ID   ACHE_XENLA              Reviewed;         504 AA.
AC   P49580;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Acetylcholine receptor subunit epsilon;
DE   Flags: Precursor;
GN   Name=chrne;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7718247; DOI=10.1016/0896-6273(95)90230-9;
RA   Murray N., Zheng Y.C., Mandel G., Brehm P., Bolinger R., Reuer Q.,
RA   Kullberg R.W.;
RT   "A single site on the epsilon subunit is responsible for the change in ACh
RT   receptor channel conductance during skeletal muscle development.";
RL   Neuron 14:865-870(1995).
RN   [2]
RP   ERRATUM OF PUBMED:7718247, AND RETRACTION NOTICE OF PUBMED:7718247.
RX   PubMed=9652915; DOI=10.1016/s0896-6273(02)02053-6;
RA   Murray N., Zheng Y.C., Mandel G., Brehm P., Bolinger R., Reuer Q.,
RA   Kullberg R.W.;
RL   Neuron 20:1050-1050(1998).
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   -!- 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   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
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; U19612; AAA92687.1; -; mRNA.
DR   RefSeq; NP_001080916.1; NM_001087447.1.
DR   AlphaFoldDB; P49580; -.
DR   SMR; P49580; -.
DR   GeneID; 386670; -.
DR   KEGG; xla:386670; -.
DR   CTD; 386670; -.
DR   Xenbase; XB-GENE-979689; chrne.L.
DR   OrthoDB; 588360at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 386670; Expressed in muscle tissue and 6 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cell membrane; 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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..504
FT                   /note="Acetylcholine receptor subunit epsilon"
FT                   /id="PRO_0000000332"
FT   TOPO_DOM        20..240
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..273
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..307
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        330..473
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        474..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        498..504
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
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"
SQ   SEQUENCE   504 AA;  57788 MW;  DA9E3BAC322BDB4F CRC64;
     MESGVRILSL LILLHNSLAS ESEESRLIKH LFTSYDQKAR PSKGLDDVVP VTLKLTLTNL
     IDLNEKEETL TTNVWVQIAW NDDRLVWNVT DYGGIGFVPV PHDIMWLPDI VLENNIDGNF
     EVAYYANVLV YNTGYIYWLP PAIFRSTCNI EITYFPFDWQ NCSLVFRSKT YSANEIDLQL
     VTDDETGLPF DQVDIDREAF TENGEWAIMH RPARKILNPK YSKEDLRYQE IVFNLIIQRK
     PLFYIINIIV PCVLISFLVV LVYFLPAKAG GQKCTVSISV LLAQTVFLFL IAQMVPETSL
     SVPLIGKYLM FVMFVSTLIV LSCVIVLNVS LRSPSTHNLS TKVKHMLLEV LPQFLHLRVE
     PCDEGEETPR ERRRSSLGIM LKAEEYVLKK PRSELMFERQ RERHGMRREP DGYRADGFDV
     GVTTTLYRNL AQCAPEIKDC VDACNFITQN TKEQNRTGSE MENWILIGKV LDVLCFWVAL
     PLFVLGTLAI FLMGHFNTAP EHPF