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Database: UniProt
Entry: A0A0L8GEB7_OCTBM
LinkDB: A0A0L8GEB7_OCTBM
Original site: A0A0L8GEB7_OCTBM 
ID   A0A0L8GEB7_OCTBM        Unreviewed;       478 AA.
AC   A0A0L8GEB7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Neurotransmitter-gated ion-channel ligand-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=OCBIM_22034848mg {ECO:0000313|EMBL:KOF75367.1};
OS   Octopus bimaculoides (California two-spotted octopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX   NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF75367.1};
RN   [1] {ECO:0000313|EMBL:KOF75367.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF75367.1};
RC   TISSUE=Gonad {ECO:0000313|EMBL:KOF75367.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000256|RuleBase:RU000687}.
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DR   EMBL; KQ422194; KOF75367.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L8GEB7; -.
DR   STRING; 37653.A0A0L8GEB7; -.
DR   EnsemblMetazoa; Ocbimv22034848m; Ocbimv22034848m.p; Ocbimv22034848m.g.
DR   EnsemblMetazoa; XM_014926260.1; XP_014781746.1; LOC106877372.
DR   OMA; HICHEQG; -.
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; 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; 2.
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:SF865; ACETYLCHOLINE RECEPTOR SUBUNIT BETA-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   3: Inferred from homology;
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};
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   TRANSMEM        205..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        236..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        270..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        436..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          18..204
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          211..453
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
SQ   SEQUENCE   478 AA;  55197 MW;  F5FE0C95D0C7CCC7 CRC64;
     MTTRLIRVHQ AHVSQPYVRD MDAKNQVMTT SVWLKHEWFD KRLSWDPKEF GNVKHIKIPS
     DSLWRPDIVL YNNADGDFVI TMTATKATVY FNGKISWEPP AIYKTYCPID VEYFPFDIQK
     CMMRFGSWTY NGLEVDLVHI CHEQGTNKSN GDIVNYMGID LKGYQQNVEW DILDVYAVRK
     IASYPCCPES YIDIRFNLLL RRKPLFYTLN LIAPCVSISL LTVLVFYLPS VSGEKITLSI
     SVLLALSVFF LLLADIIPPT SLVIPLIGKY LMFTMFMVTA SLFLTVYVLN INYRKPTTHS
     MSNWVRYYLL EKLPPYLWMK RPDINDRPLV EIGKVAVRTM NGMEVRELTL DSNTSTLLRS
     DVHTYENMRN RHPTEELEPS GCQVEKPVHY GSSKDVKVVK DIIDNIKYIA NHMKESNEDE
     QVVRDWAYVA MVVDRVLLYL FSLAVTVGTI GCFLSAPAHY DTKVTLQPID FENTSCNY
//
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