ID   A0A348G667_ODOMO        Unreviewed;       333 AA.
AC   A0A348G667;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   SubName: Full=Acetylcholine receptor alpha subunit {ECO:0000313|EMBL:BBF97940.1};
DE   Flags: Fragment;
GN   Name=ACHR_OM {ECO:0000313|EMBL:BBF97940.1};
OS   Odontomachus monticola (Trap-jaw ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ponerinae; Ponerini; Odontomachus.
OX   NCBI_TaxID=613454 {ECO:0000313|EMBL:BBF97940.1};
RN   [1] {ECO:0000313|EMBL:BBF97940.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Venom gland and sac {ECO:0000313|EMBL:BBF97940.1};
RA   Kazuma K., Masuko K., Konno K., Inagaki H.;
RT   "Combined Venom Gland Transcriptomic and Venom Peptidomic Analysis of the
RT   Predatory Ant Odontomachus monticola.";
RL   Toxins 9:323-323(2017).
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:0000256|ARBA:ARBA00003328}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00004169}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004169}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily.
CC       {ECO:0000256|ARBA:ARBA00009237}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU000687}.
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DR   EMBL; FX985609; BBF97940.1; -; mRNA.
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; -; 1.
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   2: Evidence at transcript level;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU000687};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU000687};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW   Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:BBF97940.1};
KW   Signal {ECO:0000256|RuleBase:RU000687};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000687};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU000687};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000687}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           18..333
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022261761"
FT   TRANSMEM        236..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        267..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        301..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          22..235
FT                   /note="Neur_chan_LBD"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          242..332
FT                   /note="Neur_chan_memb"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
FT   NON_TER         333
FT                   /evidence="ECO:0000313|EMBL:BBF97940.1"
SQ   SEQUENCE   333 AA;  38256 MW;  1E4CAF3E540A5D81 CRC64;
     MISVLIILLL TAGICNSNPD AKRLYDDLLS NYNRLIRPVS NNTDTVVVKL GLRLSQLIDL
     NLKDQILTTN VWLEHEWQDH KFQWEPLEYG GVTELYVPSE HIWLPDIVLY NNADGEYGVT
     TMTKAILHYT GKVLWTPPAI FKSSCEIDVR YFPFDQQTCF MKFGSWTYDG FQIDLKHINQ
     NVGDKVEVGI DLREYYPSVE WDILGVPAER HTKYYPCCHE PYPDIFFNIT LRRKTLFYTV
     NLIVPCVSIS YLSVLAFYLP ADSGEKIALC INILLSQTMF FLLISEIIPS TSLALPLLGK
     YLLFTMILVG LSVVITIIIL NVHYRKPSTH KMA
//