ID   ACHA_HERIC              Reviewed;          84 AA.
AC   P54251;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Acetylcholine receptor subunit alpha;
DE   Flags: Fragment;
GN   Name=CHRNA1;
OS   Herpestes ichneumon (Egyptian mongoose).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Herpestidae; Herpestes.
OX   NCBI_TaxID=9700;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   PubMed=1380164; DOI=10.1073/pnas.89.16.7717;
RA   Barchan D., Kachalsky S., Neumann D., Vogel Z., Ovadia M., Kochva E.,
RA   Fuchs S.;
RT   "How the mongoose can fight the snake: the binding site of the mongoose
RT   acetylcholine receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:7717-7721(1992).
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. The muscle
CC       heteropentamer composed of alpha-1, beta-1, delta, epsilon subunits
CC       interacts with the alpha-conotoxin ImII.
CC       {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; M93639; AAA30930.1; -; mRNA.
DR   PIR; A46158; A46158.
DR   AlphaFoldDB; P54251; -.
DR   SMR; P54251; -.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   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   Synapse; Transmembrane; Transport.
FT   CHAIN           <1..>84
FT                   /note="Acetylcholine receptor subunit alpha"
FT                   /id="PRO_0000076973"
FT   SITE            66
FT                   /note="Confers toxin resistance"
FT                   /evidence="ECO:0000255"
FT   SITE            68
FT                   /note="Confers toxin resistance"
FT                   /evidence="ECO:0000255"
FT   SITE            73
FT                   /note="Confers toxin resistance"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        7..21
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..72
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         84
SQ   SEQUENCE   84 AA;  9803 MW;  E50AEC7E6D696609 CRC64;
     AIFKSYCEII VTHFPFDEQN CSMKLGTWTY DSSVVVINPE SDQPDLSNFM ESGEWVIKEA
     RGWKHNVTYA CCLTTHYLDI TYHF