| IED ID | IndEnz0002001076 |
| Enzyme Type ID | protease001076 |
| Protein Name |
Venom dipeptidyl peptidase 4 Allergen C Venom dipeptidyl peptidase IV EC 3.4.14.5 allergen Api m 5 |
| Gene Name | |
| Organism | Apis mellifera (Honeybee) |
| 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 Apoidea (bees) Apidae (bumble bees and honey bees) Apinae (honey bees) Apini Apis Apis mellifera (Honeybee) |
| Enzyme Sequence | MEVLVQLALLLVVHGSLVVLVAGKSVPRVIDQDLERYEPLEEEDHRGARVPFNLEETYDQSFRANSFNGTWKTDREILYSDNYVGDIRLFDVTTGSGTVLLDSSVTADFDKASVMFSFDNSHVAIGHDYVNGFRYSIHQKCTVYNIKSRTFTDIANGDRIPLFKWSPTRNALIYVHKNDIYYQVFFEGGSDTRRITNTGVPDIVFNGIPDWVYEEEVLGSPVAFWISPDGRHLAFATFNDTNVRDIVISKYGSPGNSRDQYPNEIRIKYPKAGTTNPFVSLSVIDLHDPSSKLIDLPPPVDVVGADNVLYTANWRRDGEIVATWTNRVQNKAQLVLYDTKGNANNIYYEEETEGWLRIQPPLYHDRYVIVAKLQDSGTKAGRFLHATRLEYRNGALVDETDLTPGTCEVISLLLVDHARARLYYLGTELGKPSHKNLYSVQLSGNEPPVCLSCDVLTPEGNRCTYAYAYFSTNGSHYALYCAGPDPVFIAIVNANHRQISIWEENRSLRRKLAARTQPIVKNFNVNANGYTNKVKLYLPPDFDETKKYPLLITVYAGPNTIRITEEATYGFESYIVTNRSVIYGRIDGRGSAYKGSKMLFEIYRRLGTVEIEDQIIITRTLQEKYSWIDSNRTGIWGWSYGGFSAAMVLATDAESVFKCGISVAPVTSWIYYDSLYTERFMGLPTPEDNQSGYNDTDVSRRVEGMRGKKYMLIHGTADDNVHYQQTMMLNKALVNSDIMFQQQTYTDEAHALGNVFPHLYHTTDRFWANCLGYSH |
| Enzyme Length | 775 |
| Uniprot Accession Number | B2D0J4 |
| Absorption | |
| Active Site | ACT_SITE 639; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 718; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 750; /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 promelittin into its active form 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 (8); Signal peptide (1) |
| Keywords | Allergen;Aminopeptidase;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20348419}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 87,937 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |