ID A0A1S3J8U7_LINUN Unreviewed; 489 AA.
AC A0A1S3J8U7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Neuronal acetylcholine receptor subunit alpha-7 isoform X2 {ECO:0000313|RefSeq:XP_013406820.1};
GN Name=LOC106171172 {ECO:0000313|RefSeq:XP_013406820.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013406820.1};
RN [1] {ECO:0000313|RefSeq:XP_013406820.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013406820.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_013406820.1; XM_013551366.1.
DR AlphaFoldDB; A0A1S3J8U7; -.
DR STRING; 7574.A0A1S3J8U7; -.
DR EnsemblMetazoa; g2742.t1; g2742.t1; g2742.
DR EnsemblMetazoa; XM_013551366.1; XP_013406820.1; LOC106171172.
DR GeneID; 106171172; -.
DR KEGG; lak:106171172; -.
DR InParanoid; A0A1S3J8U7; -.
DR OMA; VYECCEE; -.
DR OrthoDB; 2938410at2759; -.
DR Proteomes; UP000085678; Unplaced.
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; cd18997; LGIC_ECD_nAChR; 1.
DR CDD; cd19051; LGIC_TM_cation; 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; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR PANTHER; PTHR18945:SF942; NICOTINIC ACETYLCHOLINE RECEPTOR ALPHA6, ISOFORM E; 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 ECO:0000313|RefSeq:XP_013406820.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
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..25
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT CHAIN 26..489
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5022267282"
FT TRANSMEM 239..258
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 270..288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 300..325
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 464..483
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 29..238
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 245..480
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
SQ SEQUENCE 489 AA; 55727 MW; 6DAA3C5D445DE70B CRC64;
MGNSTKRLFL SLAMLLTVFF QESHQGKHER RLLDTLFVDR AHNVLERPVA NEKDVLNVTF
SLTLQQILDV DEKNQIIHTN IWLDMTWTDY TFIWNEAEFG NISAIRIPAG KLWKPDVLLY
NSASEAFDGT YHTNVVIYSS GYMNWIPPGM FGSSCHIDIT WFPFDMQFCK LKFGTWSYDG
SQVDLVLKSE KGDISSFIKN GEWDLLGVTA KRNEIYYDCC PDTPYVDVTY TINIKRRTLY
YGFNLIIPCV LLSLLAILTF MLPPDAGEKV SLAVTIMLSL TVFLMIVADV LPETSDAVPL
IVIYFGMILA LCSMSVVFSV LVLSYHHRAD DTHDMPSWVK YGICEWLAWI LFVSRPGKDL
SRKAILQRQK LRKMEEKQRN SPSLLANVAE VDDYHRNGLM GVKVDRDTRS KEHFSSDSHA
CSTRNELRNI YKELKVITDK MKDDDSSSVV SSDWKFAAHV IDRLCLITFS AAIVICTLVV
LASTPHGIM
//
