Venom Protein Card
Accession: Pre01695 Melittin [Vespa velutina]
Basic info
| Organism | Vespa velutina |
| Taxonomy | Insecta > Hymenoptera > Vespidae > Vespa > Vespa velutina |
| Protein Description | Melittin |
| Mass Weight | 7542.72 Da |
| Isoelectric Point | 4.69 |
| Expression | Highly expressed in venom gland |
Annotation
| Function | Main toxin of bee venom with strong hemolytic activity and antimicrobial activity. It has enhancing effects on bee venom phospholipase A2 activity. This amphipathic toxin binds to negatively charged membrane surface and forms pore by inserting into lipid bilayers inducing the leakage of ions and molecules and the enhancement of permeability that ultimately leads to cell lysis. It acts as a voltage-gated pore with higher selectivity for anions over cations. The ion conductance has been shown to be voltage-dependent. Self- association of melittin in membranes is promoted by high ionic strength, but not by the presence of negatively charged lipids. In vivo, intradermal injection into healthy human volunteers produce sharp pain sensation and an inflammatory response. It produces pain by activating primary nociceptor cells directly and indirectly due to its ability to activate plasma membrane phospholipase A2 and its pore- forming activity. | ||
| Pfam |
|
Features
| Feature key | Position | Length |
| Signal Peptide | 1..21 | 21 |
| Propeptide | 22..43 | 22 |
| Peptide | 44..69 | 26 |
Sequence
Publication
| 1. |
Shi W.J., Zhang S.F., Zhang C.-X., Cheng J.A.; "Cloning and comparative analysis of the venom prepromelittin genes from four wasp species."; Yi Chuan Xue Bao 30:555-559(2003). |