Target Information

General Information of This Target
Target ID
BTDT00105
Target Name
Acetylcholine-binding protein
Target Bioclass
Transporter and channel
Uniprot ID
P58154
3D Structure
Download
2D Sequence
3D Structure
Source
Predict by Alphafold2
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Alphafold Parameters: msa_mode: mmseqs2_uniref_env model_type: auto num_recycles: auto
Sequence
MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEV
NEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQ
LARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDD
SEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL

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Function
Binds to acetylcholine. Modulates neuronal synaptic transmission.

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Taxonomy ID
6523
TCDB ID
1.A.9.1.19
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Kingdom: Metazoa
Phylum: Mollusca
Class: Gastropoda
Family: Lymnaeidae
Genus: Lymnaea
Species: Lymnaea stagnalis
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Alpha-elapitoxin-Dpp2d IC50
4.9 nM
 [1]
 Toxin Info    Toxin BMLCL IC50
333 nM
 [2], [3], [4]
 Toxin Info    Acidic phospholipase A2 Vur-PL2B IC50
>30 μM
 [5], [6]
 Toxin Info    Basic phospholipase A2 vurtoxin IC50
>30 μM
 [5], [6]
 Toxin Info    Acidic phospholipase A2 CM-II IC50
1 μM
 [6], [7], [8], [9]
 Toxin Info    Azemiopsin IC50
63 μM
 [10]
References
Ref 1 Isolation and structural and pharmacological characterization of -elapitoxin-Dpp2d, an amidated three finger toxin from black mamba venom. Biochemistry. 2014 Jun 17;53(23):3758-66. doi: 10.1021/bi5004475. Epub 2014 Jun 5.
Ref 2 cDNA sequence analysis of a novel member of the three loop protein family from the Chinese continental banded krait. Biosci Biotechnol Biochem. 1999 May;63(5):940-2. doi: 10.1271/bbb.63.940.
Ref 3 Muscarinic toxin-like proteins from Taiwan banded krait (Bungarus multicinctus) venom: purification, characterization and gene organization. Biol Chem. 2002 Sep;383(9):1397-406. doi: 10.1515/BC.2002.158.
Ref 4 Nonconventional three-finger toxin BMLCL from krait Bungarus multicinctus venom with high affinity interacts with nicotinic acetylcholine receptors. Dokl Biochem Biophys. 2015;464:294-7. doi: 10.1134/S1607672915050099. Epub 2015 Oct 31.
Ref 5 cDNA cloning, structural, and functional analyses of venom phospholipases A? and a Kunitz-type protease inhibitor from steppe viper Vipera ursinii renardi. Toxicon. 2011 Feb;57(2):332-41. doi: 10.1016/j.toxicon.2010.12.012. Epub 2010 Dec 23.
Ref 6 Inhibition of nicotinic acetylcholine receptors, a novel facet in the pleiotropic activities of snake venom phospholipases A2. PLoS One. 2014 Dec 18;9(12):e115428. doi: 10.1371/journal.pone.0115428. eCollection 2014.
Ref 7 Regional and accelerated molecular evolution in group I snake venom gland phospholipase A2 isozymes. Toxicon. 2000 Mar;38(3):449-62. doi: 10.1016/s0041-0101(99)00165-8.
Ref 8 Purification, some properties and amino-acid sequences of two phospholipases A (CM-II and CM-III) from Naja naja kaouthia venom. Eur J Biochem. 1980 Dec;112(3):493-9. doi: 10.1111/j.1432-1033.1980.tb06112.x.
Ref 9 A new type of thrombin inhibitor, noncytotoxic phospholipase A2, from the Naja haje cobra venom. Toxicon. 2010 Feb-Mar;55(2-3):186-94. doi: 10.1016/j.toxicon.2009.07.011. Epub 2009 Jul 19.
Ref 10 Azemiopsin from Azemiops feae viper venom, a novel polypeptide ligand of nicotinic acetylcholine receptor. J Biol Chem. 2012 Aug 3;287(32):27079-86. doi: 10.1074/jbc.M112.363051. Epub 2012 May 21.
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