ID A4GXC7_DROME Unreviewed; 560 AA.
AC A4GXC7;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Nicotinic acetylcholine receptor Dalpha7 {ECO:0000313|EMBL:ABO26063.1};
GN Name=nAcRalpha18C {ECO:0000313|EMBL:ABO26063.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:ABO26063.1};
RN [1] {ECO:0000313|EMBL:ABO26063.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16494528; DOI=10.1371/journal.pbio.0040063;
RA Fayyazuddin A., Zaheer M.A., Hiesinger P.R., Bellen H.J.;
RT "The nicotinic acetylcholine receptor Dalpha7 is required for an escape
RT behavior in Drosophila.";
RL PLoS Biol. 4:E63-E63(2006).
RN [2] {ECO:0000313|EMBL:ABO26063.1}
RP NUCLEOTIDE SEQUENCE.
RA Fayyazuddin A., Bellen H.J.;
RL Submitted (FEB-2007) 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 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; EF458626; ABO26063.1; -; mRNA.
DR AlphaFoldDB; A4GXC7; -.
DR ChEMBL; CHEMBL3350223; -.
DR VEuPathDB; VectorBase:FBgn0086778; -.
DR HOGENOM; CLU_018074_0_3_1; -.
DR ExpressionAtlas; A4GXC7; baseline and differential.
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:SF932; NICOTINIC ACETYLCHOLINE RECEPTOR ALPHA7, 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 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:ABO26063.1};
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 269..288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 330..353
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 534..558
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 61..268
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 275..550
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 63133 MW; 500A20E796544733 CRC64;
MKKPSRSRPD NPSCPGQDRT RSMSFPQPHS LPEATANGGR MLVYGLGLLI MIPACAAGPH
EKRLLHALLD NYNSLERPVV NESDPLQLSF GLTLMQIIDV DEKNQLLITN IWLKLEWNDM
NLRWNSSEFG GVRDLRIPPH RLWKPDVLMY NSADEGFDGT YATNVVVRNN GSCLYVPPGI
FKSTCKIDIT WFPFDDQRCE MKFGSWTYDG FQLDLQLQDE AGGDISSFIT NGEWDLLGVP
GKRNEIYYNC CPEPYIDITF AILIRRKTLY YFFNLIVPCV LIASMALLGF TLPPDSGEKL
SLGVTILLSL TVFLNMVAET MPATSDAVPL LGTYFNCIMF MVASSVVSTI LVLNYHHRNP
DTHEMSEWIR VIFLYWLPCI LRMQRPGQVG YECPPPPSSS SSSASGEKKQ QIQNVELKER
SSKSLLANVL DIDDDFRCNH RCASATLPHQ PTYYRTMYRQ GDDGSVGPVG PAGPVVDGRL
HEAISHTCLT SSAEYELALI LKELRWITEQ LKKEDETSDI TRDWKFAAMV VDRLCLIIFT
LFTIIATLAV LFSAPHFIFP
//
