ACHB2_HUMAN
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 03-AUG-2022, entry version 217.
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 SMR; P17787; -.
DR BioGRID; 107563; 102.
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; 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 GlyGen; P17787; 3 sites.
DR PhosphoSitePlus; P17787; -.
DR BioMuta; CHRNB2; -.
DR DMDM; 113105; -.
DR MassIVE; P17787; -.
DR PaxDb; P17787; -.
DR PeptideAtlas; P17787; -.
DR PRIDE; P17787; -.
DR ABCD; P17787; 1 sequenced antibody.
DR Antibodypedia; 20401; 272 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 CTD; 1141; -.
DR DisGeNET; 1141; -.
DR GeneCards; CHRNB2; -.
DR GeneReviews; CHRNB2; -.
DR HGNC; HGNC:1962; CHRNB2.
DR HPA; ENSG00000160716; Tissue enhanced (brain, 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; 381858at2759; -.
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; 11 hits in 1073 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 159 other tissues.
DR ExpressionAtlas; P17787; baseline and differential.
DR Genevisible; P17787; HS.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098981; C:cholinergic synapse; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
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: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 cation-selective channel activity; IDA:UniProtKB.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:1901363; F:heterocyclic compound binding; IEA:Ensembl.
DR GO; GO:0015276; F:ligand-gated ion channel activity; TAS:DFLAT.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
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:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
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:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; NAS: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; IDA:ComplexPortal.
DR GO; GO:0007613; P:memory; IMP: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:0042391; P:regulation of membrane potential; IBA:GO_Central.
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 Gene3D; 1.20.58.390; -; 2.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR032932; CHRNB2.
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 PANTHER; PTHR18945; PTHR18945; 1.
DR PANTHER; PTHR18945:SF80; PTHR18945:SF80; 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; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
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
