| TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
|---|---|---|---|---|
|
1.C.63.1.1 | Spider venom α-latrotoxin of 1401 aas, α-LTX. It induces massive exocytosis after binding to a surface receptor, latrophilin (LPH). In this process, it first induced membrane depolarization by inhibition of repolarizing K+ channels followed by the appearance of Ca2+ transients. In a second phase, the toxin induced a large inward current and a prominent increase in intracellular calcium ions, reflecting pore formation (Lajus et al. 2006). | Eukaryota |
Metazoa, Arthropoda | α-latrotoxin from Latrodectus mactans |
|
1.C.63.1.2 | α-latroinsectotoxin precursor (α-LIT) (1411aas) (Shatursky et al., 2007) | Eukaryota |
Metazoa, Arthropoda | α-LIT of Latrodectus mactans (Q02989) |
|
1.C.63.1.3 | α-latrocrustotoxin-Lt1a-like protein of 722 aas. | Eukaryota |
Metazoa, Arthropoda | Lt1a of Parasteatoda tepidariorum |
|
1.C.63.1.4 | Delta-latroinsectotoxin-Lt1a of 1214 aas and 2 TMSs near the N-terminus. It is an insecticidal presynaptic neurotoxin that induces massive neurotransmitter release at insect (but not vertebrate) neuromuscular junctions. Native toxin forms cation-permeable pores (with high permeability to calcium) in lipid membranes of locust muscle membrane and artificial lipid bilayers (Chen et al. 2021, Dulubova et al. 1996). It may bind to insect neurexin-1 homolog, insect adhesion G protein-coupled receptor L1 homolog, and insect receptor-type tyrosine-protein phosphatase S homolog, and induces neurotransmitter exocytosis both by forming tetrameric pores in membranes and signaling via G protein-coupled receptor. Oligomerization is a process independent of divalent cations (Chen et al. 2021).
| None |
Metazoa, Arthropoda | Delta-latroinsectotoxin-Lt1a of Latrodectus tredecimguttatus (Mediterranean black widow spider) |