ID   ACHB2_HUMAN             Reviewed;         502 AA.
AC   P17787; Q9UEH9;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   24-JAN-2024, entry version 225.
DE   RecName: Full=Neuronal acetylcholine receptor subunit beta-2;
DE   Flags: Precursor;
GN   Name=CHRNB2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=2377478; DOI=10.1093/nar/18.14.4272;
RA   Anand R., Lindstrom J.;
RT   "Nucleotide sequence of the human nicotinic acetylcholine receptor beta 2
RT   subunit gene.";
RL   Nucleic Acids Res. 18:4272-4272(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=8906617; DOI=10.1007/bf02736842;
RA   Elliott K.J., Ellis S.B., Berckhan K.J., Urrutia A., Chavez-Noriega L.E.,
RA   Johnson E.C., Velicelebi G., Harpold M.M.;
RT   "Comparative structure of human neuronal alpha 2-alpha 7 and beta 2-beta 4
RT   nicotinic acetylcholine receptor subunits and functional expression of the
RT   alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and beta 4 subunits.";
RL   J. Mol. Neurosci. 7:217-228(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Frontal cortex;
RX   PubMed=9009220; DOI=10.1016/s0014-5793(96)01383-x;
RA   Groot Kormelink P.J., Luyten W.H.M.L.;
RT   "Cloning and sequence of full-length cDNAs encoding the human neuronal
RT   nicotinic acetylcholine receptor (nAChR) subunits beta3 and beta4 and
RT   expression of seven nAChR subunits in the human neuroblastoma cell line SH-
RT   SY5Y and/or IMR-32.";
RL   FEBS Lett. 400:309-314(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9921897; DOI=10.1007/s004390050885;
RA   Rempel N., Heyers S., Engels H., Sleegers E., Steinlein O.K.;
RT   "The structures of the human neuronal nicotinic acetylcholine receptor
RT   beta2- and alpha3-subunit genes (CHRNB2 and CHRNA3).";
RL   Hum. Genet. 103:645-653(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10441742; DOI=10.1007/s003359901111;
RA   Lueders K.K., Elliott R.W., Marenholz I., Mischke D., DuPree M., Hamer D.;
RT   "Genomic organization and mapping of the human and mouse neuronal beta2-
RT   nicotinic acetylcholine receptor genes.";
RL   Mamm. Genome 10:900-905(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, SYNTHESIS OF 5-16, 3D-STRUCTURE MODELING, AND SUBUNIT.
RX   PubMed=15609996; DOI=10.1021/bi048918g;
RA   Ellison M., Gao F., Wang H.L., Sine S.M., McIntosh J.M., Olivera B.M.;
RT   "Alpha-conotoxins ImI and ImII target distinct regions of the human alpha7
RT   nicotinic acetylcholine receptor and distinguish human nicotinic receptor
RT   subtypes.";
RL   Biochemistry 43:16019-16026(2004).
RN   [8]
RP   INTERACTION WITH RIC3.
RX   PubMed=16120769; DOI=10.1124/mol.105.017459;
RA   Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R., Gibb A.J.,
RA   Millar N.S.;
RT   "RIC-3 enhances functional expression of multiple nicotinic acetylcholine
RT   receptor subtypes in mammalian cells.";
RL   Mol. Pharmacol. 68:1431-1438(2005).
RN   [9]
RP   INTERACTION WITH LYPD6.
RX   PubMed=27344019; DOI=10.1111/jnc.13718;
RA   Arvaniti M., Jensen M.M., Soni N., Wang H., Klein A.B., Thiriet N.,
RA   Pinborg L.H., Muldoon P.P., Wienecke J., Imad Damaj M., Kohlmeier K.A.,
RA   Gondre-Lewis M.C., Mikkelsen J.D., Thomsen M.S.;
RT   "Functional interaction between Lypd6 and nicotinic acetylcholine
RT   receptors.";
RL   J. Neurochem. 138:806-820(2016).
RN   [10]
RP   MUTAGENESIS OF PHE-197, AND SUBUNIT.
RX   PubMed=27493220; DOI=10.1073/pnas.1602619113;
RA   Kouvatsos N., Giastas P., Chroni-Tzartou D., Poulopoulou C., Tzartos S.J.;
RT   "Crystal structure of a human neuronal nAChR extracellular domain in
RT   pentameric assembly: Ligand-bound alpha2 homopentamer.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9635-9640(2016).
RN   [11]
RP   STRUCTURE BY NMR OF 231-486.
RX   PubMed=20441771; DOI=10.1016/j.bbamem.2010.04.014;
RA   Bondarenko V., Tillman T., Xu Y., Tang P.;
RT   "NMR structure of the transmembrane domain of the n-acetylcholine receptor
RT   beta2 subunit.";
RL   Biochim. Biophys. Acta 1798:1608-1614(2010).
RN   [12]
RP   STRUCTURE BY NMR OF 234-484, SUBUNIT, AND FUNCTION.
RX   PubMed=22361591; DOI=10.1016/j.bbamem.2012.02.008;
RA   Bondarenko V., Mowrey D., Tillman T., Cui T., Liu L.T., Xu Y., Tang P.;
RT   "NMR structures of the transmembrane domains of the alpha4beta2 nAChR.";
RL   Biochim. Biophys. Acta 1818:1261-1268(2012).
RN   [13]
RP   VARIANT ENFL3 LEU-287.
RX   PubMed=11062464; DOI=10.1038/81566;
RA   De Fusco M., Becchetti A., Patrignani A., Annesi G., Gambardella A.,
RA   Quattrone A., Ballabio A., Wanke E., Casari G.;
RT   "The nicotinic receptor beta-2 subunit is mutant in nocturnal frontal lobe
RT   epilepsy.";
RL   Nat. Genet. 26:275-276(2000).
RN   [14]
RP   VARIANT ENFL3 MET-287.
RX   PubMed=11104662; DOI=10.1086/316946;
RA   Phillips H.A., Favre I., Kirkpatrick M., Zuberi S.M., Goudie D.,
RA   Heron S.E., Scheffer I.E., Sutherland G.R., Berkovic S.F., Bertrand D.,
RA   Mulley J.C.;
RT   "CHRNB2 is the second acetylcholine receptor subunit associated with
RT   autosomal dominant nocturnal frontal lobe epilepsy.";
RL   Am. J. Hum. Genet. 68:225-231(2001).
RN   [15]
RP   VARIANT HIS-397.
RX   PubMed=11906688; DOI=10.1080/14622200110098419;
RA   Lueders K.K., Hu S., McHugh L., Myakishev M.V., Sirota L.A., Hamer D.H.;
RT   "Genetic and functional analysis of single nucleotide polymorphisms in the
RT   beta2-neuronal nicotinic acetylcholine receptor gene (CHRNB2).";
RL   Nicotine Tob. Res. 4:115-125(2002).
CC   -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC       extensive change in conformation that affects all subunits and leads to
CC       opening of an ion-conducting channel across the plasma membrane
CC       permeable to sodiun ions. {ECO:0000269|PubMed:22361591}.
CC   -!- SUBUNIT: Neuronal AChR is composed of two different types of subunits:
CC       alpha and beta. Beta-2 subunit can be combined to alpha-2, alpha-3 or
CC       alpha-4 to give rise to functional receptors, complexes with beta-2 may
CC       be heteropentamers. Alpha-2/4:beta-2 nAChR complexes are proposed to
CC       exist in two subtypes: LS (low agonist sensitivity) with a (alpha-
CC       2/4)3:(beta-2)2 and HS (high agonist sensitivity) with a (alpha-
CC       2/4)2:(beta-2)3 stoichiometry; the subtypes differ in their subunit
CC       binding interfaces which are involved in ligand binding
CC       (PubMed:27493220, PubMed:22361591). Interacts with RIC3; which is
CC       required for proper folding and assembly (PubMed:16120769). Interacts
CC       with LYPD6 (PubMed:27344019). The heteropentamer alpha-3-beta-2
CC       interacts with alpha-conotoxins BuIA, MII, PnIA and GID (By
CC       similarity). The heteropentamer alpha-3-beta-2 interacts with the
CC       alpha-conotoxins ImI and ImII (PubMed:15609996). The heteropentamer
CC       alpha-4-beta-2 interacts with the alpha-conotoxins PnIA, GID and MII
CC       (By similarity). {ECO:0000250|UniProtKB:P12390,
CC       ECO:0000269|PubMed:15609996, ECO:0000269|PubMed:16120769,
CC       ECO:0000269|PubMed:22361591, ECO:0000269|PubMed:27344019,
CC       ECO:0000305|PubMed:27493220}.
CC   -!- INTERACTION:
CC       P17787; P43681-1: CHRNA4; NbExp=4; IntAct=EBI-9008612, EBI-20716158;
CC       P17787; P30532: CHRNA5; NbExp=3; IntAct=EBI-9008612, EBI-6657490;
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- DISEASE: Epilepsy, nocturnal frontal lobe, 3 (ENFL3) [MIM:605375]: An
CC       autosomal dominant focal epilepsy characterized by nocturnal seizures
CC       with hyperkinetic automatisms and poorly organized stereotyped
CC       movements. {ECO:0000269|PubMed:11062464, ECO:0000269|PubMed:11104662}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. Beta-2/CHRNB2 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X53179; CAA37320.1; -; mRNA.
DR   EMBL; U62437; AAB40115.1; -; mRNA.
DR   EMBL; Y08415; CAA69692.1; -; mRNA.
DR   EMBL; AJ001935; CAA05108.1; -; Genomic_DNA.
DR   EMBL; AJ001936; CAA05108.1; JOINED; Genomic_DNA.
DR   EMBL; AJ001937; CAA05108.1; JOINED; Genomic_DNA.
DR   EMBL; AJ001938; CAA05108.1; JOINED; Genomic_DNA.
DR   EMBL; AJ001939; CAA05108.1; JOINED; Genomic_DNA.
DR   EMBL; AF077186; AAD45422.1; -; Genomic_DNA.
DR   EMBL; BC075040; AAH75040.1; -; mRNA.
DR   EMBL; BC075041; AAH75041.1; -; mRNA.
DR   CCDS; CCDS1070.1; -.
DR   PIR; S10505; S10505.
DR   RefSeq; NP_000739.1; NM_000748.2.
DR   PDB; 2K58; NMR; -; B=231-265.
DR   PDB; 2K59; NMR; -; B=264-291.
DR   PDB; 2KSR; NMR; -; A=231-330, A=453-486.
DR   PDB; 2LM2; NMR; -; A=231-330, A=458-485.
DR   PDB; 5KXI; X-ray; 3.94 A; B/C/E=26-355, B/C/E=446-502.
DR   PDB; 6CNJ; EM; 3.40 A; B/C/E=26-353, B/C/E=446-502.
DR   PDB; 6CNK; EM; 3.70 A; C/E=26-353, C/E=446-502.
DR   PDB; 6UR8; EM; 3.71 A; B/C/E=26-502.
DR   PDB; 6USF; EM; 3.87 A; B/C/E=26-502.
DR   PDBsum; 2K58; -.
DR   PDBsum; 2K59; -.
DR   PDBsum; 2KSR; -.
DR   PDBsum; 2LM2; -.
DR   PDBsum; 5KXI; -.
DR   PDBsum; 6CNJ; -.
DR   PDBsum; 6CNK; -.
DR   PDBsum; 6UR8; -.
DR   PDBsum; 6USF; -.
DR   AlphaFoldDB; P17787; -.
DR   EMDB; EMD-20857; -.
DR   EMDB; EMD-20863; -.
DR   EMDB; EMD-7535; -.
DR   EMDB; EMD-7536; -.
DR   SMR; P17787; -.
DR   BioGRID; 107563; 103.
DR   ComplexPortal; CPX-168; Neuronal nicotinic acetylcholine receptor complex, 3xalpha4-2xbeta2.
DR   ComplexPortal; CPX-187; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2.
DR   ComplexPortal; CPX-2170; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2.
DR   ComplexPortal; CPX-218; Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2.
DR   ComplexPortal; CPX-2180; Neuronal nicotinic acetylcholine receptor complex, 2xalpha4-3xbeta2.
DR   ComplexPortal; CPX-2192; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3.
DR   ComplexPortal; CPX-2193; Neuronal nicotinic acetylcholine receptor complex, alpha3-beta2.
DR   ComplexPortal; CPX-240; Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2.
DR   CORUM; P17787; -.
DR   IntAct; P17787; 6.
DR   STRING; 9606.ENSP00000357461; -.
DR   BindingDB; P17787; -.
DR   ChEMBL; CHEMBL1883; -.
DR   DrugBank; DB00572; Atropine.
DR   DrugBank; DB00237; Butabarbital.
DR   DrugBank; DB00565; Cisatracurium.
DR   DrugBank; DB09028; Cytisine.
DR   DrugBank; DB01245; Decamethonium.
DR   DrugBank; DB00514; Dextromethorphan.
DR   DrugBank; DB07720; Epibatidine.
DR   DrugBank; DB00898; Ethanol.
DR   DrugBank; DB00753; Isoflurane.
DR   DrugBank; DB00657; Mecamylamine.
DR   DrugBank; DB00333; Methadone.
DR   DrugBank; DB00184; Nicotine.
DR   DrugBank; DB00981; Physostigmine.
DR   DrugBank; DB05458; Pozanicline.
DR   DrugBank; DB05855; Rivanicline.
DR   DrugBank; DB05740; RPI-78M.
DR   DrugBank; DB00747; Scopolamine.
DR   DrugBank; DB00202; Succinylcholine.
DR   DrugBank; DB01273; Varenicline.
DR   DrugCentral; P17787; -.
DR   TCDB; 1.A.9.1.6; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR   GlyCosmos; P17787; 3 sites, No reported glycans.
DR   GlyGen; P17787; 3 sites.
DR   PhosphoSitePlus; P17787; -.
DR   BioMuta; CHRNB2; -.
DR   DMDM; 113105; -.
DR   MassIVE; P17787; -.
DR   PaxDb; 9606-ENSP00000357461; -.
DR   PeptideAtlas; P17787; -.
DR   ABCD; P17787; 1 sequenced antibody.
DR   Antibodypedia; 20401; 308 antibodies from 33 providers.
DR   DNASU; 1141; -.
DR   Ensembl; ENST00000368476.4; ENSP00000357461.3; ENSG00000160716.6.
DR   GeneID; 1141; -.
DR   KEGG; hsa:1141; -.
DR   MANE-Select; ENST00000368476.4; ENSP00000357461.3; NM_000748.3; NP_000739.1.
DR   AGR; HGNC:1962; -.
DR   CTD; 1141; -.
DR   DisGeNET; 1141; -.
DR   GeneCards; CHRNB2; -.
DR   GeneReviews; CHRNB2; -.
DR   HGNC; HGNC:1962; CHRNB2.
DR   HPA; ENSG00000160716; Group enriched (brain, pituitary gland, retina).
DR   MalaCards; CHRNB2; -.
DR   MIM; 118507; gene.
DR   MIM; 605375; phenotype.
DR   neXtProt; NX_P17787; -.
DR   OpenTargets; ENSG00000160716; -.
DR   Orphanet; 98784; Autosomal dominant nocturnal frontal lobe epilepsy.
DR   PharmGKB; PA115; -.
DR   VEuPathDB; HostDB:ENSG00000160716; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000158417; -.
DR   HOGENOM; CLU_018074_1_3_1; -.
DR   InParanoid; P17787; -.
DR   OrthoDB; 5489962at2759; -.
DR   PhylomeDB; P17787; -.
DR   TreeFam; TF315605; -.
DR   PathwayCommons; P17787; -.
DR   Reactome; R-HSA-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR   Reactome; R-HSA-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR   Reactome; R-HSA-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR   SignaLink; P17787; -.
DR   BioGRID-ORCS; 1141; 13 hits in 1158 CRISPR screens.
DR   ChiTaRS; CHRNB2; human.
DR   EvolutionaryTrace; P17787; -.
DR   GeneWiki; CHRNB2; -.
DR   GenomeRNAi; 1141; -.
DR   Pharos; P17787; Tclin.
DR   PRO; PR:P17787; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P17787; Protein.
DR   Bgee; ENSG00000160716; Expressed in cervix squamous epithelium and 160 other cell types or tissues.
DR   ExpressionAtlas; P17787; baseline and differential.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:UniProtKB.
DR   GO; GO:0098981; C:cholinergic synapse; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0044853; C:plasma membrane raft; ISS:ARUK-UCL.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; IEA:Ensembl.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0042166; F:acetylcholine binding; IMP:UniProtKB.
DR   GO; GO:0015464; F:acetylcholine receptor activity; IDA:UniProtKB.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IDA:UniProtKB.
DR   GO; GO:1901363; F:heterocyclic compound binding; IEA:Ensembl.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; TAS:DFLAT.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0050997; F:quaternary ammonium group binding; IEA:Ensembl.
DR   GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISS:ARUK-UCL.
DR   GO; GO:0008306; P:associative learning; ISS:UniProtKB.
DR   GO; GO:0042113; P:B cell activation; ISS:UniProtKB.
DR   GO; GO:0035095; P:behavioral response to nicotine; IMP:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; ISS:UniProtKB.
DR   GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR   GO; GO:0021771; P:lateral geniculate nucleus development; ISS:UniProtKB.
DR   GO; GO:0007612; P:learning; IMP:UniProtKB.
DR   GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR   GO; GO:0051899; P:membrane depolarization; ISS:UniProtKB.
DR   GO; GO:0007613; P:memory; IMP:UniProtKB.
DR   GO; GO:0006811; P:monoatomic ion transport; NAS:UniProtKB.
DR   GO; GO:0045759; P:negative regulation of action potential; ISS:UniProtKB.
DR   GO; GO:0050877; P:nervous system process; IMP:UniProtKB.
DR   GO; GO:0021631; P:optic nerve morphogenesis; ISS:UniProtKB.
DR   GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:UniProtKB.
DR   GO; GO:0033603; P:positive regulation of dopamine secretion; ISS:UniProtKB.
DR   GO; GO:0042320; P:regulation of circadian sleep/wake cycle, REM sleep; ISS:UniProtKB.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB.
DR   GO; GO:0042053; P:regulation of dopamine metabolic process; ISS:UniProtKB.
DR   GO; GO:0014059; P:regulation of dopamine secretion; ISS:UniProtKB.
DR   GO; GO:0051963; P:regulation of synapse assembly; ISS:UniProtKB.
DR   GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; ISS:UniProtKB.
DR   GO; GO:1905144; P:response to acetylcholine; ISS:ARUK-UCL.
DR   GO; GO:0042220; P:response to cocaine; ISS:UniProtKB.
DR   GO; GO:0045471; P:response to ethanol; ISS:UniProtKB.
DR   GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR   GO; GO:0035094; P:response to nicotine; IDA:UniProtKB.
DR   GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR   GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR   GO; GO:0006939; P:smooth muscle contraction; ISS:UniProtKB.
DR   GO; GO:0035176; P:social behavior; ISS:UniProtKB.
DR   GO; GO:0060084; P:synaptic transmission involved in micturition; ISS:UniProtKB.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; ISS:UniProtKB.
DR   GO; GO:0021562; P:vestibulocochlear nerve development; ISS:UniProtKB.
DR   GO; GO:0008542; P:visual learning; IMP:UniProtKB.
DR   GO; GO:0007601; P:visual perception; ISS:UniProtKB.
DR   CDD; cd19025; LGIC_ECD_nAChR_B2; 1.
DR   CDD; cd19064; LGIC_TM_nAChR; 1.
DR   Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR   Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 2.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR   InterPro; IPR038050; Neuro_actylchol_rec.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945:SF901; NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT BETA-2; 1.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00254; NICOTINICR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR   SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
DR   Genevisible; P17787; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Disease variant; Disulfide bond; Epilepsy;
KW   Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW   Membrane; Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
KW   Synapse; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..502
FT                   /note="Neuronal acetylcholine receptor subunit beta-2"
FT                   /id="PRO_0000000379"
FT   TOPO_DOM        26..233
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        285..299
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        322..458
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        459..478
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            84
FT                   /note="Key residue that may interfere with effective access
FT                   of the conotoxin BuIA to the channel binding site"
FT                   /evidence="ECO:0000250|UniProtKB:P12390"
FT   SITE            136
FT                   /note="Key residue for a rapid dissociation (K(off)) from
FT                   the conotoxin BuIA"
FT                   /evidence="ECO:0000250|UniProtKB:P12390"
FT   SITE            144
FT                   /note="Key residue for a rapid dissociation (K(off)) from
FT                   the conotoxin BuIA"
FT                   /evidence="ECO:0000250|UniProtKB:P12390"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        485
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        155..169
FT                   /evidence="ECO:0000250"
FT   VARIANT         287
FT                   /note="V -> L (in ENFL3; dbSNP:rs74315291)"
FT                   /evidence="ECO:0000269|PubMed:11062464"
FT                   /id="VAR_012714"
FT   VARIANT         287
FT                   /note="V -> M (in ENFL3; approximately 10-fold increase in
FT                   acetylcholine sensitivity; dbSNP:rs74315291)"
FT                   /evidence="ECO:0000269|PubMed:11104662"
FT                   /id="VAR_012715"
FT   VARIANT         397
FT                   /note="Q -> H (in dbSNP:rs55685423)"
FT                   /evidence="ECO:0000269|PubMed:11906688"
FT                   /id="VAR_021564"
FT   MUTAGEN         197
FT                   /note="F->Y: Increases ligand activation in LS and HS nAChR
FT                   subtypes."
FT                   /evidence="ECO:0000269|PubMed:27493220"
FT   CONFLICT        26
FT                   /note="T -> A (in Ref. 4; CAA05108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        426
FT                   /note="E -> A (in Ref. 4; CAA05108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        446
FT                   /note="S -> SVR (in Ref. 4; CAA05108)"
FT                   /evidence="ECO:0000305"
FT   HELIX           28..36
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   TURN            39..41
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   TURN            51..53
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   STRAND          56..71
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   TURN            72..75
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   STRAND          76..88
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   TURN            96..101
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   STRAND          104..107
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   TURN            109..111
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   STRAND          118..122
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   STRAND          135..138
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   STRAND          141..145
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   STRAND          166..174
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   STRAND          182..186
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   STRAND          201..207
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   STRAND          209..214
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   TURN            216..218
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   STRAND          222..232
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   HELIX           235..249
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   HELIX           250..254
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   TURN            255..257
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   HELIX           260..262
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   HELIX           265..286
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   HELIX           289..291
FT                   /evidence="ECO:0007829|PDB:2LM2"
FT   HELIX           296..322
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   TURN            326..328
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   HELIX           333..342
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   HELIX           344..346
FT                   /evidence="ECO:0007829|PDB:6CNJ"
FT   HELIX           447..475
FT                   /evidence="ECO:0007829|PDB:6CNJ"
SQ   SEQUENCE   502 AA;  57019 MW;  7EEDEF6ADFDC9F23 CRC64;
     MARRCGPVAL LLGFGLLRLC SGVWGTDTEE RLVEHLLDPS RYNKLIRPAT NGSELVTVQL
     MVSLAQLISV HEREQIMTTN VWLTQEWEDY RLTWKPEEFD NMKKVRLPSK HIWLPDVVLY
     NNADGMYEVS FYSNAVVSYD GSIFWLPPAI YKSACKIEVK HFPFDQQNCT MKFRSWTYDR
     TEIDLVLKSE VASLDDFTPS GEWDIVALPG RRNENPDDST YVDITYDFII RRKPLFYTIN
     LIIPCVLITS LAILVFYLPS DCGEKMTLCI SVLLALTVFL LLISKIVPPT SLDVPLVGKY
     LMFTMVLVTF SIVTSVCVLN VHHRSPTTHT MAPWVKVVFL EKLPALLFMQ QPRHHCARQR
     LRLRRRQRER EGAGALFFRE APGADSCTCF VNRASVQGLA GAFGAEPAPV AGPGRSGEPC
     GCGLREAVDG VRFIADHMRS EDDDQSVSED WKYVAMVIDR LFLWIFVFVC VFGTIGMFLQ
     PLFQNYTTTT FLHSDHSAPS SK
//