ID   ACH1_MANSE              Reviewed;         516 AA.
AC   P91766;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Acetylcholine receptor subunit alpha-like;
DE   AltName: Full=MARA1;
DE   Flags: Precursor;
GN   Name=ARA1;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9753155; DOI=10.1046/j.1460-9568.1998.00095.x;
RA   Eastham H.M., Lind R.J., Eastlake J.L., Clarke B.S., Towner P.,
RA   Reynolds S.E., Wolstenholme A.J., Wonnacott S.;
RT   "Characterization of a nicotinic acetylcholine receptor from the insect
RT   Manduca sexta.";
RL   Eur. J. Neurosci. 10:879-889(1998).
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       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. {ECO:0000305}.
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DR   EMBL; Y09795; CAA70928.1; -; mRNA.
DR   AlphaFoldDB; P91766; -.
DR   SMR; P91766; -.
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:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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; 2.
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   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   Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..516
FT                   /note="Acetylcholine receptor subunit alpha-like"
FT                   /id="PRO_0000000303"
FT   TOPO_DOM        22..243
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        327..465
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        466..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        149..163
FT                   /evidence="ECO:0000250"
FT   DISULFID        222..223
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   516 AA;  58720 MW;  E7A71E8C45D13BD2 CRC64;
     MRSVTKYYLH GVVLFATGCA GNPDAKRLYD DLLSNYNKLV RPVLNVSDAL TVRIKLKLSQ
     LIDVNLKNQI MTTNLWVEQS WYDYKLSWEP REYGGVEMLH VPSDHIWRPD IVLYNNADGN
     FEVTLATKAT LNYTGRVEWR PPAIYKSSCE IDVEYFPFDQ QTCVMKFGSW TYDGFQVDLR
     HIDEVRGTNV VELGVDLSEF YTSVEWDILE VPAVRNEKFY TCCDEPYLDI TFNITMRRKT
     LFYTVNLIIP CMGISFLTVL VFYLPSDSGE KVSLSISILL SLTVFFLLLA EIIPPTSLVV
     PLLGKFVLFT MILDTFSICV TVVVLNVHFR SPQTHTMSPW VRRVFIHVLP RLLVMRRPHY
     RLDPHRSRFA GLVTGAGETT LWDEGSPGVP APPRPPPCAP PLAPCAACAP AEAPALCDAL
     RRWHRCPELH KAIDGINYIA DQTRKEEEST RVKEDWKYVA MVLDRPFLWI FTLAVVVGSA
     GIILQAPTLY DERAPIDVRL SEIAYTAAKP RPPPPR