ID   ACHE_BOVIN              Reviewed;         491 AA.
AC   P02715; Q547R5;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Acetylcholine receptor subunit epsilon;
DE   Flags: Precursor;
GN   Name=CHRNE;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3839289; DOI=10.1038/315761a0;
RA   Takai T., Noda M., Mishina M., Shimizu S., Furutani Y., Kayano T.,
RA   Ikeda T., Kubo T., Takahashi H., Takahashi T., Kuno M., Numa S.;
RT   "Cloning, sequencing and expression of cDNA for a novel subunit of
RT   acetylcholine receptor from calf muscle.";
RL   Nature 315:761-764(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14592869; DOI=10.1196/annals.1254.014;
RA   Sieb J.P., Kraner S., Thompson P.N., Steinlein O.K.;
RT   "Congenital myasthenic syndrome in cattle due to homozygosity for a
RT   truncating mutation in the acetylcholine receptor (AChR) epsilon-subunit
RT   gene.";
RL   Ann. N. Y. Acad. Sci. 998:125-127(2003).
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       The muscle heteropentamer composed of alpha-1, beta-1, delta, epsilon
CC       subunits interacts with the alpha-conotoxin ImII (By similarity).
CC       {ECO:0000250|UniProtKB:Q04844}.
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; X02597; CAA26442.1; -; mRNA.
DR   EMBL; AF457659; AAN76988.1; -; Genomic_DNA.
DR   EMBL; AF457656; AAN76988.1; JOINED; Genomic_DNA.
DR   EMBL; AF457657; AAN76988.1; JOINED; Genomic_DNA.
DR   EMBL; AF457658; AAN76988.1; JOINED; Genomic_DNA.
DR   PIR; A03174; ACBOE.
DR   RefSeq; NP_776697.1; NM_174272.2.
DR   AlphaFoldDB; P02715; -.
DR   SMR; P02715; -.
DR   STRING; 9913.ENSBTAP00000042804; -.
DR   PaxDb; P02715; -.
DR   PRIDE; P02715; -.
DR   Ensembl; ENSBTAT00000045415; ENSBTAP00000042804; ENSBTAG00000004908.
DR   GeneID; 281688; -.
DR   KEGG; bta:281688; -.
DR   CTD; 1145; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004908; -.
DR   VGNC; VGNC:27335; CHRNE.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000160933; -.
DR   HOGENOM; CLU_018074_1_4_1; -.
DR   InParanoid; P02715; -.
DR   OrthoDB; 588360at2759; -.
DR   TreeFam; TF315605; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000004908; Expressed in longissimus thoracis muscle and 104 other tissues.
DR   ExpressionAtlas; P02715; baseline and differential.
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:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IBA:GO_Central.
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:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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: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   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..20
FT   CHAIN           21..491
FT                   /note="Acetylcholine receptor subunit epsilon"
FT                   /id="PRO_0000000328"
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..491
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"
SQ   SEQUENCE   491 AA;  54565 MW;  30E301DA117FA395 CRC64;
     MAGALLCALL LLQLLGRGEG KNEELRLYHY LFDTYDPGRR PVQEPEDTVT ISLKVTLTNL
     ISLNEKEETL TTSVWIGIDW QDYRLNYSKG DFGGVETLRV PSELVWLPEI VLENNIDGQF
     GVAYEANVLV SEGGYLSWLP PAIYRSTCAV EVTYFPFDWQ NCSLVFRSQT YNAEEVEFVF
     AVDDEGKTIS KIDIDTEAYT ENGEWAIDFC PGVIRRHDGD SAGGPGETDV IYSLIIRRKP
     LFYVINIIVP CVLISGLVLL AYFLPAQAGG QKCTVSINVL LAQTVFLFLI AQKTPETSLS
     VPLLGRYLIF VMVVATLIVM NCVIVLNVSL RTPTTHAMSP RLRYVLLELL PQLLGSGAPP
     EIPRAASPPR RASSLGLLLR AEELILKKPR SELVFEQQRH RHGTWTATLC QNLGAAAPEI
     RCCVDAVNFV ASSTRDQEAT GEEVSDWVRM GKALDSICFW AALVLFLVGS SLIFLGAYFN
     RVPQLPYPPC M