Venom Protein Card
Accession: Pre05167 Apamin preproprotein [Apis mellifera]
Basic info
| Organism | Apis mellifera |
| Taxonomy | Insecta > Hymenoptera > Apidae > Apis > Apis mellifera |
| Protein Description | Apamin preproprotein |
| Mass Weight | 5223.34 Da |
| Isoelectric Point | 8.77 |
| Expression | Highly expressed in venom gland |
Annotation
| Function | Neurotoxin that blocks voltage-independent calcium-activated potassium channels (KCa2.1/KCNN1/SK1, KCa2.2/KCNN2/SK2, KCa2.3/KCNN3/SK3). | ||
| Pfam |
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Features
| Feature key | Position | Length |
| Signal Peptide | 1..27 | 27 |
| Peptide | 28..45 | 18 |
Sequence
Publication
| 1. |
Gmachl M., Kreil G.; "The precursors of the bee venom constituents apamin and MCD peptide are encoded by two genes in tandem which share the same 3'-exon."; J. Biol. Chem. 270:12704-12708(1995). |
| 2. |
Haux P., Sawerthal H., Habermann E.; "Sequence analysis of bee venom neurotoxin (apamine) from its tryptic and chymotryptic cleavage products."; Hoppe-Seyler's Z. Physiol. Chem. 348:737-738(1967). |
| 3. |
Shipolini R., Bradbury A.F., Callewaert G.L., Vernon C.A.; J. Chem. Soc. Chem. Commun. 1967:679-680(1967). |
| 4. |
Pease J.H.B., Wemmer D.E.; "Solution structure of apamin determined by nuclear magnetic resonance and distance geometry."; Biochemistry 27:8491-8498(1988). |
| 5. |
Andrianov A.M., Akhrem A.A.; "Spatial structure of apamin in solution."; Mol. Biol. (Mosk.) 25:937-945(1991). |
| 6. |
Labee-Jullie C., Granier C., Alberico F., Defendini M.-L., Ceard B., Rochat H., van Rietschoten J.; "Binding and toxicity of apamin. Characterization of the active site."; Eur. J. Biochem. 196:639-645(1991). |