ACHE_MOUSE
ID ACHE_MOUSE Reviewed; 493 AA.
AC P20782;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Acetylcholine receptor subunit epsilon;
DE Flags: Precursor;
GN Name=Chrne; Synonyms=Acre;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2708381; DOI=10.1016/s0021-9258(18)83278-1;
RA Buonanno A., Mudd J., Merlie J.P.;
RT "Isolation and characterization of the beta and epsilon subunit genes of
RT mouse muscle acetylcholine receptor.";
RL J. Biol. Chem. 264:7611-7616(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2251144; DOI=10.1093/nar/18.22.6714;
RA Gardner P.D.;
RT "Nucleotide sequence of the epsilon-subunit of the mouse muscle nicotinic
RT acetylcholine receptor.";
RL Nucleic Acids Res. 18:6714-6714(1990).
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; J04698; AAA37153.1; -; Genomic_DNA.
DR EMBL; X55718; CAA39251.1; -; mRNA.
DR CCDS; CCDS24956.1; -.
DR PIR; S13592; ACMSE.
DR RefSeq; NP_033733.1; NM_009603.1.
DR AlphaFoldDB; P20782; -.
DR SMR; P20782; -.
DR ComplexPortal; CPX-257; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon.
DR STRING; 10090.ENSMUSP00000099616; -.
DR BindingDB; P20782; -.
DR ChEMBL; CHEMBL3091265; -.
DR GlyGen; P20782; 2 sites.
DR PhosphoSitePlus; P20782; -.
DR SwissPalm; P20782; -.
DR PaxDb; P20782; -.
DR PRIDE; P20782; -.
DR ProteomicsDB; 285976; -.
DR Antibodypedia; 11366; 182 antibodies from 28 providers.
DR DNASU; 11448; -.
DR Ensembl; ENSMUST00000102556; ENSMUSP00000099616; ENSMUSG00000014609.
DR GeneID; 11448; -.
DR KEGG; mmu:11448; -.
DR UCSC; uc007jvo.1; mouse.
DR CTD; 1145; -.
DR MGI; MGI:87894; Chrne.
DR VEuPathDB; HostDB:ENSMUSG00000014609; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000160933; -.
DR HOGENOM; CLU_018074_1_4_1; -.
DR InParanoid; P20782; -.
DR OMA; ACNFIAD; -.
DR OrthoDB; 588360at2759; -.
DR TreeFam; TF315605; -.
DR Reactome; R-MMU-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR BioGRID-ORCS; 11448; 2 hits in 72 CRISPR screens.
DR PRO; PR:P20782; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P20782; protein.
DR Bgee; ENSMUSG00000014609; Expressed in spermatid and 34 other tissues.
DR ExpressionAtlas; P20782; baseline and differential.
DR Genevisible; P20782; MM.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IPI:ComplexPortal.
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:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
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; IDA:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IGI:MGI.
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; ISO:MGI.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IDA:ComplexPortal.
DR GO; GO:0006812; P:cation transport; ISO:MGI.
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; IGI:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0003009; P:skeletal muscle contraction; ISO:MGI.
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..493
FT /note="Acetylcholine receptor subunit epsilon"
FT /id="PRO_0000000330"
FT TOPO_DOM 21..239
FT /note="Extracellular"
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"
SQ SEQUENCE 493 AA; 54914 MW; F3E468644F3FB7DF CRC64;
MAGALLGALL LLTLFGRSQG KNEELSLYHH LFDNYDPECR PVRRPEDTVT ITLKVTLTNL
ISLNEKEETL TTSVWIGIDW HDYRLNYSKD DFAGVGILRV PSEHVWLPEI VLENNIDGQF
GVAYDSNVLV YEGGYVSWLP PAIYRSTCAV EVTYFPFDWQ NCSLIFRSQT YNAEEVEFIF
AVDDDGNTIN KIDIDTAAFT ENGEWAIDYC PGMIRRYEGG STEGPGETDV IYTLIIRRKP
LFYVINIIVP CVLISGLVLL AYFLPAQAGG QKCTVSINVL LAQTVFLFLI AQKIPETSLS
VPLLGRYLIF VMVVATLIVM NCVIVLNVSL RTPTTHATSP RLRQILLELL PRLLGSSPPP
EDPRTASPAR RASSVGILLR AEELILKKPR SELVFEGQRH RHGTWTAALC QNLGAAAPEI
RCCVDAVNFV AESTRDQEAT GEELSDWVRM GKALDNVCFW AALVLFSVGS TLIFLGGYFN
QVPDLPYPPC IQP
