ID   A0A348G667_ODOMO        Unreviewed;       333 AA.
AC   A0A348G667;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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   -!- 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:ARBA00034104}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00034104}. Synaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00034099}.
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   AlphaFoldDB; A0A348G667; -.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   CDD; cd19031; LGIC_ECD_nAChR_proto_alpha-like; 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; 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   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945:SF430; ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-LIKE 2; 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   2: Evidence at transcript level;
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="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          242..332
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
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
//