ACHE_HUMAN
ID ACHE_HUMAN Reviewed; 493 AA.
AC Q04844; D3DTK6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Acetylcholine receptor subunit epsilon;
DE Flags: Precursor;
GN Name=CHRNE; Synonyms=ACHRE;
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=Muscle fibroblast;
RX PubMed=7688301; DOI=10.1111/j.1432-1033.1993.tb18027.x;
RA Beeson D.M.W., Brydson M., Betty M., Jeremiah S., Povey S., Vincent A.,
RA Newsom-Davis J.;
RT "Primary structure of the human muscle acetylcholine receptor. cDNA cloning
RT of the gamma and epsilon subunits.";
RL Eur. J. Biochem. 215:229-238(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Abicht A., Stucka R., Lochmuller H.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP VARIANT CMS4A PHE-289.
RX PubMed=7538206; DOI=10.1212/wnl.45.5.982;
RA Gomez C.M., Gammack J.T.;
RT "A leucine-to-phenylalanine substitution in the acetylcholine receptor ion
RT channel in a family with the slow-channel syndrome.";
RL Neurology 45:982-985(1995).
RN [6]
RP VARIANT CMS4A PRO-284, AND CHARACTERIZATION OF VARIANT CMS4A PRO-284.
RX PubMed=7531341; DOI=10.1073/pnas.92.3.758;
RA Ohno K., Hutchinson D.O., Milone M., Brengman J.M., Bouzat C., Sine S.M.,
RA Engel A.G.;
RT "Congenital myasthenic syndrome caused by prolonged acetylcholine receptor
RT channel openings due to a mutation in the M2 domain of the epsilon
RT subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:758-762(1995).
RN [7]
RP VARIANT CMS4A PHE-289, AND CHARACTERIZATION OF VARIANT CMS4A PHE-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 VARIANTS CMS4B ARG-13; LEU-141 AND LEU-163, AND CHARACTERIZATION OF
RP VARIANTS CMS4B ARG-13; LEU-141 AND LEU-163.
RX PubMed=8755487; DOI=10.1016/s0896-6273(00)80289-5;
RA Ohno K., Wang H.-L., Milone M., Bren N., Brengman J.M., Nakano S.,
RA Quiram P., Pruitt J.N. II, Sine S.M., Engel A.G.;
RT "Congenital myasthenic syndrome caused by decreased agonist binding
RT affinity due to a mutation in the acetylcholine receptor epsilon subunit.";
RL Neuron 17:157-170(1996).
RN [9]
RP VARIANTS CMS4C LEU-167; LEU-265 AND TRP-331, AND CHARACTERIZATION OF
RP VARIANTS CMS4C LEU-167; LEU-265 AND TRP-331.
RX PubMed=9158150; DOI=10.1093/hmg/6.5.753;
RA Ohno K., Quiram P.A., Milone M., Wang H.-L., Harper M.C., Pruitt J.N. II,
RA Brengman J.M., Pao L., Fischbeck K.H., Crawford T.O., Sine S.M.,
RA Engel A.G.;
RT "Congenital myasthenic syndromes due to heteroallelic nonsense/missense
RT mutations in the acetylcholine receptor epsilon subunit gene:
RT identification and functional characterization of six new mutations.";
RL Hum. Mol. Genet. 6:753-766(1997).
RN [10]
RP VARIANT CMS4B PRO-431, AND CHARACTERIZATION OF VARIANT CMS4B PRO-431.
RX PubMed=10962020; DOI=10.1085/jgp.116.3.449;
RA Wang H.-L., Ohno K., Milone M., Brengman J.M., Evoli A., Batocchi A.-P.,
RA Middleton L.T., Christodoulou K., Engel A.G., Sine S.M.;
RT "Fundamental gating mechanism of nicotinic receptor channel revealed by
RT mutation causing a congenital myasthenic syndrome.";
RL J. Gen. Physiol. 116:449-462(2000).
RN [11]
RP VARIANTS CMS4A PRO-98 AND PHE-241.
RX PubMed=12141316; DOI=10.1212/wnl.59.2.162;
RA Croxen R., Hatton C., Shelley C., Brydson M., Chauplannaz G.,
RA Oosterhuis H., Vincent A., Newsom-Davis J., Colquhoun D., Beeson D.;
RT "Recessive inheritance and variable penetrance of slow-channel congenital
RT myasthenic syndromes.";
RL Neurology 59:162-168(2002).
RN [12]
RP VARIANT CMS4B ARG-75, AND CHARACTERIZATION OF VARIANT CMS4B ARG-75.
RX PubMed=22592360; DOI=10.1212/wnl.0b013e31825b5bda;
RA Shen X.M., Brengman J.M., Edvardson S., Sine S.M., Engel A.G.;
RT "Highly fatal fast-channel syndrome caused by AChR epsilon subunit mutation
RT at the agonist binding site.";
RL Neurology 79:449-454(2012).
RN [13]
RP VARIANT CMS4A ALA-285, CHARACTERIZATION OF VARIANT CMS4A ALA-285, 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 -!- 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 -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- DISEASE: Note=The muscle AChR is the major target antigen in the
CC autoimmune disease myasthenia gravis. Myasthenia gravis is
CC characterized by sporadic muscular fatigability and weakness, occurring
CC chiefly in muscles innervated by cranial nerves, and characteristically
CC improved by cholinesterase-inhibiting drugs.
CC -!- DISEASE: Myasthenic syndrome, congenital, 4A, slow-channel (CMS4A)
CC [MIM:605809]: 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. CMS4A 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:12141316,
CC ECO:0000269|PubMed:27375219, ECO:0000269|PubMed:7531341,
CC ECO:0000269|PubMed:7538206, 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, 4B, fast-channel (CMS4B)
CC [MIM:616324]: 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. CMS4B is a fast-channel
CC myasthenic syndrome. It is caused by kinetic abnormalities of the AChR,
CC resulting in brief opening and activity of the channel, with a rapid
CC decay in endplate current, failure to achieve threshold depolarization
CC of the endplate and consequent failure to fire an action potential.
CC {ECO:0000269|PubMed:10962020, ECO:0000269|PubMed:22592360,
CC ECO:0000269|PubMed:8755487}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Myasthenic syndrome, congenital, 4C, associated with
CC acetylcholine receptor deficiency (CMS4C) [MIM:608931]: 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. CMS4C 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. {ECO:0000269|PubMed:9158150}. Note=The disease
CC is caused by variants affecting the gene represented 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. Epsilon/CHRNE sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X66403; CAA47030.1; -; mRNA.
DR EMBL; AF105999; AAD24503.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90395.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90396.1; -; Genomic_DNA.
DR CCDS; CCDS11058.1; -.
DR PIR; S34775; S34775.
DR RefSeq; NP_000071.1; NM_000080.3.
DR AlphaFoldDB; Q04844; -.
DR SMR; Q04844; -.
DR BioGRID; 107567; 35.
DR ComplexPortal; CPX-255; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon.
DR STRING; 9606.ENSP00000293780; -.
DR BindingDB; Q04844; -.
DR ChEMBL; CHEMBL2484; -.
DR DrugCentral; Q04844; -.
DR TCDB; 1.A.9.1.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR GlyGen; Q04844; 2 sites.
DR iPTMnet; Q04844; -.
DR PhosphoSitePlus; Q04844; -.
DR BioMuta; CHRNE; -.
DR DMDM; 1168301; -.
DR jPOST; Q04844; -.
DR MaxQB; Q04844; -.
DR PaxDb; Q04844; -.
DR PeptideAtlas; Q04844; -.
DR PRIDE; Q04844; -.
DR ProteomicsDB; 58287; -.
DR Antibodypedia; 11366; 182 antibodies from 28 providers.
DR DNASU; 1145; -.
DR Ensembl; ENST00000649488.2; ENSP00000497829.1; ENSG00000108556.10.
DR GeneID; 1145; -.
DR KEGG; hsa:1145; -.
DR MANE-Select; ENST00000649488.2; ENSP00000497829.1; NM_000080.4; NP_000071.1.
DR UCSC; uc002fzk.2; human.
DR CTD; 1145; -.
DR DisGeNET; 1145; -.
DR GeneCards; CHRNE; -.
DR GeneReviews; CHRNE; -.
DR HGNC; HGNC:1966; CHRNE.
DR HPA; ENSG00000108556; Group enriched (heart muscle, pituitary gland).
DR MalaCards; CHRNE; -.
DR MIM; 100725; gene.
DR MIM; 254200; phenotype.
DR MIM; 605809; phenotype.
DR MIM; 608931; phenotype.
DR MIM; 616324; phenotype.
DR neXtProt; NX_Q04844; -.
DR OpenTargets; ENSG00000108556; -.
DR Orphanet; 98913; Postsynaptic congenital myasthenic syndromes.
DR PharmGKB; PA26498; -.
DR VEuPathDB; HostDB:ENSG00000108556; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000160933; -.
DR HOGENOM; CLU_018074_1_4_1; -.
DR InParanoid; Q04844; -.
DR OMA; ACNFIAD; -.
DR OrthoDB; 588360at2759; -.
DR PhylomeDB; Q04844; -.
DR TreeFam; TF315605; -.
DR PathwayCommons; Q04844; -.
DR Reactome; R-HSA-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR SignaLink; Q04844; -.
DR BioGRID-ORCS; 1145; 18 hits in 1075 CRISPR screens.
DR ChiTaRS; CHRNE; human.
DR GeneWiki; CHRNE; -.
DR GenomeRNAi; 1145; -.
DR Pharos; Q04844; Tclin.
DR PRO; PR:Q04844; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q04844; protein.
DR Bgee; ENSG00000108556; Expressed in right atrium auricular region and 94 other tissues.
DR ExpressionAtlas; Q04844; baseline and differential.
DR Genevisible; Q04844; HS.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; TAS:ProtInc.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; TAS:Reactome.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0015464; F:acetylcholine receptor activity; TAS:ProtInc.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IBA:GO_Central.
DR GO; GO:0008324; F:cation transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; TAS:ProtInc.
DR Gene3D; 1.20.58.390; -; 2.
DR Gene3D; 2.70.170.10; -; 1.
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 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 PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Congenital myasthenic syndrome; Disease variant;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..20
FT CHAIN 21..493
FT /note="Acetylcholine receptor subunit epsilon"
FT /id="PRO_0000000329"
FT TOPO_DOM 21..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..493
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 148..162
FT /evidence="ECO:0000250"
FT VARIANT 13
FT /note="G -> R (in CMS4B; impaired association with alpha
FT CHRNA1 subunit of AChR; dbSNP:rs372635387)"
FT /evidence="ECO:0000269|PubMed:8755487"
FT /id="VAR_021213"
FT VARIANT 18
FT /note="G -> V (in dbSNP:rs4790235)"
FT /id="VAR_048170"
FT VARIANT 75
FT /note="W -> R (in CMS4B; strongly reduces agonist affinity
FT and gating efficiency; dbSNP:rs193919341)"
FT /evidence="ECO:0000269|PubMed:22592360"
FT /id="VAR_071629"
FT VARIANT 98
FT /note="L -> P (in CMS4A; rare example of recessive
FT inheritance; dbSNP:rs28929768)"
FT /evidence="ECO:0000269|PubMed:12141316"
FT /id="VAR_019567"
FT VARIANT 141
FT /note="P -> L (in CMS4B; marked decrease in rate of AChR
FT channel opening; reduction in frequency of open channel
FT state and resistance to desensitization by ACh;
FT dbSNP:rs121909512)"
FT /evidence="ECO:0000269|PubMed:8755487"
FT /id="VAR_000289"
FT VARIANT 163
FT /note="S -> L (in CMS4B; fails to assemble with alpha
FT CHRNA1 subunit of AChR; dbSNP:rs121909516)"
FT /evidence="ECO:0000269|PubMed:8755487"
FT /id="VAR_021214"
FT VARIANT 167
FT /note="R -> L (in CMS4C; significantly reduced AChR
FT expression; dbSNP:rs121909514)"
FT /evidence="ECO:0000269|PubMed:9158150"
FT /id="VAR_000290"
FT VARIANT 241
FT /note="L -> F (in CMS4A; mild form with variable
FT penetrance; dbSNP:rs28999110)"
FT /evidence="ECO:0000269|PubMed:12141316"
FT /id="VAR_019568"
FT VARIANT 265
FT /note="P -> L (in CMS4C; prolongs burst open duration 2-
FT fold by slowing the rate of channel closing;
FT dbSNP:rs759226183)"
FT /evidence="ECO:0000269|PubMed:9158150"
FT /id="VAR_000291"
FT VARIANT 284
FT /note="T -> P (in CMS4A; markedly prolonged channel
FT openings in presence of agonist; as well as opening in the
FT absence of agonist; dbSNP:rs121909510)"
FT /evidence="ECO:0000269|PubMed:7531341"
FT /id="VAR_000292"
FT VARIANT 285
FT /note="V -> A (in CMS4A; slow-channel mutation; increases
FT gating equilibrium constant by 25-fold, owing to increased
FT opening rate and decreased closing rate; no effect on the
FT choline dissociation rate constant; dbSNP:rs1597618787)"
FT /evidence="ECO:0000269|PubMed:27375219"
FT /id="VAR_077364"
FT VARIANT 289
FT /note="L -> F (in CMS4A; slows rate of AChR channel closure
FT and increases apparent affinity for ACh; causes pathologic
FT channel openings even in the absence of ACh resulting in a
FT leaky channel; dbSNP:rs121909511)"
FT /evidence="ECO:0000269|PubMed:7538206,
FT ECO:0000269|PubMed:8872460"
FT /id="VAR_000293"
FT VARIANT 331
FT /note="R -> W (in CMS4C; shortens burst duration 2-fold by
FT slowing the rate of channel opening and speeding the rate
FT of ACh dissociation; has a mild fast-channel kinetic effect
FT on the AChR by shortening the long burst and increasing the
FT decay of the endplate current; dbSNP:rs121909515)"
FT /evidence="ECO:0000269|PubMed:9158150"
FT /id="VAR_000294"
FT VARIANT 431
FT /note="A -> P (in CMS4B; causes an increase in
FT distributions of rates for channel opening and closing
FT increasing the range of activation kinetics;
FT dbSNP:rs121909517)"
FT /evidence="ECO:0000269|PubMed:10962020"
FT /id="VAR_021215"
SQ SEQUENCE 493 AA; 54697 MW; A34AF273AF8B31FE CRC64;
MARAPLGVLL LLGLLGRGVG KNEELRLYHH LFNNYDPGSR PVREPEDTVT ISLKVTLTNL
ISLNEKEETL TTSVWIGIDW QDYRLNYSKD DFGGIETLRV PSELVWLPEI VLENNIDGQF
GVAYDANVLV YEGGSVTWLP PAIYRSVCAV EVTYFPFDWQ NCSLIFRSQT YNAEEVEFTF
AVDNDGKTIN KIDIDTEAYT ENGEWAIDFC PGVIRRHHGG ATDGPGETDV IYSLIIRRKP
LFYVINIIVP CVLISGLVLL AYFLPAQAGG QKCTVSINVL LAQTVFLFLI AQKIPETSLS
VPLLGRFLIF VMVVATLIVM NCVIVLNVSQ RTPTTHAMSP RLRHVLLELL PRLLGSPPPP
EAPRAASPPR RASSVGLLLR AEELILKKPR SELVFEGQRH RQGTWTAAFC QSLGAAAPEV
RCCVDAVNFV AESTRDQEAT GEEVSDWVRM GNALDNICFW AALVLFSVGS SLIFLGAYFN
RVPDLPYAPC IQP
