ID A0A3Q3N1E1_9TELE Unreviewed; 521 AA.
AC A0A3Q3N1E1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Acetylcholine receptor subunit delta {ECO:0000256|ARBA:ARBA00039504};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000026069.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000026069.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|RuleBase:RU000687}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU000687}.
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DR AlphaFoldDB; A0A3Q3N1E1; -.
DR STRING; 205130.ENSMAMP00000026069; -.
DR Ensembl; ENSMAMT00000026740.2; ENSMAMP00000026069.1; ENSMAMG00000017489.2.
DR GeneTree; ENSGT00940000159794; -.
DR OrthoDB; 5489962at2759; -.
DR Proteomes; UP000261640; 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; 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:SF61; ACETYLCHOLINE RECEPTOR SUBUNIT DELTA; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
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..23
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT CHAIN 24..521
FT /note="Acetylcholine receptor subunit delta"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5022271124"
FT TRANSMEM 249..272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 314..335
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 476..497
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 27..248
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 255..493
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
SQ SEQUENCE 521 AA; 60483 MW; 72AEE3398A4F0445 CRC64;
MKLQRAAQGV AILLVLFSSE SWCRNEEERL INYLFKERGY NKELRPVKRQ QEAVDIYLAL
TLSNLISLKE ADETLLTNVW IDHTWTDYRL SWNTTEFDGI EMLRLPSSMV WLPEIVLENN
NDAQFQVAYY SNVLVDPTGL CYWLPPAIFR SSCSINVNYF PFDWQNCTLK FTSLTYNAKE
IRMLLKEEAD ETSKWTVEWI IIDPASFTEN GEWEIIHRPA KKNIYKHIPM ESNKHQDITF
YLVIKRKPLF YIVNIIIPCV LISFLASLVY YLPADSGEKM TLSISVLLAQ SVFLLLISQR
LPETSMSIPL IVKYLMFIMV LVTIVVLNCV VVLNLHFRTP STHVMSEWTK KFFLERLPRI
LHMSHPTEAE TYWDGALPRR SSSVGYIATA EEYYSVKSRS ELMFEKQSER HGLMARTTHA
AVVKSQEDGG VTEQLYAEIK PAVDGANYII KHMRNKNDYN EEKDNWSGIA RTVDRLCLFL
VTPVMTFGTI IIFLMGICNH PPHLPFKGDS HDYREENPRL L
//
