ID   ACHB_HUMAN              Reviewed;         501 AA.
AC   P11230; B7Z5H1; Q8IZ46; Q96FB8;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 3.
DT   27-MAR-2024, entry version 235.
DE   RecName: Full=Acetylcholine receptor subunit beta {ECO:0000305};
DE   Flags: Precursor;
GN   Name=CHRNB1 {ECO:0000312|HGNC:HGNC:1961}; Synonyms=ACHRB, CHRNB;
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] (ISOFORM 1).
RX   PubMed=2740233; DOI=10.1093/nar/17.11.4391;
RA   Beeson D.M.W., Brydson M., Newsom-Davis J.;
RT   "Nucleotide sequence of human muscle acetylcholine receptor beta-subunit.";
RL   Nucleic Acids Res. 17:4391-4391(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLY-32 AND
RP   TYR-124.
RC   TISSUE=Eye, and Muscle;
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   [5]
RP   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   [6]
RP   VARIANT CMS2A MET-285.
RX   PubMed=8651643; DOI=10.1002/ana.410390607;
RA   Gomez C.M., Maselli R., Gammack J., Lasalde J., Tamamizu S.,
RA   Cornblath D.R., Lehar M., McNamee M., Kuncl R.W.;
RT   "A beta-subunit mutation in the acetylcholine receptor channel gate causes
RT   severe slow-channel syndrome.";
RL   Ann. Neurol. 39:712-723(1996).
RN   [7]
RP   VARIANT CMS2A MET-289.
RX   PubMed=8872460; DOI=10.1093/hmg/5.9.1217;
RA   Engel A.G., Ohno K., Milone M., Wang H.-L., Nakano S., Bouzat C.,
RA   Pruitt J.N. II, Hutchinson D.O., Brengman J.M., Bren N., Sieb J.P.,
RA   Sine S.M.;
RT   "New mutations in acetylcholine receptor subunit genes reveal heterogeneity
RT   in the slow-channel congenital myasthenic syndrome.";
RL   Hum. Mol. Genet. 5:1217-1227(1996).
RN   [8]
RP   VARIANT CMS2C 449-GLU--GLU-451 DEL, AND CHARACTERIZATION OF VARIANT CMS2C
RP   449-GLU--GLU-451 DEL.
RX   PubMed=10562302; DOI=10.1172/jci8179;
RA   Quiram P.A., Ohno K., Milone M., Patterson M.C., Pruitt J.N. II,
RA   Brengman J.M., Sine S.M., Engel A.G.;
RT   "Mutation causing congenital myasthenia reveals acetylcholine receptor
RT   beta/delta subunit interaction essential for assembly.";
RL   J. Clin. Invest. 104:1403-1410(1999).
RN   [9]
RP   VARIANT CMS2A ALA-289, CHARACTERIZATION OF VARIANT CMS2A ALA-289, AND
RP   FUNCTION.
RX   PubMed=27375219; DOI=10.1002/humu.23043;
RA   Shen X.M., Okuno T., Milone M., Otsuka K., Takahashi K., Komaki H.,
RA   Giles E., Ohno K., Engel A.G.;
RT   "Mutations causing slow-channel myasthenia reveal that a valine ring in the
RT   channel pore of muscle AChR is optimized for stabilizing channel gating.";
RL   Hum. Mutat. 37:1051-1059(2016).
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       {ECO:0000269|PubMed:27375219}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000250|UniProtKB:P04758};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P04758};
CC   -!- SUBUNIT: Pentamer of two alpha chains, and one each of the beta, delta,
CC       and gamma (in immature muscle) or epsilon (in mature muscle) chains.
CC       The muscle heteropentamer composed of alpha-1, beta-1, delta, epsilon
CC       subunits interacts with the alpha-conotoxin ImII (PubMed:15609996).
CC       {ECO:0000269|PubMed:15609996}.
CC   -!- INTERACTION:
CC       P11230; Q9NWX5: ASB6; NbExp=3; IntAct=EBI-724218, EBI-6425205;
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P11230-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P11230-2; Sequence=VSP_056675;
CC   -!- DISEASE: Myasthenic syndrome, congenital, 2A, slow-channel (CMS2A)
CC       [MIM:616313]: A form of congenital myasthenic syndrome, a group of
CC       disorders characterized by failure of neuromuscular transmission,
CC       including pre-synaptic, synaptic, and post-synaptic disorders that are
CC       not of autoimmune origin. Clinical features are easy fatigability and
CC       muscle weakness affecting the axial and limb muscles (with hypotonia in
CC       early-onset forms), the ocular muscles (leading to ptosis and
CC       ophthalmoplegia), and the facial and bulbar musculature (affecting
CC       sucking and swallowing, and leading to dysphonia). The symptoms
CC       fluctuate and worsen with physical effort. CMS2A is a slow-channel
CC       myasthenic syndrome. It is caused by kinetic abnormalities of the AChR,
CC       resulting in prolonged AChR channel opening episodes, prolonged
CC       endplate currents, and depolarization block. This is associated with
CC       calcium overload, which may contribute to subsequent degeneration of
CC       the endplate and postsynaptic membrane. {ECO:0000269|PubMed:27375219,
CC       ECO:0000269|PubMed:8651643, ECO:0000269|PubMed:8872460}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Myasthenic syndrome, congenital, 2C, associated with
CC       acetylcholine receptor deficiency (CMS2C) [MIM:616314]: A form of
CC       congenital myasthenic syndrome, a group of disorders characterized by
CC       failure of neuromuscular transmission, including pre-synaptic,
CC       synaptic, and post-synaptic disorders that are not of autoimmune
CC       origin. Clinical features are easy fatigability and muscle weakness
CC       affecting the axial and limb muscles (with hypotonia in early-onset
CC       forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and
CC       the facial and bulbar musculature (affecting sucking and swallowing,
CC       and leading to dysphonia). The symptoms fluctuate and worsen with
CC       physical effort. CMS2C is an autosomal recessive disorder of
CC       postsynaptic neuromuscular transmission, due to deficiency of AChR at
CC       the endplate that results in low amplitude of the miniature endplate
CC       potential and current. CMS2C is clinically characterized by early-onset
CC       muscle weakness with variable severity. {ECO:0000269|PubMed:10562302}.
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-1/CHRNB1 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X14830; CAA32939.1; -; mRNA.
DR   EMBL; AK298938; BAH12907.1; -; mRNA.
DR   EMBL; AC113189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC011371; AAH11371.1; -; mRNA.
DR   EMBL; BC023553; AAH23553.1; -; mRNA.
DR   CCDS; CCDS11106.1; -. [P11230-1]
DR   PIR; S04607; S04607.
DR   RefSeq; NP_000738.2; NM_000747.2. [P11230-1]
DR   AlphaFoldDB; P11230; -.
DR   SMR; P11230; -.
DR   BioGRID; 107562; 43.
DR   ComplexPortal; CPX-2179; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma.
DR   ComplexPortal; CPX-255; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon.
DR   IntAct; P11230; 2.
DR   STRING; 9606.ENSP00000304290; -.
DR   BindingDB; P11230; -.
DR   ChEMBL; CHEMBL1907588; -.
DR   ChEMBL; CHEMBL3885508; -.
DR   ChEMBL; CHEMBL4106145; -.
DR   DrugCentral; P11230; -.
DR   TCDB; 1.A.9.1.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR   GlyCosmos; P11230; 1 site, No reported glycans.
DR   GlyGen; P11230; 1 site.
DR   iPTMnet; P11230; -.
DR   PhosphoSitePlus; P11230; -.
DR   BioMuta; CHRNB1; -.
DR   DMDM; 21903373; -.
DR   EPD; P11230; -.
DR   jPOST; P11230; -.
DR   MassIVE; P11230; -.
DR   PaxDb; 9606-ENSP00000304290; -.
DR   PeptideAtlas; P11230; -.
DR   ProteomicsDB; 52725; -. [P11230-1]
DR   ProteomicsDB; 6694; -.
DR   Antibodypedia; 992; 286 antibodies from 35 providers.
DR   DNASU; 1140; -.
DR   Ensembl; ENST00000306071.7; ENSP00000304290.2; ENSG00000170175.11. [P11230-1]
DR   Ensembl; ENST00000536404.6; ENSP00000439209.2; ENSG00000170175.11. [P11230-2]
DR   Ensembl; ENST00000639692.2; ENSP00000492221.1; ENSG00000283946.2. [P11230-1]
DR   Ensembl; ENST00000639993.1; ENSP00000491113.1; ENSG00000283946.2. [P11230-2]
DR   GeneID; 1140; -.
DR   KEGG; hsa:1140; -.
DR   MANE-Select; ENST00000306071.7; ENSP00000304290.2; NM_000747.3; NP_000738.2.
DR   UCSC; uc002ghb.4; human. [P11230-1]
DR   AGR; HGNC:1961; -.
DR   CTD; 1140; -.
DR   DisGeNET; 1140; -.
DR   GeneCards; CHRNB1; -.
DR   GeneReviews; CHRNB1; -.
DR   HGNC; HGNC:1961; CHRNB1.
DR   HPA; ENSG00000170175; Tissue enhanced (skeletal muscle, tongue).
DR   MalaCards; CHRNB1; -.
DR   MIM; 100710; gene.
DR   MIM; 616313; phenotype.
DR   MIM; 616314; phenotype.
DR   neXtProt; NX_P11230; -.
DR   OpenTargets; ENSG00000170175; -.
DR   Orphanet; 98913; Postsynaptic congenital myasthenic syndromes.
DR   PharmGKB; PA26494; -.
DR   VEuPathDB; HostDB:ENSG00000170175; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000158661; -.
DR   HOGENOM; CLU_018074_1_4_1; -.
DR   InParanoid; P11230; -.
DR   OMA; PCILITV; -.
DR   OrthoDB; 5489962at2759; -.
DR   PhylomeDB; P11230; -.
DR   TreeFam; TF315605; -.
DR   PathwayCommons; P11230; -.
DR   SignaLink; P11230; -.
DR   BioGRID-ORCS; 1140; 14 hits in 1156 CRISPR screens.
DR   ChiTaRS; CHRNB1; human.
DR   GeneWiki; CHRNB1; -.
DR   GenomeRNAi; 1140; -.
DR   Pharos; P11230; Tclin.
DR   PRO; PR:P11230; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P11230; Protein.
DR   Bgee; ENSG00000170175; Expressed in gastrocnemius and 99 other cell types or tissues.
DR   ExpressionAtlas; P11230; baseline and differential.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; IMP:UniProtKB.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; NAS:UniProtKB.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; IEA:Ensembl.
DR   GO; GO:0045202; C:synapse; IMP:UniProtKB.
DR   GO; GO:0042166; F:acetylcholine binding; ISS:UniProtKB.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IBA:GO_Central.
DR   GO; GO:0015267; F:channel activity; IMP:UniProtKB.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; ISS:UniProtKB.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0035095; P:behavioral response to nicotine; IMP:UniProtKB.
DR   GO; GO:0006812; P:monoatomic cation transport; IMP:UniProtKB.
DR   GO; GO:0055001; P:muscle cell development; IMP:UniProtKB.
DR   GO; GO:0006936; P:muscle contraction; IMP:UniProtKB.
DR   GO; GO:0050877; P:nervous system process; IMP:UniProtKB.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:UniProtKB.
DR   GO; GO:0001941; P:postsynaptic membrane organization; IMP:UniProtKB.
DR   GO; GO:0042391; P:regulation of membrane potential; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:UniProtKB.
DR   CDD; cd19024; LGIC_ECD_nAChR_B1; 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:SF477; ACETYLCHOLINE RECEPTOR SUBUNIT BETA; 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; P11230; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Congenital myasthenic syndrome;
KW   Disease variant; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..23
FT   CHAIN           24..501
FT                   /note="Acetylcholine receptor subunit beta"
FT                   /id="PRO_0000000315"
FT   TOPO_DOM        24..244
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..469
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        470..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         390
FT                   /note="Phosphotyrosine; by Tyr-kinases"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        151..165
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..72
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056675"
FT   VARIANT         32
FT                   /note="E -> G (in dbSNP:rs17856697)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_048169"
FT   VARIANT         124
FT                   /note="D -> Y (in dbSNP:rs17856698)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_070842"
FT   VARIANT         285
FT                   /note="L -> M (in CMS2A; dbSNP:rs137852811)"
FT                   /evidence="ECO:0000269|PubMed:8651643"
FT                   /id="VAR_000287"
FT   VARIANT         289
FT                   /note="V -> A (in CMS2A; slow-channel mutation; increases
FT                   gating equilibrium constant by 33-fold, owing to increased
FT                   opening rate and decreased closing rate; no effect on the
FT                   choline dissociation rate constant)"
FT                   /evidence="ECO:0000269|PubMed:27375219"
FT                   /id="VAR_077363"
FT   VARIANT         289
FT                   /note="V -> M (in CMS2A; dbSNP:rs137852810)"
FT                   /evidence="ECO:0000269|PubMed:8872460"
FT                   /id="VAR_000288"
FT   VARIANT         449..451
FT                   /note="Missing (in CMS2C; impairs AChR assembly by
FT                   disrupting a specific interaction between beta and delta
FT                   subunits)"
FT                   /evidence="ECO:0000269|PubMed:10562302"
FT                   /id="VAR_017494"
FT   CONFLICT        15
FT                   /note="A -> P (in Ref. 1; CAA32939)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        210
FT                   /note="I -> N (in Ref. 1; CAA32939)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   501 AA;  56698 MW;  365CBFA795A51394 CRC64;
     MTPGALLMLL GALGAPLAPG VRGSEAEGRL REKLFSGYDS SVRPAREVGD RVRVSVGLIL
     AQLISLNEKD EEMSTKVYLD LEWTDYRLSW DPAEHDGIDS LRITAESVWL PDVVLLNNND
     GNFDVALDIS VVVSSDGSVR WQPPGIYRSS CSIQVTYFPF DWQNCTMVFS SYSYDSSEVS
     LQTGLGPDGQ GHQEIHIHEG TFIENGQWEI IHKPSRLIQP PGDPRGGREG QRQEVIFYLI
     IRRKPLFYLV NVIAPCILIT LLAIFVFYLP PDAGEKMGLS IFALLTLTVF LLLLADKVPE
     TSLSVPIIIK YLMFTMVLVT FSVILSVVVL NLHHRSPHTH QMPLWVRQIF IHKLPLYLRL
     KRPKPERDLM PEPPHCSSPG SGWGRGTDEY FIRKPPSDFL FPKPNRFQPE LSAPDLRRFI
     DGPNRAVALL PELREVVSSI SYIARQLQEQ EDHDALKEDW QFVAMVVDRL FLWTFIIFTS
     VGTLVIFLDA TYHLPPPDPF P
//