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Acetylcholine receptor subunit epsilon

 ACHE_HUMAN              Reviewed;         493 AA.
Q04844; D3DTK6;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
27-SEP-2017, entry version 168.
RecName: Full=Acetylcholine receptor subunit epsilon;
Flags: Precursor;
Name=CHRNE; Synonyms=ACHRE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Muscle fibroblast;
PubMed=7688301; DOI=10.1111/j.1432-1033.1993.tb18027.x;
Beeson D.M.W., Brydson M., Betty M., Jeremiah S., Povey S.,
Vincent A., Newsom-Davis J.;
"Primary structure of the human muscle acetylcholine receptor. cDNA
cloning of the gamma and epsilon subunits.";
Eur. J. Biochem. 215:229-238(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Abicht A., Stucka R., Lochmuller H.;
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
SUBUNIT.
PubMed=15609996; DOI=10.1021/bi048918g;
Ellison M., Gao F., Wang H.L., Sine S.M., McIntosh J.M., Olivera B.M.;
"Alpha-conotoxins ImI and ImII target distinct regions of the human
alpha7 nicotinic acetylcholine receptor and distinguish human
nicotinic receptor subtypes.";
Biochemistry 43:16019-16026(2004).
[5]
VARIANT CMS4A PHE-289.
PubMed=7538206; DOI=10.1212/WNL.45.5.982;
Gomez C.M., Gammack J.T.;
"A leucine-to-phenylalanine substitution in the acetylcholine receptor
ion channel in a family with the slow-channel syndrome.";
Neurology 45:982-985(1995).
[6]
VARIANT CMS4A PRO-284, AND CHARACTERIZATION OF VARIANT CMS4A PRO-284.
PubMed=7531341; DOI=10.1073/pnas.92.3.758;
Ohno K., Hutchinson D.O., Milone M., Brengman J.M., Bouzat C.,
Sine S.M., Engel A.G.;
"Congenital myasthenic syndrome caused by prolonged acetylcholine
receptor channel openings due to a mutation in the M2 domain of the
epsilon subunit.";
Proc. Natl. Acad. Sci. U.S.A. 92:758-762(1995).
[7]
VARIANT CMS4A PHE-289, AND CHARACTERIZATION OF VARIANT CMS4A PHE-289.
PubMed=8872460; DOI=10.1093/hmg/5.9.1217;
Engel A.G., Ohno K., Milone M., Wang H.-L., Nakano S., Bouzat C.,
Pruitt J.N. II, Hutchinson D.O., Brengman J.M., Bren N., Sieb J.P.,
Sine S.M.;
"New mutations in acetylcholine receptor subunit genes reveal
heterogeneity in the slow-channel congenital myasthenic syndrome.";
Hum. Mol. Genet. 5:1217-1227(1996).
[8]
VARIANTS CMS4B ARG-13; LEU-141 AND LEU-163, AND CHARACTERIZATION OF
VARIANTS CMS4B ARG-13; LEU-141 AND LEU-163.
PubMed=8755487; DOI=10.1016/S0896-6273(00)80289-5;
Ohno K., Wang H.-L., Milone M., Bren N., Brengman J.M., Nakano S.,
Quiram P., Pruitt J.N. II, Sine S.M., Engel A.G.;
"Congenital myasthenic syndrome caused by decreased agonist binding
affinity due to a mutation in the acetylcholine receptor epsilon
subunit.";
Neuron 17:157-170(1996).
[9]
VARIANTS CMS4C LEU-167; LEU-265 AND TRP-331, AND CHARACTERIZATION OF
VARIANTS CMS4C LEU-167; LEU-265 AND TRP-331.
PubMed=9158150; DOI=10.1093/hmg/6.5.753;
Ohno K., Quiram P.A., Milone M., Wang H.-L., Harper M.C.,
Pruitt J.N. II, Brengman J.M., Pao L., Fischbeck K.H., Crawford T.O.,
Sine S.M., Engel A.G.;
"Congenital myasthenic syndromes due to heteroallelic
nonsense/missense mutations in the acetylcholine receptor epsilon
subunit gene: identification and functional characterization of six
new mutations.";
Hum. Mol. Genet. 6:753-766(1997).
[10]
VARIANT CMS4B PRO-431, AND CHARACTERIZATION OF VARIANT CMS4B PRO-431.
PubMed=10962020; DOI=10.1085/jgp.116.3.449;
Wang H.-L., Ohno K., Milone M., Brengman J.M., Evoli A.,
Batocchi A.-P., Middleton L.T., Christodoulou K., Engel A.G.,
Sine S.M.;
"Fundamental gating mechanism of nicotinic receptor channel revealed
by mutation causing a congenital myasthenic syndrome.";
J. Gen. Physiol. 116:449-462(2000).
[11]
VARIANTS CMS4A PRO-98 AND PHE-241.
PubMed=12141316; DOI=10.1212/WNL.59.2.162;
Croxen R., Hatton C., Shelley C., Brydson M., Chauplannaz G.,
Oosterhuis H., Vincent A., Newsom-Davis J., Colquhoun D., Beeson D.;
"Recessive inheritance and variable penetrance of slow-channel
congenital myasthenic syndromes.";
Neurology 59:162-168(2002).
[12]
VARIANT CMS4B ARG-75, AND CHARACTERIZATION OF VARIANT CMS4B ARG-75.
PubMed=22592360; DOI=10.1212/WNL.0b013e31825b5bda;
Shen X.M., Brengman J.M., Edvardson S., Sine S.M., Engel A.G.;
"Highly fatal fast-channel syndrome caused by AChR epsilon subunit
mutation at the agonist binding site.";
Neurology 79:449-454(2012).
[13]
VARIANT CMS4A ALA-285, CHARACTERIZATION OF VARIANT CMS4A ALA-285, AND
FUNCTION.
PubMed=27375219; DOI=10.1002/humu.23043;
Shen X.M., Okuno T., Milone M., Otsuka K., Takahashi K., Komaki H.,
Giles E., Ohno K., Engel A.G.;
"Mutations causing slow-channel myasthenia reveal that a valine ring
in the channel pore of muscle AChR is optimized for stabilizing
channel gating.";
Hum. Mutat. 37:1051-1059(2016).
-!- FUNCTION: After binding acetylcholine, the AChR responds by an
extensive change in conformation that affects all subunits and
leads to opening of an ion-conducting channel across the plasma
membrane. {ECO:0000269|PubMed:27375219}.
-!- SUBUNIT: Pentamer of two alpha chains, and one each of the beta,
delta, and gamma (in immature muscle) or epsilon (in mature
muscle) chains. The muscle heteropentamer composed of alpha-1,
beta-1, delta, epsilon subunits interacts with the alpha-conotoxin
ImII (PubMed:15609996). {ECO:0000269|PubMed:15609996}.
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
membrane protein.
-!- DISEASE: Note=The muscle AChR is the major target antigen in the
autoimmune disease myasthenia gravis. Myasthenia gravis is
characterized by sporadic muscular fatigability and weakness,
occurring chiefly in muscles innervated by cranial nerves, and
characteristically improved by cholinesterase-inhibiting drugs.
-!- DISEASE: Myasthenic syndrome, congenital, 4A, slow-channel (CMS4A)
[MIM:605809]: A form of congenital myasthenic syndrome, a group of
disorders characterized by failure of neuromuscular transmission,
including pre-synaptic, synaptic, and post-synaptic disorders that
are not of autoimmune origin. Clinical features are easy
fatigability and muscle weakness affecting the axial and limb
muscles (with hypotonia in early-onset forms), the ocular muscles
(leading to ptosis and ophthalmoplegia), and the facial and bulbar
musculature (affecting sucking and swallowing, and leading to
dysphonia). The symptoms fluctuate and worsen with physical
effort. CMS4A is a slow-channel myasthenic syndrome. It is caused
by kinetic abnormalities of the AChR, resulting in prolonged AChR
channel opening episodes, prolonged endplate currents, and
depolarization block. This is associated with calcium overload,
which may contribute to subsequent degeneration of the endplate
and postsynaptic membrane. {ECO:0000269|PubMed:12141316,
ECO:0000269|PubMed:27375219, ECO:0000269|PubMed:7531341,
ECO:0000269|PubMed:7538206, ECO:0000269|PubMed:8872460}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Myasthenic syndrome, congenital, 4B, fast-channel (CMS4B)
[MIM:616324]: A form of congenital myasthenic syndrome, a group of
disorders characterized by failure of neuromuscular transmission,
including pre-synaptic, synaptic, and post-synaptic disorders that
are not of autoimmune origin. Clinical features are easy
fatigability and muscle weakness affecting the axial and limb
muscles (with hypotonia in early-onset forms), the ocular muscles
(leading to ptosis and ophthalmoplegia), and the facial and bulbar
musculature (affecting sucking and swallowing, and leading to
dysphonia). The symptoms fluctuate and worsen with physical
effort. CMS4B is a fast-channel myasthenic syndrome. It is caused
by kinetic abnormalities of the AChR, resulting in brief opening
and activity of the channel, with a rapid decay in endplate
current, failure to achieve threshold depolarization of the
endplate and consequent failure to fire an action potential.
{ECO:0000269|PubMed:10962020, ECO:0000269|PubMed:22592360,
ECO:0000269|PubMed:8755487}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Myasthenic syndrome, congenital, 4C, associated with
acetylcholine receptor deficiency (CMS4C) [MIM:608931]: A form of
congenital myasthenic syndrome, a group of disorders characterized
by failure of neuromuscular transmission, including pre-synaptic,
synaptic, and post-synaptic disorders that are not of autoimmune
origin. Clinical features are easy fatigability and muscle
weakness affecting the axial and limb muscles (with hypotonia in
early-onset forms), the ocular muscles (leading to ptosis and
ophthalmoplegia), and the facial and bulbar musculature (affecting
sucking and swallowing, and leading to dysphonia). The symptoms
fluctuate and worsen with physical effort. CMS4C is an autosomal
recessive disorder of postsynaptic neuromuscular transmission, due
to deficiency of AChR at the endplate that results in low
amplitude of the miniature endplate potential and current.
{ECO:0000269|PubMed:9158150}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
Epsilon/CHRNE sub-subfamily. {ECO:0000305}.
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EMBL; X66403; CAA47030.1; -; mRNA.
EMBL; AF105999; AAD24503.1; -; Genomic_DNA.
EMBL; CH471108; EAW90395.1; -; Genomic_DNA.
EMBL; CH471108; EAW90396.1; -; Genomic_DNA.
CCDS; CCDS11058.1; -.
PIR; S34775; S34775.
RefSeq; NP_000071.1; NM_000080.3.
UniGene; Hs.654535; -.
PDB; 2DF9; Model; -; A=240-332.
PDBsum; 2DF9; -.
ProteinModelPortal; Q04844; -.
BioGrid; 107567; 2.
STRING; 9606.ENSP00000293780; -.
BindingDB; Q04844; -.
ChEMBL; CHEMBL2484; -.
DrugBank; DB00674; Galantamine.
TCDB; 1.A.9.1.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
iPTMnet; Q04844; -.
PhosphoSitePlus; Q04844; -.
BioMuta; CHRNE; -.
DMDM; 1168301; -.
MaxQB; Q04844; -.
PaxDb; Q04844; -.
PeptideAtlas; Q04844; -.
PRIDE; Q04844; -.
Ensembl; ENST00000293780; ENSP00000293780; ENSG00000108556.
GeneID; 1145; -.
KEGG; hsa:1145; -.
UCSC; uc002fzk.2; human.
CTD; 1145; -.
DisGeNET; 1145; -.
EuPathDB; HostDB:ENSG00000108556.7; -.
GeneCards; CHRNE; -.
GeneReviews; CHRNE; -.
H-InvDB; HIX0027273; -.
HGNC; HGNC:1966; CHRNE.
MalaCards; CHRNE; -.
MIM; 100725; gene.
MIM; 254200; phenotype.
MIM; 605809; phenotype.
MIM; 608931; phenotype.
MIM; 616324; phenotype.
neXtProt; NX_Q04844; -.
OpenTargets; ENSG00000108556; -.
Orphanet; 98913; Postsynaptic congenital myasthenic syndromes.
PharmGKB; PA26498; -.
eggNOG; KOG3645; Eukaryota.
eggNOG; ENOG410XQGR; LUCA.
GeneTree; ENSGT00760000118930; -.
HOGENOM; HOG000006757; -.
HOVERGEN; HBG003756; -.
InParanoid; Q04844; -.
KO; K04817; -.
OMA; ESTRDQE; -.
OrthoDB; EOG091G0R20; -.
PhylomeDB; Q04844; -.
TreeFam; TF315605; -.
Reactome; R-HSA-629587; Highly sodium permeable acetylcholine nicotinic receptors.
GeneWiki; CHRNE; -.
GenomeRNAi; 1145; -.
PRO; PR:Q04844; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108556; -.
CleanEx; HS_CHRNE; -.
Genevisible; Q04844; HS.
GO; GO:0005892; C:acetylcholine-gated channel complex; TAS:ProtInc.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0015464; F:acetylcholine receptor activity; TAS:ProtInc.
GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; TAS:ProtInc.
GO; GO:0008324; F:cation transmembrane transporter activity; TAS:ProtInc.
GO; GO:0015276; F:ligand-gated ion channel activity; TAS:Reactome.
GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
GO; GO:0035094; P:response to nicotine; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007271; P:synaptic transmission, cholinergic; TAS:ProtInc.
GO; GO:0006810; P:transport; TAS:ProtInc.
Gene3D; 2.70.170.10; -; 1.
InterPro; IPR006202; Neur_chan_lig-bd.
InterPro; IPR006201; Neur_channel.
InterPro; IPR006029; Neurotrans-gated_channel_TM.
InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
PANTHER; PTHR18945; PTHR18945; 1.
Pfam; PF02931; Neur_chan_LBD; 1.
Pfam; PF02932; Neur_chan_memb; 1.
PRINTS; PR00254; NICOTINICR.
PRINTS; PR00252; NRIONCHANNEL.
SUPFAM; SSF63712; SSF63712; 1.
SUPFAM; SSF90112; SSF90112; 1.
PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Complete proteome;
Congenital myasthenic syndrome; Disease mutation; Disulfide bond;
Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
Membrane; Polymorphism; Postsynaptic cell membrane; Receptor;
Reference proteome; Signal; Synapse; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 20
CHAIN 21 493 Acetylcholine receptor subunit epsilon.
/FTId=PRO_0000000329.
TOPO_DOM 21 239 Extracellular. {ECO:0000255}.
TRANSMEM 240 264 Helical. {ECO:0000255}.
TOPO_DOM 265 272 Cytoplasmic. {ECO:0000255}.
TRANSMEM 273 291 Helical. {ECO:0000255}.
TOPO_DOM 292 306 Extracellular. {ECO:0000255}.
TRANSMEM 307 328 Helical. {ECO:0000255}.
TOPO_DOM 329 456 Cytoplasmic. {ECO:0000255}.
TRANSMEM 457 480 Helical. {ECO:0000255}.
TOPO_DOM 481 493 Extracellular. {ECO:0000255}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 148 162 {ECO:0000250}.
VARIANT 13 13 G -> R (in CMS4B; impaired association
with alpha CHRNA1 subunit of AChR;
dbSNP:rs372635387).
{ECO:0000269|PubMed:8755487}.
/FTId=VAR_021213.
VARIANT 18 18 G -> V (in dbSNP:rs4790235).
/FTId=VAR_048170.
VARIANT 75 75 W -> R (in CMS4B; strongly reduces
agonist affinity and gating efficiency;
dbSNP:rs193919341).
{ECO:0000269|PubMed:22592360}.
/FTId=VAR_071629.
VARIANT 98 98 L -> P (in CMS4A; rare example of
recessive inheritance; dbSNP:rs28929768).
{ECO:0000269|PubMed:12141316}.
/FTId=VAR_019567.
VARIANT 141 141 P -> L (in CMS4B; marked decrease in rate
of AChR channel opening; reduction in
frequency of open channel state and
resistance to desensitization by ACh;
dbSNP:rs121909512).
{ECO:0000269|PubMed:8755487}.
/FTId=VAR_000289.
VARIANT 163 163 S -> L (in CMS4B; fails to assemble with
alpha CHRNA1 subunit of AChR;
dbSNP:rs121909516).
{ECO:0000269|PubMed:8755487}.
/FTId=VAR_021214.
VARIANT 167 167 R -> L (in CMS4C; significantly reduced
AChR expression; dbSNP:rs121909514).
{ECO:0000269|PubMed:9158150}.
/FTId=VAR_000290.
VARIANT 241 241 L -> F (in CMS4A; mild form with variable
penetrance; dbSNP:rs28999110).
{ECO:0000269|PubMed:12141316}.
/FTId=VAR_019568.
VARIANT 265 265 P -> L (in CMS4C; prolongs burst open
duration 2-fold by slowing the rate of
channel closing; dbSNP:rs759226183).
{ECO:0000269|PubMed:9158150}.
/FTId=VAR_000291.
VARIANT 284 284 T -> P (in CMS4A; markedly prolonged
channel openings in presence of agonist;
as well as opening in the absence of
agonist; dbSNP:rs121909510).
{ECO:0000269|PubMed:7531341}.
/FTId=VAR_000292.
VARIANT 285 285 V -> A (in CMS4A; slow-channel mutation;
increases gating equilibrium constant by
25-fold, owing to increased opening rate
and decreased closing rate; no effect on
the choline dissociation rate constant).
{ECO:0000269|PubMed:27375219}.
/FTId=VAR_077364.
VARIANT 289 289 L -> F (in CMS4A; slows rate of AChR
channel closure and increases apparent
affinity for ACh; causes pathologic
channel openings even in the absence of
ACh resulting in a leaky channel;
dbSNP:rs121909511).
{ECO:0000269|PubMed:7538206,
ECO:0000269|PubMed:8872460}.
/FTId=VAR_000293.
VARIANT 331 331 R -> W (in CMS4C; shortens burst duration
2-fold by slowing the rate of channel
opening and speeding the rate of ACh
dissociation; has a mild fast-channel
kinetic effect on the AChR by shortening
the long burst and increasing the decay
of the endplate current;
dbSNP:rs121909515).
{ECO:0000269|PubMed:9158150}.
/FTId=VAR_000294.
VARIANT 431 431 A -> P (in CMS4B; causes an increase in
distributions of rates for channel
opening and closing increasing the range
of activation kinetics;
dbSNP:rs121909517).
{ECO:0000269|PubMed:10962020}.
/FTId=VAR_021215.
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


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EIAAB14649 Fce1a,Fc-epsilon RI-alpha,Fcer1a,FcERI,High affinity immunoglobulin epsilon receptor subunit alpha,IgE Fc receptor subunit alpha,Mouse,Mus musculus


 

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