ID A0A348G667_ODOMO Unreviewed; 333 AA. AC A0A348G667; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 13-SEP-2023, entry version 20. 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: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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //