ACHA_MOUSE
ID ACHA_MOUSE Reviewed; 457 AA.
AC P04756;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Acetylcholine receptor subunit alpha;
DE Flags: Precursor;
GN Name=Chrna1; Synonyms=Acra;
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 [MRNA].
RX PubMed=3755237; DOI=10.1093/nar/14.12.5111;
RA Isenberg K.E., Mudd J., Shah V., Merlie J.P.;
RT "Nucleotide sequence of the mouse muscle nicotinic acetylcholine receptor
RT alpha subunit.";
RL Nucleic Acids Res. 14:5111-5111(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Boulter J.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-457.
RX PubMed=2993547; DOI=10.1523/jneurosci.05-09-02545.1985;
RA Boulter J., Luyten W., Evans K., Mason P., Ballivet M., Goldman D.J.,
RA Stengelin S.F., Martin G., Heinemann S.F., Patrick J.;
RT "Isolation of a clone coding for the alpha-subunit of a mouse acetylcholine
RT receptor.";
RL J. Neurosci. 5:2545-2552(1985).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 21-231 IN COMPLEX WITH
RP ALPHA-BUNGAROTOXIN, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-161.
RX PubMed=17643119; DOI=10.1038/nn1942;
RA Dellisanti C.D., Yao Y., Stroud J.C., Wang Z.Z., Chen L.;
RT "Crystal structure of the extracellular domain of nAChR alpha1 bound to
RT alpha-bungarotoxin at 1.94 A resolution.";
RL Nat. Neurosci. 10:953-962(2007).
CC -!- FUNCTION: Upon acetylcholine binding, the AChR responds by an extensive
CC change in conformation that affects all subunits and leads to opening
CC of an ion-conducting channel across the plasma membrane.
CC {ECO:0000250|UniProtKB:P02708}.
CC -!- SUBUNIT: One of the alpha chains that assemble within the acetylcholine
CC receptor, a pentamer of two alpha chains, a beta, a delta, and a gamma
CC (in immature muscle) or epsilon (in mature muscle) chains
CC (PubMed:17643119). The muscle heteropentamer composed of alpha-1, beta-
CC 1, delta, epsilon subunits interacts with the alpha-conotoxin ImII (By
CC similarity). {ECO:0000250|UniProtKB:P02708,
CC ECO:0000269|PubMed:17643119}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P02708}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P02708}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-1/CHRNA1 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X03986; CAA27624.1; -; mRNA.
DR EMBL; M17640; AAB53942.1; -; mRNA.
DR EMBL; AK029177; BAC26337.1; -; mRNA.
DR CCDS; CCDS16132.1; -.
DR PIR; A24383; A24383.
DR PIR; I49458; I49458.
DR RefSeq; NP_031415.2; NM_007389.5.
DR PDB; 2QC1; X-ray; 1.94 A; B=21-231.
DR PDB; 5HBV; X-ray; 2.70 A; B=22-231.
DR PDBsum; 2QC1; -.
DR PDBsum; 5HBV; -.
DR AlphaFoldDB; P04756; -.
DR SMR; P04756; -.
DR BioGRID; 197931; 5.
DR ComplexPortal; CPX-252; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma.
DR ComplexPortal; CPX-257; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon.
DR DIP; DIP-59594N; -.
DR IntAct; P04756; 2.
DR MINT; P04756; -.
DR STRING; 10090.ENSMUSP00000028515; -.
DR BindingDB; P04756; -.
DR ChEMBL; CHEMBL3038460; -.
DR ChEMBL; CHEMBL3137264; -.
DR GlyGen; P04756; 1 site.
DR iPTMnet; P04756; -.
DR PhosphoSitePlus; P04756; -.
DR SwissPalm; P04756; -.
DR PaxDb; P04756; -.
DR PRIDE; P04756; -.
DR ProteomicsDB; 285920; -.
DR ABCD; P04756; 4 sequenced antibodies.
DR Antibodypedia; 19487; 440 antibodies from 37 providers.
DR DNASU; 11435; -.
DR Ensembl; ENSMUST00000028515; ENSMUSP00000028515; ENSMUSG00000027107.
DR GeneID; 11435; -.
DR KEGG; mmu:11435; -.
DR UCSC; uc008kcy.2; mouse.
DR CTD; 1134; -.
DR MGI; MGI:87885; Chrna1.
DR VEuPathDB; HostDB:ENSMUSG00000027107; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000156851; -.
DR HOGENOM; CLU_018074_1_0_1; -.
DR InParanoid; P04756; -.
DR OMA; STHIMPE; -.
DR OrthoDB; 381858at2759; -.
DR PhylomeDB; P04756; -.
DR TreeFam; TF315605; -.
DR Reactome; R-MMU-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR Reactome; R-MMU-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR BioGRID-ORCS; 11435; 2 hits in 74 CRISPR screens.
DR EvolutionaryTrace; P04756; -.
DR PRO; PR:P04756; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P04756; protein.
DR Bgee; ENSMUSG00000027107; Expressed in tarsal region and 66 other tissues.
DR ExpressionAtlas; P04756; baseline and differential.
DR Genevisible; P04756; 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:0009986; C:cell surface; IDA:MGI.
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:0016020; C:membrane; IDA:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0042166; F:acetylcholine binding; IGI:MGI.
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:0046716; P:muscle cell cellular homeostasis; ISO:MGI.
DR GO; GO:0050881; P:musculoskeletal movement; ISO:MGI.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0007528; P:neuromuscular junction development; ISO:MGI.
DR GO; GO:0050905; P:neuromuscular process; ISO:MGI.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; ISO:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; ISO:MGI.
DR GO; GO:0019228; P:neuronal action potential; ISO:MGI.
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 GO; GO:0048630; P:skeletal muscle tissue growth; ISO:MGI.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IEA:GOC.
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 TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT CHAIN 21..457
FT /note="Acetylcholine receptor subunit alpha"
FT /id="PRO_0000000306"
FT TOPO_DOM 21..230
FT /note="Extracellular"
FT TRANSMEM 231..255
FT /note="Helical"
FT TRANSMEM 263..281
FT /note="Helical"
FT TRANSMEM 297..316
FT /note="Helical"
FT TOPO_DOM 317..428
FT /note="Cytoplasmic"
FT TRANSMEM 429..447
FT /note="Helical"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17643119"
FT DISULFID 148..162
FT /evidence="ECO:0000269|PubMed:17643119"
FT DISULFID 212..213
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000269|PubMed:17643119"
FT CONFLICT 13
FT /note="C -> S (in Ref. 2; AAB53942 and 4; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:2QC1"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2QC1"
FT STRAND 49..64
FT /evidence="ECO:0007829|PDB:2QC1"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:2QC1"
FT STRAND 69..81
FT /evidence="ECO:0007829|PDB:2QC1"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:2QC1"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2QC1"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2QC1"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2QC1"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2QC1"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2QC1"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2QC1"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:2QC1"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2QC1"
FT STRAND 159..170
FT /evidence="ECO:0007829|PDB:2QC1"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:2QC1"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:2QC1"
FT STRAND 194..210
FT /evidence="ECO:0007829|PDB:2QC1"
FT STRAND 218..229
FT /evidence="ECO:0007829|PDB:2QC1"
SQ SEQUENCE 457 AA; 51939 MW; 5CB606D144F29436 CRC64;
MELSTVLLLL GLCSAGLVLG SEHETRLVAK LFEDYSSVVR PVEDHREIVQ VTVGLQLIQL
INVDEVNQIV TTNVRLKQQW VDYNLKWNPD DYGGVKKIHI PSEKIWRPDV VLYNNADGDF
AIVKFTKVLL DYTGHITWTP PAIFKSYCEI IVTHFPFDEQ NCSMKLGTWT YDGSVVAINP
ESDQPDLSNF MESGEWVIKE ARGWKHWVFY SCCPTTPYLD ITYHFVMQRL PLYFIVNVII
PCLLFSFLTS LVFYLPTDSG EKMTLSISVL LSLTVFLLVI VELIPSTSSA VPLIGKYMLF
TMVFVIASII ITVIVINTHH RSPSTHIMPE WVRKVFIDTI PNIMFFSTMK RPSRDKQEKR
IFTEDIDISD ISGKPGPPPM GFHSPLIKHP EVKSAIEGVK YIAETMKSDQ ESNNAAEEWK
YVAMVMDHIL LGVFMLVCLI GTLAVFAGRL IELHQQG
