ACHE_RAT
ID ACHE_RAT Reviewed; 494 AA.
AC P09660; Q6LAD4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Acetylcholine receptor subunit epsilon;
DE Flags: Precursor;
GN Name=Chrne; Synonyms=Achre;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Muscle;
RX PubMed=1702709; DOI=10.1111/j.1432-1033.1990.tb15637.x;
RA Witzemann V., Stein E., Barg B., Konno T., Koenen M., Kues W., Criado M.,
RA Hofmann M., Sakmann B.;
RT "Primary structure and functional expression of the alpha-, beta-, gamma-,
RT delta- and epsilon-subunits of the acetylcholine receptor from rat
RT muscle.";
RL Eur. J. Biochem. 194:437-448(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=3205730; DOI=10.1093/nar/16.22.10920;
RA Criado M., Witzemann V., Koenen M., Sakmann B.;
RT "Nucleotide sequence of the rat muscle acetylcholine receptor epsilon-
RT subunit.";
RL Nucleic Acids Res. 16:10920-10920(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RC STRAIN=Fischer; TISSUE=Liver;
RX PubMed=8034713; DOI=10.1016/s0021-9258(17)32189-0;
RA Walke W., Staple J., Adams L., Gnegy M., Chahine K., Goldman D.;
RT "Calcium-dependent regulation of rat and chick muscle nicotinic
RT acetylcholine receptor (nAChR) gene expression.";
RL J. Biol. Chem. 269:19447-19456(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-305.
RC STRAIN=Sprague-Dawley;
RX PubMed=3666131; DOI=10.1016/0014-5793(87)80518-5;
RA Witzemann V., Barg B., Nishikawa Y., Sakmann B., Numa S.;
RT "Differential regulation of muscle acetylcholine receptor gamma- and
RT epsilon-subunit mRNAs.";
RL FEBS Lett. 223:104-112(1987).
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; X74836; CAA52830.1; -; mRNA.
DR EMBL; X13252; CAA31628.1; -; mRNA.
DR EMBL; Z23062; CAA80597.1; -; Genomic_DNA.
DR EMBL; X06365; CAA29663.1; -; Genomic_DNA.
DR PIR; S01959; ACRTE.
DR RefSeq; NP_058890.1; NM_017194.1.
DR AlphaFoldDB; P09660; -.
DR SMR; P09660; -.
DR ComplexPortal; CPX-258; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon.
DR STRING; 10116.ENSRNOP00000005050; -.
DR BindingDB; P09660; -.
DR ChEMBL; CHEMBL4961; -.
DR GlyGen; P09660; 2 sites.
DR jPOST; P09660; -.
DR PaxDb; P09660; -.
DR GeneID; 29422; -.
DR KEGG; rno:29422; -.
DR UCSC; RGD:2353; rat.
DR CTD; 1145; -.
DR RGD; 2353; Chrne.
DR eggNOG; KOG3645; Eukaryota.
DR InParanoid; P09660; -.
DR OrthoDB; 588360at2759; -.
DR PhylomeDB; P09660; -.
DR Reactome; R-RNO-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR PRO; PR:P09660; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:RGD.
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:RGD.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISO:RGD.
DR GO; GO:0006812; P:cation transport; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0003009; P:skeletal muscle contraction; IDA:RGD.
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 /evidence="ECO:0000250"
FT CHAIN 21..494
FT /note="Acetylcholine receptor subunit epsilon"
FT /id="PRO_0000000331"
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..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..494
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"
FT CONFLICT 391..392
FT /note="SE -> R (in Ref. 2; CAA31628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 54948 MW; 6476E4C938A6A9B6 CRC64;
MTMALLGTLL LLALFGRSQG KNEELSLYHH LFDNYDPECR PVRRPEDTVT ITLKVTLTNL
ISLNEKEETL TTSVWIGIEW QDYRLNFSKD DFAGVEILRV PSEHVWLPEI VLENNIDGQF
GVAYDCNVLV YEGGSVSWLP PAIYRSTCAV EVTYFPFDWQ NCSLIFRSQT YNAEEVELIF
AVDDDGNAIN KIDIDTAAFT ENGEWAIDYC PGMIRHYEGG STEDPGETDV IYTLIIRRKP
LFYVINIIVP CVLISGLVLL AYFLPAQAGG QKCTVSINVL LAQTVFLFLI AQKIPETSLS
VPLLGRYLIF VMVVATLIVM NCVIVLNVSL RTPTTHATSP RLRQILLELL PRLLGLSPPP
EDPGAASPAR RASSVGILLR AEELILKKPR SELVFEGQRH RHGTWTAAAL CQNLGAAAPE
VRCCVDAVNF VAESTRDQEA TGEELSDWVR MGKALDNVCF WAALVLFSVG STLIFLGGYF
NQVPDLPYPP CIQP
