ID Q8WSF8_APLCA Unreviewed; 236 AA. AC Q8WSF8; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 08-JUN-2016, entry version 84. DE SubName: Full=Soluble acetylcholine receptor {ECO:0000313|EMBL:AAL37251.1}; OS Aplysia californica (California sea hare). OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda; OC Heterobranchia; Euthyneura; Euopisthobranchia; Aplysiomorpha; OC Aplysioidea; Aplysiidae; Aplysia. OX NCBI_TaxID=6500 {ECO:0000313|EMBL:AAL37251.1}; RN [1] {ECO:0000213|PDB:2BYN, ECO:0000213|PDB:2BYP, ECO:0000213|PDB:2BYQ} RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 18-236, GLYCOSYLATION AT RP ASN-91, AND DISULFIDE BONDS. RX PubMed=16193063; DOI=10.1038/sj.emboj.7600828; RA Hansen S.B., Sulzenbacher G., Huxford T., Marchot P., Taylor P., RA Bourne Y.; RT "Structures of Aplysia AChBP complexes with nicotinic agonists and RT antagonists reveal distinctive binding interfaces and conformations."; RL EMBO J. 24:3635-3646(2005). RN [2] {ECO:0000213|PDB:2BR7, ECO:0000213|PDB:2BR8} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=15951818; DOI=10.1038/nsmb951; RA Celie P.H., Kasheverov I.E., Mordvintsev D.Y., Hogg R.C., RA van Nierop P., van Elk R., van Rossum-Fikkert S.E., Zhmak M.N., RA Bertrand D., Tsetlin V., Sixma T.K., Smit A.B.; RT "Crystal structure of nicotinic acetylcholine receptor homolog AChBP RT in complex with an alpha-conotoxin PnIA variant."; RL Nat. Struct. Mol. Biol. 12:582-588(2005). RN [3] {ECO:0000313|EMBL:AAL37251.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17190607; DOI=10.1016/j.cell.2006.09.052; RA Moroz L.L., Edwards J.R., Puthanveettil S.V., Kohn A.B., Ha T., RA Heyland A., Knudsen B., Sahni A., Yu F., Liu L., Jezzini S., RA Lovell P., Iannucculli W., Chen M., Nguyen T., Sheng H., Shaw R., RA Kalachikov S., Panchin Y.V., Farmerie W., Russo J.J., Ju J., RA Kandel E.R.; RT "Neuronal transcriptome of Aplysia: neuronal compartments and RT circuitry."; RL Cell 127:1453-1467(2006). RN [4] {ECO:0000213|PDB:2C9T} RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=16505382; DOI=10.1073/pnas.0507889103; RA Ulens C., Hogg R.C., Celie P.H., Bertrand D., Tsetlin V., Smit A.B., RA Sixma T.K.; RT "Structural determinants of selective alpha-conotoxin binding to a RT nicotinic acetylcholine receptor homolog AChBP."; RL Proc. Natl. Acad. Sci. U.S.A. 103:3615-3620(2006). RN [5] {ECO:0000213|PDB:2UZ6} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=17660751; DOI=10.1038/sj.emboj.7601785; RA Dutertre S., Ulens C., Buttner R., Fish A., van Elk R., Kendel Y., RA Hopping G., Alewood P.F., Schroeder C., Nicke A., Smit A.B., RA Sixma T.K., Lewis R.J.; RT "AChBP-targeted alpha-conotoxin correlates distinct binding RT orientations with nAChR subtype selectivity."; RL EMBO J. 26:3858-3867(2007). RN [6] {ECO:0000213|PDB:2PGZ, ECO:0000213|PDB:2PH9} RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 18-236, GLYCOSYLATION AT RP ASN-91, AND DISULFIDE BONDS. RX PubMed=17481657; DOI=10.1016/j.jmb.2007.03.067; RA Hansen S.B., Taylor P.; RT "Galanthamine and non-competitive inhibitor binding to ACh-binding RT protein: evidence for a binding site on non-alpha-subunit interfaces RT of heteromeric neuronal nicotinic receptors."; RL J. Mol. Biol. 369:895-901(2007). RN [7] {ECO:0000213|PDB:3GUA} RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 18-225, AND DISULFIDE BONDS. RX PubMed=18940802; DOI=10.1074/jbc.C800194200; RA Hansen S.B., Wang H.L., Taylor P., Sine S.M.; RT "An ion selectivity filter in the extracellular domain of Cys-loop RT receptors reveals determinants for ion conductance."; RL J. Biol. Chem. 283:36066-36070(2008). RN [8] {ECO:0000213|PDB:3C79, ECO:0000213|PDB:3C84} RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 18-236, AND DISULFIDE BONDS. RX PubMed=18477694; DOI=10.1073/pnas.0802197105; RA Talley T.T., Harel M., Hibbs R.E., Radic Z., Tomizawa M., Casida J.E., RA Taylor P.; RT "Atomic interactions of neonicotinoid agonists with AChBP: molecular RT recognition of the distinctive electronegative pharmacophore."; RL Proc. Natl. Acad. Sci. U.S.A. 105:7606-7611(2008). RN [9] {ECO:0000213|PDB:2WN9, ECO:0000213|PDB:2WNC, ECO:0000213|PDB:2WNJ} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 18-236, GLYCOSYLATION AT RP ASN-91, AND DISULFIDE BONDS. RX PubMed=19696737; DOI=10.1038/emboj.2009.227; RA Hibbs R.E., Sulzenbacher G., Shi J., Talley T.T., Conrod S., Kem W.R., RA Taylor P., Marchot P., Bourne Y.; RT "Structural determinants for interaction of partial agonists with RT acetylcholine binding protein and neuronal alpha7 nicotinic RT acetylcholine receptor."; RL EMBO J. 28:3040-3051(2009). RN [10] {ECO:0000213|PDB:2W8F, ECO:0000213|PDB:2W8G, ECO:0000213|PDB:2Y7Y} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=19331415; DOI=10.1021/jm801400g; RA Ulens C., Akdemir A., Jongejan A., van Elk R., Bertrand S., RA Perrakis A., Leurs R., Smit A.B., Sixma T.K., Bertrand D., RA de Esch I.J.; RT "Use of acetylcholine binding protein in the search for novel alpha7 RT nicotinic receptor ligands. In silico docking, pharmacological RT screening, and X-ray analysis."; RL J. Med. Chem. 52:2372-2383(2009). RN [11] {ECO:0000213|PDB:4ZJS} RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 48-77 AND 99-236, AND RP DISULFIDE BONDS. RX PubMed=19890000; DOI=10.1523/JNEUROSCI.2833-09.2009; RA Luo J., Taylor P., Losen M., de Baets M.H., Shelton G.D., RA Lindstrom J.; RT "Main immunogenic region structure promotes binding of conformation- RT dependent myasthenia gravis autoantibodies, nicotinic acetylcholine RT receptor conformation maturation, and agonist sensitivity."; RL J. Neurosci. 29:13898-13908(2009). RN [12] {ECO:0000213|PDB:2WZY, ECO:0000213|PDB:2X00} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-236, AND DISULFIDE BONDS. RX PubMed=20224036; DOI=10.1073/pnas.0912372107; RA Bourne Y., Radic Z., Araoz R., Talley T.T., Benoit E., Servent D., RA Taylor P., Molgo J., Marchot P.; RT "Structural determinants in phycotoxins and AChBP conferring high RT affinity binding and nicotinic AChR antagonism."; RL Proc. Natl. Acad. Sci. U.S.A. 107:6076-6081(2010). RN [13] {ECO:0000213|PDB:3PEO} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 18-236, AND DISULFIDE BONDS. RA Talley T.T., Harel M., Yamauchi G.J., Radic Z., Hansen S., Huxford T., RA Taylor P.W.; RT "The curare alkaloids: analyzing the poses of complexes with the RT acetylcholine binding protein in relation to structure and binding RT energetics."; RL Submitted (OCT-2010) to the PDB data bank. RN [14] {ECO:0000213|PDB:3PMZ} RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 18-236 IN COMPLEX WITH RP MAGNESIUM, AND DISULFIDE BONDS. RA Talley T.T., Harel M., Yamauchi J.G., Radic Z., Hansen S., Huxford T., RA Taylor P.W.; RT "The Curare Alkaloids: Analyzing the Poses of Complexes with the RT Acetylcholine Binding Protein in Relation to Structure and Binding RT Energies."; RL Submitted (NOV-2010) to the PDB data bank. RN [15] {ECO:0000213|PDB:2XNT, ECO:0000213|PDB:2XNU, ECO:0000213|PDB:2XNV} RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=21920761; DOI=10.1016/j.bmc.2011.08.028; RA Akdemir A., Rucktooa P., Jongejan A., Elk R.v., Bertrand S., RA Sixma T.K., Bertrand D., Smit A.B., Leurs R., de Graaf C., RA de Esch I.J.; RT "Acetylcholine binding protein (AChBP) as template for hierarchical in RT silico screening procedures to identify structurally novel ligands for RT the nicotinic receptors."; RL Bioorg. Med. Chem. 19:6107-6119(2011). RN [16] {ECO:0000213|PDB:2Y54, ECO:0000213|PDB:2Y56, ECO:0000213|PDB:2Y57} RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=21322593; DOI=10.1021/ja110571r; RA Edink E., Rucktooa P., Retra K., Akdemir A., Nahar T., Zuiderveld O., RA van Elk R., Janssen E., van Nierop P., van Muijlwijk-Koezen J., RA Smit A.B., Sixma T.K., Leurs R., de Esch I.J.; RT "Fragment growing induces conformational changes in acetylcholine- RT binding protein: a structural and thermodynamic analysis."; RL J. Am. Chem. Soc. 133:5363-5371(2011). RN [17] {ECO:0000213|PDB:2XZ5, ECO:0000213|PDB:2XZ6} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=21115477; DOI=10.1074/jbc.M110.188730; RA Brams M., Gay E.A., Saez J.C., Guskov A., van Elk R., RA van der Schors R.C., Peigneur S., Tytgat J., Strelkov S.V., Smit A.B., RA Yakel J.L., Ulens C.; RT "Crystal structures of a cysteine-modified mutant in loop D of RT acetylcholine-binding protein."; RL J. Biol. Chem. 286:4420-4428(2011). RN [18] {ECO:0000213|PDB:3SH1, ECO:0000213|PDB:3SIO, ECO:0000213|PDB:3T4M} RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 18-236, GLYCOSYLATION AT RP ASN-91, AND DISULFIDE BONDS. RX PubMed=22009746; DOI=10.1074/jbc.M111.286583; RA Nemecz A., Taylor P.; RT "Creating an alpha7 nicotinic acetylcholine recognition domain from RT the acetylcholine-binding protein: crystallographic and ligand RT selectivity analyses."; RL J. Biol. Chem. 286:42555-42565(2011). RN [19] {ECO:0000213|PDB:2XYS, ECO:0000213|PDB:2XYT} RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=21468359; DOI=10.1371/journal.pbio.1001034; RA Brams M., Pandya A., Kuzmin D., van Elk R., Krijnen L., Yakel J.L., RA Tsetlin V., Smit A.B., Ulens C.; RT "A structural and mutagenic blueprint for molecular recognition of RT strychnine and d-tubocurarine by different cys-loop receptors."; RL PLoS Biol. 9:e1001034-e1001034(2011). RN [20] {ECO:0000213|PDB:4DBM} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 18-236, GLYCOSYLATION AT RP ASN-91, AND DISULFIDE BONDS. RX PubMed=22394239; DOI=10.1021/ja3001858; RA Grimster N.P., Stump B., Fotsing J.R., Weide T., Talley T.T., RA Yamauchi J.G., Nemecz A., Kim C., Ho K.Y., Sharpless K.B., Taylor P., RA Fokin V.V.; RT "Generation of candidate ligands for nicotinic acetylcholine receptors RT via in situ click chemistry with a soluble acetylcholine binding RT protein template."; RL J. Am. Chem. Soc. 134:6732-6740(2012). RN [21] {ECO:0000213|PDB:4AFT, ECO:0000213|PDB:4BQT} RP X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=22553201; DOI=10.1074/jbc.M112.360347; RA Rucktooa P., Haseler C.A., van Elk R., Smit A.B., Gallagher T., RA Sixma T.K.; RT "Structural characterization of binding mode of smoking cessation RT drugs to nicotinic acetylcholine receptors through study of ligand RT complexes with acetylcholine-binding protein."; RL J. Biol. Chem. 287:23283-23293(2012). RN [22] {ECO:0000213|PDB:4EZ1} RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 18-236, AND DISULFIDE BONDS. RA Filchakova O.M., Talley T.T., Reger A.S., Kim C., Ho K., Han K., RA Taylor P., McIntosh J.M.; RT "Pairwise interaction of alpha-conotoxin BuIA Pro6 with the beta RT subunit of nicotinic acetylcholine receptor."; RL Submitted (MAY-2012) to the PDB data bank. RN [23] {ECO:0000213|PDB:4FRR} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 18-225, AND DISULFIDE BONDS. RA Mukhopadhyay S., Mesecar A.D.; RT "X-ray structure of Acetylcholine binding protein from Aplysia RT californica in presence of 3-((S)-azetidin-2-ylmethoxy)-5-((1S,2R)-2- RT (2-methoxyethyl)cyclopropyl)pyridine."; RL Submitted (JUN-2012) to the PDB data bank. RN [24] {ECO:0000213|PDB:2YMD, ECO:0000213|PDB:2YME} RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 20-231, GLYCOSYLATION AT RP ASN-91, AND DISULFIDE BONDS. RX PubMed=23196367; DOI=10.1038/embor.2012.189; RA Kesters D., Thompson A.J., Brams M., van Elk R., Spurny R., RA Geitmann M., Villalgordo J.M., Guskov A., Danielson U.H., Lummis S.C., RA Smit A.B., Ulens C.; RT "Structural basis of ligand recognition in 5-HT3 receptors."; RL EMBO Rep. 14:49-56(2013). RN [25] {ECO:0000213|PDB:4BFQ} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-236, AND DISULFIDE BONDS. RX PubMed=23695669; DOI=10.1038/NCOMMS2900; RA Stornaiuolo M., De Kloe G.E., Rucktooa P., Fish A., van Elk R., RA Edink E.S., Bertrand D., Smit A.B., de Esch I.J., Sixma T.K.; RT "Assembly of a pi-pi stack of ligands in the binding site of an RT acetylcholine-binding protein."; RL Nat. Commun. 4:1875-1875(2013). RN [26] {ECO:0000213|PDB:4WV9} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 18-224, AND DISULFIDE BONDS. RA Talley T.T.; RT "Crystal structure of acetylcholine binding protein (AChBP) from RT Aplysia Californica in complex with click chemistry compound."; RL Submitted (NOV-2014) to the PDB data bank. RN [27] {ECO:0000213|PDB:5AIN} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 20-231, AND DISULFIDE BONDS. RX PubMed=25648658; DOI=10.1021/CN500369H; RA Price K.L., Lillestol R.K., Ulens C., Lummis S.C.; RT "Varenicline Interactions at the 5-HT3 Receptor Ligand Binding Site RT are Revealed by 5-HTBP."; RL ACS Chem. Neurosci. 6:1151-1157(2015). RN [28] {ECO:0000213|PDB:4XHE, ECO:0000213|PDB:4XK9} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 18-225, AND DISULFIDE BONDS. RX PubMed=26004441; DOI=10.1016/j.str.2015.04.009; RA Bourne Y., Sulzenbacher G., Radic Z., Araoz R., Reynaud M., Benoit E., RA Zakarian A., Servent D., Molgo J., Taylor P., Marchot P.; RT "Marine Macrocyclic Imines, Pinnatoxins A and G: Structural RT Determinants and Functional Properties to Distinguish Neuronal alpha7 RT from Muscle alpha1(2)betagammadelta nAChRs."; RL Structure 23:1106-1115(2015). RN [29] {ECO:0000213|PDB:4ZK4} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 18-198 AND 215-236, AND RP DISULFIDE BONDS. RA Bobango J., Wu J., Talley T.T.; RT "Crystal structure of a chimeric acetylcholine binding protein from RT Aplysia californica (Ac-AChBP) containing loop C from the human alpha RT 3 nicotinic acetylcholine receptor in complex with 7-(5-isopropoxy- RT pyridin-3-yl)-1-methyl-1,7-diaza-spiro[4.4]nonane."; RL Submitted (APR-2015) to the PDB data bank. RN [30] {ECO:0000213|PDB:5BRX, ECO:0000213|PDB:5BW2} RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 18-236, AND DISULFIDE BONDS. RA Bobango J., Sankaran B., Park J.F., Wu J., Talley T.T.; RT "Comparisons of Binding Affinities for Neuronal Nicotinic Receptors RT (NNRs) and AChBPs."; RL Submitted (JUN-2015) to the PDB data bank. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF322877; AAL37251.1; -; mRNA. DR RefSeq; NP_001191488.1; NM_001204559.1. DR UniGene; Acl.89; -. DR PDB; 2BR7; X-ray; 3.00 A; A/B/C/D/E=20-236. DR PDB; 2BR8; X-ray; 2.40 A; A/B/C/D/E=20-236. DR PDB; 2BYN; X-ray; 2.02 A; A/B/C/D/E=18-236. DR PDB; 2BYP; X-ray; 2.07 A; A/B/C/D/E=18-225. DR PDB; 2BYQ; X-ray; 3.40 A; A/B/C/D/E=18-236. DR PDB; 2BYR; X-ray; 2.45 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 2BYS; X-ray; 2.05 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 2C9T; X-ray; 2.25 A; A/B/C/D/E/F/G/H/I/J=20-236. DR PDB; 2PGZ; X-ray; 1.76 A; A/B/C/D/E=18-236. DR PDB; 2PH9; X-ray; 2.88 A; A/B/C/D/E=18-236. DR PDB; 2UZ6; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=20-236. DR PDB; 2W8F; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=20-236. DR PDB; 2W8G; X-ray; 2.60 A; A/B/C/D/E=20-236. DR PDB; 2WN9; X-ray; 1.75 A; A/B/C/D/E=18-236. DR PDB; 2WNC; X-ray; 2.20 A; A/B/C/D/E=18-236. DR PDB; 2WNJ; X-ray; 1.80 A; A/B/C/D/E=18-236. DR PDB; 2WNL; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 2WZY; X-ray; 2.51 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 2X00; X-ray; 2.40 A; A/B/C/D/E=18-236. DR PDB; 2XNT; X-ray; 3.21 A; A/B/C/D/E/F/G/H/I/J=1-236. DR PDB; 2XNU; X-ray; 2.55 A; A/B/C/D/E=1-236. DR PDB; 2XNV; X-ray; 2.44 A; A/B/C/D/E/F/G/H/I/J=1-236. DR PDB; 2XYS; X-ray; 1.91 A; A/B/C/D/E=20-236. DR PDB; 2XYT; X-ray; 2.05 A; A/B/C/D/E/F/G/H/I/J=20-236. DR PDB; 2XZ5; X-ray; 2.80 A; A/B/C/D/E=20-236. DR PDB; 2XZ6; X-ray; 3.14 A; A/B/C/D/E/F/G/H/I/J=20-236. DR PDB; 2Y54; X-ray; 3.65 A; A/B/C/D/E=20-236. DR PDB; 2Y56; X-ray; 3.59 A; A/B/C/D/E=20-236. DR PDB; 2Y57; X-ray; 3.30 A; A/B/C/D/E=20-236. DR PDB; 2Y58; X-ray; 3.25 A; A/B/C/D/E=20-236. DR PDB; 2Y7Y; X-ray; 1.90 A; A/B/C/D/E=20-236. DR PDB; 2YMD; X-ray; 1.96 A; A/B/C/D/E/F/G/H/I/J=20-231. DR PDB; 2YME; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=20-224. DR PDB; 3C79; X-ray; 2.48 A; A/B/C/D/E=18-236. DR PDB; 3C84; X-ray; 1.94 A; A/B/C/D/E=18-236. DR PDB; 3GUA; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J=18-225. DR PDB; 3PEO; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 3PMZ; X-ray; 2.44 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 3SH1; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 3SIO; X-ray; 2.32 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 3T4M; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 4AFT; X-ray; 3.20 A; A/B/C/D/E=20-236. DR PDB; 4BFQ; X-ray; 2.40 A; A/B/C/D/E=20-236. DR PDB; 4BQT; X-ray; 2.88 A; A/B/C/D/E=20-236. DR PDB; 4DBM; X-ray; 2.30 A; A/B/C/D/E=18-236. DR PDB; 4EZ1; X-ray; 2.49 A; A/B/C/D/E=18-236. DR PDB; 4FRR; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=18-225. DR PDB; 4WV9; X-ray; 2.00 A; A/B/C/D/E=18-224. DR PDB; 4XHE; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J=18-225. DR PDB; 4XK9; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 4ZJS; X-ray; 2.23 A; A/B/C/D/E=48-77, A/B/C/D/E=99-236. DR PDB; 4ZK4; X-ray; 1.90 A; A/B/C/D/E=18-198, A/B/C/D/E=215-236. DR PDB; 5AIN; X-ray; 2.30 A; A/B/C/D/E=20-231. DR PDB; 5BRX; X-ray; 2.05 A; A/B/C/D/E/F/G/H/I/J=18-236. DR PDB; 5BW2; X-ray; 2.27 A; A/B/C/D/E=18-236. DR PDBsum; 2BR7; -. DR PDBsum; 2BR8; -. DR PDBsum; 2BYN; -. DR PDBsum; 2BYP; -. DR PDBsum; 2BYQ; -. DR PDBsum; 2BYR; -. DR PDBsum; 2BYS; -. DR PDBsum; 2C9T; -. DR PDBsum; 2PGZ; -. DR PDBsum; 2PH9; -. DR PDBsum; 2UZ6; -. DR PDBsum; 2W8F; -. DR PDBsum; 2W8G; -. DR PDBsum; 2WN9; -. DR PDBsum; 2WNC; -. DR PDBsum; 2WNJ; -. DR PDBsum; 2WNL; -. DR PDBsum; 2WZY; -. DR PDBsum; 2X00; -. DR PDBsum; 2XNT; -. DR PDBsum; 2XNU; -. DR PDBsum; 2XNV; -. DR PDBsum; 2XYS; -. DR PDBsum; 2XYT; -. DR PDBsum; 2XZ5; -. DR PDBsum; 2XZ6; -. DR PDBsum; 2Y54; -. DR PDBsum; 2Y56; -. DR PDBsum; 2Y57; -. DR PDBsum; 2Y58; -. DR PDBsum; 2Y7Y; -. DR PDBsum; 2YMD; -. DR PDBsum; 2YME; -. DR PDBsum; 3C79; -. DR PDBsum; 3C84; -. DR PDBsum; 3GUA; -. DR PDBsum; 3PEO; -. DR PDBsum; 3PMZ; -. DR PDBsum; 3SH1; -. DR PDBsum; 3SIO; -. DR PDBsum; 3T4M; -. DR PDBsum; 4AFT; -. DR PDBsum; 4BFQ; -. DR PDBsum; 4BQT; -. DR PDBsum; 4DBM; -. DR PDBsum; 4EZ1; -. DR PDBsum; 4FRR; -. DR PDBsum; 4WV9; -. DR PDBsum; 4XHE; -. DR PDBsum; 4XK9; -. DR PDBsum; 4ZJS; -. DR PDBsum; 4ZK4; -. DR PDBsum; 5AIN; -. DR PDBsum; 5BRX; -. DR PDBsum; 5BW2; -. DR ProteinModelPortal; Q8WSF8; -. DR SMR; Q8WSF8; 18-226. DR DIP; DIP-46103N; -. DR MINT; MINT-7300724; -. DR BindingDB; Q8WSF8; -. DR ChEMBL; CHEMBL1944497; -. DR GeneID; 100533247; -. DR EvolutionaryTrace; Q8WSF8; -. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 2.70.170.10; -; 1. DR InterPro; IPR006202; Neur_chan_lig-bd. DR InterPro; IPR006201; Neur_channel. DR PANTHER; PTHR18945; PTHR18945; 1. DR Pfam; PF02931; Neur_chan_LBD; 1. DR SUPFAM; SSF63712; SSF63712; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2BR7, ECO:0000213|PDB:2BR8, KW ECO:0000213|PDB:2BYN, ECO:0000213|PDB:2BYP}; KW Magnesium {ECO:0000213|PDB:2WNL, ECO:0000213|PDB:3C84, KW ECO:0000213|PDB:3PMZ, ECO:0000213|PDB:3SH1}; KW Metal-binding {ECO:0000213|PDB:2WNL, ECO:0000213|PDB:3C84, KW ECO:0000213|PDB:3PMZ, ECO:0000213|PDB:3SH1}; KW Receptor {ECO:0000313|EMBL:AAL37251.1}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 236 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004316614. FT DOMAIN 35 222 Neur_chan_LBD. {ECO:0000259|Pfam: FT PF02931}. FT METAL 167 167 Magnesium 1. {ECO:0000213|PDB:3PMZ}. FT METAL 167 167 Magnesium 2. {ECO:0000213|PDB:3PMZ}. FT METAL 170 170 Magnesium 2. {ECO:0000213|PDB:3PMZ}. FT METAL 210 210 Magnesium 1. {ECO:0000213|PDB:3PMZ}. FT CARBOHYD 91 91 N-linked (GlcNAc...). {ECO:0000213|PDB: FT 2BYN, ECO:0000213|PDB:2BYP, FT ECO:0000213|PDB:2PGZ}. FT /FTId=CAR_5005390077. FT DISULFID 144 157 {ECO:0000213|PDB:2BR7, ECO:0000213|PDB: FT 2BR8, ECO:0000213|PDB:2BYN}. FT DISULFID 207 208 {ECO:0000213|PDB:2BR7, ECO:0000213|PDB: FT 2BR8, ECO:0000213|PDB:2BYN}. SQ SEQUENCE 236 AA; 26568 MW; 6D0DE487C46707BE CRC64; MLVSVYLALL VACVGQAHSQ ANLMRLKSDL FNRSPMYPGP TKDDPLTVTL GFTLQDIVKA DSSTNEVDLV YYEQQRWKLN SLMWDPNEYG NITDFRTSAA DIWTPDITAY SSTRPVQVLS PQIAVVTHDG SVMFIPAQRL SFMCDPTGVD SEEGATCAVK FGSWVYSGFE IDLKTDTDQV DLSSYYASSK YEILSATQTR QVQHYSCCPE PYIDVNLVVK FRERRAGNGF FRNLFD //