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Database: UniProt
Entry: A0A452FL11_CAPHI
LinkDB: A0A452FL11_CAPHI
Original site: A0A452FL11_CAPHI 
ID   A0A452FL11_CAPHI        Unreviewed;       486 AA.
AC   A0A452FL11;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Acetylcholine receptor subunit epsilon {ECO:0000256|ARBA:ARBA00039794};
GN   Name=CHRNE {ECO:0000313|Ensembl:ENSCHIP00000024774.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000024774.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000024774.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000024774.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00003328}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00034104}. Synaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00034099}.
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:0000256|ARBA:ARBA00038451}.
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DR   EMBL; LWLT01000022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A452FL11; -.
DR   Ensembl; ENSCHIT00000032635.1; ENSCHIP00000024774.1; ENSCHIG00000021805.1.
DR   GeneTree; ENSGT00940000160933; -.
DR   OMA; PFPPCIQ; -.
DR   Proteomes; UP000291000; Chromosome 19.
DR   Bgee; ENSCHIG00000021805; Expressed in longissimus thoracis muscle and 18 other cell types or tissues.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   CDD; cd19030; LGIC_ECD_nAChR_E; 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   PANTHER; PTHR18945:SF59; ACETYLCHOLINE RECEPTOR SUBUNIT EPSILON; 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.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU000687};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU000687};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW   Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000687};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU000687};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000687}.
FT   TRANSMEM        236..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        270..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        299..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        452..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          21..235
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          242..469
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
SQ   SEQUENCE   486 AA;  54127 MW;  36023D88ACEAF8BB CRC64;
     MTSMDFLSCA GRGEGKNEEL RLYHYLFDNY DPGRRPVQEP EDTVTVSLKV TLTNLISLNE
     KEETLTTSVW IGIDWQDYRL NYSKGDFGGV ETLRVPSELV WLPEIVLENN IDGQFGVAYE
     ANVLISEGGY VSWLPPAIYR STCAVEVTYF PFDWQNCSLV FRSQTYNAEE VEFVFAVDDE
     GETISKIDID TEAYTENGEW AIDFCPGVIR RHDGDSPGGP GETDVIYSLI IRRKPLFYVI
     NIIVPCVLIS GLVLLAYFLP AQAGGQKCTV SINVLLAQTV FLFLIAQKTP ETSLSVPLLG
     RYLIFVMVVA TLIVMNCVIV LNVSLRTPTT HAMSPRLRHV LLELLPQLLG SGAPPEIPRA
     ASPPRRASSL GLLLRAEELI LKKPRSELVF EQQRHRHGNW TATLCQNLGA AAPEIRCCVD
     AVNFVASSTR DQEATGEEVS DWVRMGKALD SICFWAALVL FLVGSSLIFL GAYFNRVPQL
     PYPPCM
//
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