ID ACHA_BOVIN Reviewed; 457 AA.
AC P02709;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 27-MAR-2024, entry version 166.
DE RecName: Full=Acetylcholine receptor subunit alpha;
DE Flags: Precursor;
GN Name=CHRNA1;
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=6688857; DOI=10.1038/305818a0;
RA Noda M., Furutani Y., Takahashi H., Toyosato M., Tanabe T., Shimizu S.,
RA Kikyotani S., Kayano T., Hirose T., Inayama S., Numa S.;
RT "Cloning and sequence analysis of calf cDNA and human genomic DNA encoding
RT alpha-subunit precursor of muscle acetylcholine receptor.";
RL Nature 305:818-823(1983).
RN [2]
RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBUNIT.
RX PubMed=2423878; DOI=10.1038/321406a0;
RA Mishina M., Takai T., Imoto K., Noda M., Takahashi T., Numa S.,
RA Methfessel C., Sakmann B.;
RT "Molecular distinction between fetal and adult forms of muscle
RT acetylcholine receptor.";
RL Nature 321:406-411(1986).
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:0000269|PubMed:2423878}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:2423878};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:2423878};
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:2423878). The muscle heteropentamer composed of alpha-1, beta-
CC 1, delta, epsilon subunits interacts with the alpha-conotoxin ImII.
CC {ECO:0000250|UniProtKB:P02708, ECO:0000269|PubMed:2423878}.
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; X02509; CAA26345.1; -; mRNA.
DR PIR; A03169; ACBOA1.
DR RefSeq; NP_788837.1; NM_176664.2.
DR AlphaFoldDB; P02709; -.
DR SMR; P02709; -.
DR STRING; 9913.ENSBTAP00000024298; -.
DR GlyCosmos; P02709; 1 site, No reported glycans.
DR PaxDb; 9913-ENSBTAP00000024298; -.
DR Ensembl; ENSBTAT00000024298.6; ENSBTAP00000024298.5; ENSBTAG00000018253.6.
DR GeneID; 338070; -.
DR KEGG; bta:338070; -.
DR CTD; 1134; -.
DR VEuPathDB; HostDB:ENSBTAG00000018253; -.
DR VGNC; VGNC:27322; CHRNA1.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000156851; -.
DR HOGENOM; CLU_018074_1_2_1; -.
DR InParanoid; P02709; -.
DR OMA; XVFIDTI; -.
DR OrthoDB; 5489962at2759; -.
DR TreeFam; TF315605; -.
DR Reactome; R-BTA-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR Reactome; R-BTA-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000018253; Expressed in corpus luteum and 43 other cell types or tissues.
DR ExpressionAtlas; P02709; baseline and differential.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0099634; C:postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0042166; F:acetylcholine binding; IEA:Ensembl.
DR GO; GO:0015464; F:acetylcholine receptor activity; IEA:Ensembl.
DR GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IBA:GO_Central.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:Ensembl.
DR GO; GO:0070050; P:neuron cellular homeostasis; IEA:Ensembl.
DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IBA:GO_Central.
DR GO; GO:0003009; P:skeletal muscle contraction; IEA:Ensembl.
DR GO; GO:0048630; P:skeletal muscle tissue growth; IEA:Ensembl.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
DR CDD; cd19014; LGIC_ECD_nAChR_A1; 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 NCBIfam; TIGR00860; LIC; 1.
DR PANTHER; PTHR18945:SF74; ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA; 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 1: Evidence at protein 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..457
FT /note="Acetylcholine receptor subunit alpha"
FT /id="PRO_0000000304"
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:0000255"
FT DISULFID 148..162
FT /evidence="ECO:0000250"
FT DISULFID 212..213
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 457 AA; 51948 MW; 40261D335FD47A32 CRC64;
MEPRPLLLLL GLCSAGLVLG SEHETRLVAK LFEDYNSVVR PVEDHRQAVE VTVGLQLIQL
INVDEVNQIV TTNVRLKQQW VDYNLKWNPD DYGGVKKIHI PSEKIWRPDL VLYNNADGDF
AIVKFTKVLL DYTGHITWTP PAIFKSYCEI IVTHFPFDEQ NCSMKLGTWT YDGSVVVINP
ESDQPDLSNF MESGEWVIKE SRGWKHWVFY ACCPSTPYLD ITYHFVMQRL PLYFIVNVII
PCLLFSFLTG LVFYLPTDSG EKMTLSISVL LSLTVFLLVI VELIPSTSSA VPLIGKYMLF
TMVFVIASII ITVIVINTHH RSPSTHVMPE WVRKVFIDTI PNIMFFSTMK RPSREKQDKK
IFTEDIDISD ISGKPGPPPM GFHSPLIKHP EVKSAIEGIK YIAETMKSDQ ESNNAAEEWK
YVAMVMDHIL LAVFMLVCII GTLAVFAGRL IELNQQG
//
