their active forms and/or modulate the chemotactic activity of immune cells after the insect sting. {ECO:0000269|PubMed:20348419}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (3); Glycosylation (7); Signal peptide (1) |
| Keywords | Allergen;Aminopeptidase;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20348419}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 88,924 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |