Venom Protein Card
Accession: Pre02141 Phospholipase A1 [Vespa basalis]
Basic info
| Organism | Vespa basalis |
| Taxonomy | Insecta > Hymenoptera > Vespidae > Vespa > Vespa basalis |
| Protein Description | Phospholipase A1 |
| Mass Weight | 33184.88 Da |
| Isoelectric Point | 8.91 |
| Expression | Highly expressed in venom gland |
Annotation
| Function | Catalyzes the hydrolysis of phosphatidylcholine with phospholipase A1 activity (By similarity). Shows potent hemolytic activity that is responsible for its lethal effect. In vivo, induces local inflammatory effects. | ||
| Pfam |
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Features
| Feature key | Position | Length |
| Chain | 1..300 | 300 |
Sequence
3D Structure
Not available now!
Publication
| 1. |
Hou M.H., Chuang C.Y., Ko T.P., Hu N.J., Chou C.C., Shih Y.P., Ho C.L., Wang A.H.; "Crystal structure of vespid phospholipase A(1) reveals insights into the mechanism for cause of membrane dysfunction."; Insect Biochem. Mol. Biol. 68:79-88(2016). |
| 2. |
Ho C.L., Hwang L.L., Chen C.T.; "Edema-inducing activity of a lethal protein with phospholipase A1 activity isolated from the black-bellied hornet (Vespa basalis) venom."; Toxicon 31:605-613(1993). |