ID   ACHA_NAJNA              Reviewed;         104 AA.
AC   P14143;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Acetylcholine receptor subunit alpha;
DE   Flags: Fragment;
GN   Name=CHRNA1;
OS   Naja naja (Indian cobra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=35670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2780569; DOI=10.1073/pnas.86.18.7255;
RA   Neumann D., Barchan D., Horowitz M., Kochva E., Fuchs S.;
RT   "Snake acetylcholine receptor: cloning of the domain containing the four
RT   extracellular cysteines of the alpha subunit.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:7255-7259(1989).
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       or epsilon chains. {ECO:0000250|UniProtKB:P02708}.
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; M26388; AAA49384.1; -; mRNA.
DR   AlphaFoldDB; P14143; -.
DR   SMR; P14143; -.
DR   Proteomes; UP000694559; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   PANTHER; PTHR18945; PTHR18945; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF63712; SSF63712; 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; Synapse; Transport.
FT   CHAIN           <1..>104
FT                   /note="Acetylcholine receptor subunit alpha"
FT                   /id="PRO_0000076975"
FT   TOPO_DOM        <1..>104
FT                   /note="Extracellular"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        10..24
FT                   /evidence="ECO:0000250"
FT   DISULFID        74..75
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         104
SQ   SEQUENCE   104 AA;  12194 MW;  47A39E2C9BFBA7A0 CRC64;
     NPPAIFKSYC EIIVTYFPFD EQNCSMKLGT WTYDGTVVAI YPEGPRPDLS NYMQSGEWTL
     KDYRGFWHSV NYSCCLDTPY LDITYHFILL RLPLYFIVNV IIPC