Venom Protein Card
Accession: Pre05382 Melittin [Apis cerana]
Basic info
| Organism | Apis cerana |
| Taxonomy | Insecta > Hymenoptera > Apidae > Apis > Apis cerana |
| Protein Description | Melittin |
| Mass Weight | 8514.84 Da |
| Isoelectric Point | 6.03 |
| 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 |
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Features
| Feature key | Position | Length |
| Signal Peptide | 1..30 | 30 |
| Propeptide | 31..50 | 20 |
| Peptide | 51..76 | 26 |
Sequence
3D Structure
Not available now!
Publication
| 1. |
Le H.Q., Le B.T.; "Gene encoding melittin in honeybee Apis cerana colleted in Hanoi Vietnam."; Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. |
| 2. |
Kreil G.; "Structure of melittin isolated from two species of honey bees."; FEBS Lett. 33:241-244(1973). |