General Information of This Target
Target ID
BTDT00034
Target Name
Acetylcholine receptor subunit delta (chrnd)
Target Bioclass
Transporter and channel
Uniprot ID
P02718
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
Gene Name
chrnd
Sequence
MGNIHFVYLLISCLYYSGCSGVNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTL
SNLISLKETDETLTSNVWMDHAWYDHRLTWNASEYSDISILRLPPELVWIPDIVLQNNND
GQYHVAYFCNVLVRPNGYVTWLPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYDANEIT
MDLMTDTIDGKDYPIEWIIIDPEAFTENGEWEIIHKPAKKNIYPDKFPNGTNYQDVTFYL
IIRRKPLFYVINFITPCVLISFLASLAFYLPAESGEKMSTAISVLLAQAVFLLLTSQRLP
ETALAVPLIGKYLMFIMSLVTGVIVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILH
MSRADESEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPR
IGFGNNNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMF
IITPVMVLGTIFIFVMGNFNHPPAKPFEGDPFDYSSDHPRCA

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Family
the ligand-gated ion channel (TC 1.A.9) family
Function
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.

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Taxonomy ID
7787
TCDB ID
1.A.9.1.9
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Kingdom: Metazoa
Phylum: Chordata
Class: Chondrichthyes
Order: Torpediniformes
Family: Torpedinidae
Genus: Tetronarce
Species: Tetronarce californica
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Toxin BMLCL IC50
31 nM
[1], [2], [3]
 Toxin Info    Acidic phospholipase A2 Vur-PL2B IC50
>100 μM
[4], [5]
 Toxin Info    Azemiopsin IC50
0.03 - 0.18 μM
[6]
 Toxin Info    Basic phospholipase A2 vurtoxin IC50
0.26 μM
[4], [5]
 Toxin Info    Acidic phospholipase A2 CM-II IC50
1.2 μM
[5- 9]
References
Ref 1 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 2 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 3 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 4 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 5 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 6 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.
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.
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