ID   ACHA7_RAT               Reviewed;         502 AA.
AC   Q05941; Q53YK2;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   04-NOV-2026, entry version 187.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-7;
DE            Short=nAChR7;
DE   AltName: Full=Nicotinic acetylcholine receptor subunit alpha-7;
DE   Flags: Precursor;
GN   Name=Chrna7; Synonyms=Acra7;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7678857; DOI=10.1523/jneurosci.13-02-00596.1993;
RA   Seguela P., Wadiche J., Dineley-Miller K., Dani J.A., Patrick J.W.;
RT   "Molecular cloning, functional properties, and distribution of rat brain
RT   alpha 7: a nicotinic cation channel highly permeable to calcium.";
RL   J. Neurosci. 13:596-604(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Boulter J.;
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SEQUENCE REVISION TO 363.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Hartley M.;
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Groot-Kormelink P.J.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH RIC3, MUTAGENESIS OF LEU-433; LYS-435; VAL-440; ASN-445;
RP   ARG-446; PHE-447 AND ARG-448, AND SUBCELLULAR LOCATION.
RX   PubMed=15927954; DOI=10.1074/jbc.m503746200;
RA   Castillo M., Mulet J., Gutierrez L.M., Ortiz J.A., Castelan F., Gerber S.,
RA   Sala S., Sala F., Criado M.;
RT   "Dual role of the RIC-3 protein in trafficking of serotonin and nicotinic
RT   acetylcholine receptors.";
RL   J. Biol. Chem. 280:27062-27068(2005).
RN   [6]
RP   INTERACTION WITH RIC3.
RX   PubMed=16120769; DOI=10.1124/mol.105.017459;
RA   Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R., Gibb A.J.,
RA   Millar N.S.;
RT   "RIC-3 enhances functional expression of multiple nicotinic acetylcholine
RT   receptor subtypes in mammalian cells.";
RL   Mol. Pharmacol. 68:1431-1438(2005).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17709503; DOI=10.4049/jimmunol.179.5.2889;
RA   Razani-Boroujerdi S., Boyd R.T., Davila-Garcia M.I., Nandi J.S.,
RA   Mishra N.C., Singh S.P., Pena-Philippides J.C., Langley R., Sopori M.L.;
RT   "T cells express alpha7-nicotinic acetylcholine receptor subunits that
RT   require a functional TCR and leukocyte-specific protein tyrosine kinase for
RT   nicotine-induced Ca2+ response.";
RL   J. Immunol. 179:2889-2898(2007).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=17510177; DOI=10.1113/jphysiol.2007.135319;
RA   Fayuk D., Yakel J.L.;
RT   "Dendritic Ca2+ signalling due to activation of alpha 7-containing
RT   nicotinic acetylcholine receptors in rat hippocampal neurons.";
RL   J. Physiol. (Lond.) 582:597-611(2007).
RN   [9]
RP   FUNCTION, TISSUE SPECIFICITY, AND ACTIVITY REGULATION.
RX   PubMed=22250215; DOI=10.1113/jphysiol.2011.226860;
RA   Beckel J.M., Birder L.A.;
RT   "Differential expression and function of nicotinic acetylcholine receptors
RT   in the urinary bladder epithelium of the rat.";
RL   J. Physiol. (Lond.) 590:1465-1480(2012).
RN   [10]
RP   MUTAGENESIS OF SER-81 AND LEU-141, AND ACTIVITY REGULATION.
RX   PubMed=25740413; DOI=10.1124/mol.114.096511;
RA   Azam L., Papakyriakou A., Zouridakis M., Giastas P., Tzartos S.J.,
RA   McIntosh J.M.;
RT   "Molecular interaction of alpha-conotoxin RgIA with the rat alpha9alpha10
RT   nicotinic acetylcholine receptor.";
RL   Mol. Pharmacol. 87:855-864(2015).
RN   [11]
RP   ERRATUM OF PUBMED:25740413.
RX   PubMed=27559150; DOI=10.1124/mol.114.096511err;
RA   Azam L., Papakyriakou A., Zouridakis M., Giastas P., Tzartos S.J.,
RA   McIntosh J.M.;
RT   "Corrections to 'Molecular interaction of alpha-conotoxin RgIA with the rat
RT   alpha9alpha10 nicotinic acetylcholine receptor'.";
RL   Mol. Pharmacol. 90:415-417(2016).
CC   -!- FUNCTION: Component of neuronal acetylcholine receptors (nAChRs) that
CC       function as pentameric, ligand-gated cation channels with high calcium
CC       permeability among other activities. nAChRs are excitatory
CC       neurotrasnmitter receptors formed by a collection of nAChR subunits
CC       known to mediate synaptic transmission in the nervous system and the
CC       neuromuscular junction. Each nAchR subunit confers differential
CC       attributes to channel properties, including activation, deactivation
CC       and desensitization kinetics, pH sensitivity, cation permeability, and
CC       binding to allosteric modulators (PubMed:17510177). CHRNA7 forms
CC       homopentameric neuronal acetylcholine receptors abundantly expressed in
CC       the central nervous system, characterized by fast desensitization and
CC       high calcium permeability. Also forms heteropentamers with CHRNB2,
CC       mainly expressed in basal forebrain cholinergic neurons (By
CC       similarity). Involved in the modulation of calcium-dependent signaling
CC       pathways and influences the release of neurotransmitters, including
CC       dopamine, glutamate and GABA (PubMed:17510177). Also expressed in non-
CC       neuronal cells such as immune cells like lymphocytes, monocytes and
CC       macrophages. In T cells, activation induces metabotropic signaling that
CC       results in an increase of intracellular Ca2+ concentrations,
CC       independent of ionotropic receptor functions (PubMed:17709503). In
CC       macrophages, required for acetylcholine-mediated inhibition of TNF and
CC       other inflammatory cytokine release. Once activated by acetylcholine,
CC       nicotine or other agonists, selectively inhibits production of pro-
CC       inflammatory cytokines while leaving anti-inflammatory cytokines
CC       undisturbed. Stimulates the cholinergic anti-inflammatory pathway,
CC       controlling inflammation by inhibiting NFKB nuclear translocation and
CC       activating the JAK2-STAT3 pathway, independently of ion channel
CC       activity (By similarity). Also expressed in the urothelium where it
CC       modulates reflex bladder activity by increasing intracellular calcium
CC       through internal stores and decreasing basal ATP release
CC       (PubMed:22250215). {ECO:0000250|UniProtKB:P36544,
CC       ECO:0000269|PubMed:17510177, ECO:0000269|PubMed:17709503,
CC       ECO:0000269|PubMed:22250215}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671,
CC         ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:17510177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000250|UniProtKB:P02709};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P02709};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=choline(out) = choline(in); Xref=Rhea:RHEA:32751,
CC         ChEBI:CHEBI:15354; Evidence={ECO:0000250|UniProtKB:P36544};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NH4(+)(in) = NH4(+)(out); Xref=Rhea:RHEA:28747,
CC         ChEBI:CHEBI:28938; Evidence={ECO:0000250|UniProtKB:P36544};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143,
CC         ChEBI:CHEBI:32682; Evidence={ECO:0000250|UniProtKB:P36544};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanidine(out) = guanidine(in); Xref=Rhea:RHEA:73883,
CC         ChEBI:CHEBI:30087;
CC   -!- ACTIVITY REGULATION: Activated by a myriad of ligands such as
CC       acetylcholine, cytisine, nicotine, choline and epibatidine
CC       (PubMed:17510177, PubMed:22250215). Oligomeric amyloid-beta protein 42
CC       activates specifially CHRNA7:CHRNB2 nAchRs. Activity is modulated by
CC       positive allosteric modulators (PAMs), such as flavonoids, with a wide
CC       range of chemical diversity, pharmacological sensitivity and efficacy.
CC       AChR activity is inhibited by the antagonists alpha-conotoxons RgIA,
CC       ImI and ImII, small disulfide-constrained peptides from cone snails
CC       (PubMed:25740413). Alpha-conotoxin PnIC selectively inhibits
CC       CHRNA7:CHRNB2 over CHRNA7 homopentamer (By similarity).
CC       {ECO:0000250|UniProtKB:P36544, ECO:0000269|PubMed:17510177,
CC       ECO:0000269|PubMed:22250215, ECO:0000269|PubMed:25740413}.
CC   -!- SUBUNIT: Homopentamer. Can also form heteropentamers with CHRNB2,
CC       mainly found in basal forebrain cholinergic neurons (By similarity).
CC       Interacts with RIC3; which is required for proper folding and assembly
CC       (PubMed:15927954, PubMed:16120769). Interacts with LYPD6 (By
CC       similarity). Interacts with CANX (By similarity).
CC       {ECO:0000250|UniProtKB:P36544, ECO:0000250|UniProtKB:P54131,
CC       ECO:0000269|PubMed:15927954, ECO:0000269|PubMed:16120769,
CC       ECO:0000269|PubMed:25740413}.
CC   -!- INTERACTION:
CC       Q05941; PRO_0000000092 [P05067]: APP; Xeno; NbExp=3; IntAct=EBI-79422, EBI-821758;
CC       Q05941; Q7Z2K8: GPRIN1; Xeno; NbExp=6; IntAct=EBI-79422, EBI-11152848;
CC       Q05941; P60615; Xeno; NbExp=4; IntAct=EBI-79422, EBI-7516391;
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000269|PubMed:17510177}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:15927954}; Multi-pass
CC       membrane protein {ECO:0000255}. Note=RIC3 promotes its trafficking to
CC       the cell membrane (PubMed:15927954). TMEM35A/NACHO promotes its
CC       trafficking to the cell membrane (By similarity).
CC       {ECO:0000250|UniProtKB:P49582, ECO:0000269|PubMed:15927954}.
CC   -!- TISSUE SPECIFICITY: Expressed in neurons (PubMed:17510177). Expressed
CC       in umbrella cells of urothelium (at protein level) (PubMed:22250215).
CC       {ECO:0000269|PubMed:17510177, ECO:0000269|PubMed:22250215}.
CC   -!- PTM: Glycosylations at Asn-46, Asn-90 and Asn-133 are essential for
CC       TMEM35A/NACHO-mediated proper subunit assembly and trafficking to the
CC       cell membrane. {ECO:0000250|UniProtKB:P49582}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-7/CHRNA7 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; S53987; AAB25224.2; -; mRNA.
DR   EMBL; L31619; AAC33136.1; -; mRNA.
DR   EMBL; AY574256; AAS90352.1; -; mRNA.
DR   PIR; T01378; T01378.
DR   RefSeq; NP_036964.3; NM_012832.4.
DR   AlphaFoldDB; Q05941; -.
DR   SMR; Q05941; -.
DR   ComplexPortal; CPX-233; Neuronal nicotinic acetylcholine receptor complex, alpha7.
DR   ComplexPortal; CPX-237; Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2.
DR   FunCoup; Q05941; 1538.
DR   IntAct; Q05941; 5.
DR   STRING; 10116.ENSRNOP00000045255; -.
DR   BindingDB; Q05941; -.
DR   ChEMBL; CHEMBL4980; -.
DR   DrugCentral; Q05941; -.
DR   GuidetoPHARMACOLOGY; 468; -.
DR   GlyCosmos; Q05941; 3 sites, No reported glycans.
DR   GlyGen; Q05941; 3 sites.
DR   iPTMnet; Q05941; -.
DR   PhosphoSitePlus; Q05941; -.
DR   SwissPalm; Q05941; -.
DR   PaxDb; 10116-ENSRNOP00000045255; -.
DR   Ensembl; ENSRNOT00000082487.3; ENSRNOP00000073551.2; ENSRNOG00000010853.9.
DR   Ensembl; ENSRNOT00055025208; ENSRNOP00055020610; ENSRNOG00055014663.
DR   Ensembl; ENSRNOT00060031572; ENSRNOP00060025640; ENSRNOG00060018361.
DR   Ensembl; ENSRNOT00065041441; ENSRNOP00065033852; ENSRNOG00065024127.
DR   GeneID; 25302; -.
DR   KEGG; rno:25302; -.
DR   UCSC; RGD:2348; rat.
DR   AGR; RGD:2348; -.
DR   CTD; 1139; -.
DR   RGD; 2348; Chrna7.
DR   eggNOG; KOG3646; Eukaryota.
DR   GeneTree; ENSGT00940000154617; -.
DR   InParanoid; Q05941; -.
DR   OrthoDB; 11434at9989; -.
DR   PhylomeDB; Q05941; -.
DR   Reactome; R-RNO-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR   PRO; PR:Q05941; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   ExpressionAtlas; Q05941; baseline and differential.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:ARUK-UCL.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR   GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
DR   GO; GO:0030673; C:axolemma; ISO:RGD.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR   GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR   GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR   GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:UniProt.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:0098690; C:glycinergic synapse; IDA:SynGO.
DR   GO; GO:0030426; C:growth cone; IDA:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; EXP:UniProtKB.
DR   GO; GO:0044853; C:plasma membrane raft; IDA:ARUK-UCL.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; IDA:SynGO.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
DR   GO; GO:0098897; C:spine apparatus membrane; IDA:SynGO.
DR   GO; GO:0042166; F:acetylcholine binding; IDA:RGD.
DR   GO; GO:0015464; F:acetylcholine receptor activity; ISO:RGD.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IDA:UniProtKB.
DR   GO; GO:0008179; F:adenylate cyclase binding; IPI:RGD.
DR   GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR   GO; GO:0051117; F:ATPase binding; IDA:RGD.
DR   GO; GO:0017081; F:chloride channel regulator activity; ISO:RGD.
DR   GO; GO:0005216; F:monoatomic ion channel activity; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR   GO; GO:0097110; F:scaffold protein binding; IDA:RGD.
DR   GO; GO:0015643; F:toxic substance binding; ISO:RGD.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:RGD.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0095500; P:acetylcholine receptor signaling pathway; IDA:ARUK-UCL.
DR   GO; GO:1990051; P:activation of protein kinase C activity; ISO:RGD.
DR   GO; GO:0008306; P:associative learning; ISO:RGD.
DR   GO; GO:0042113; P:B cell activation; ISO:RGD.
DR   GO; GO:0048149; P:behavioral response to ethanol; ISO:RGD.
DR   GO; GO:0035095; P:behavioral response to nicotine; ISO:RGD.
DR   GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR   GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0050890; P:cognition; ISO:RGD.
DR   GO; GO:0140059; P:dendrite arborization; ISO:RGD.
DR   GO; GO:0097061; P:dendritic spine organization; ISO:RGD.
DR   GO; GO:0006897; P:endocytosis; ISO:RGD.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR   GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
DR   GO; GO:0060112; P:generation of ovulation cycle rhythm; ISO:RGD.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; ISO:RGD.
DR   GO; GO:0007611; P:learning or memory; IMP:RGD.
DR   GO; GO:0051899; P:membrane depolarization; ISO:RGD.
DR   GO; GO:0007613; P:memory; IDA:ARUK-UCL.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0098815; P:modulation of excitatory postsynaptic potential; ISO:RGD.
DR   GO; GO:0006812; P:monoatomic cation transport; IDA:RGD.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; ISO:RGD.
DR   GO; GO:0006811; P:monoatomic ion transport; ISO:RGD.
DR   GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISO:RGD.
DR   GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; ISO:RGD.
DR   GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR   GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISO:RGD.
DR   GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:RGD.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR   GO; GO:0019228; P:neuronal action potential; IMP:RGD.
DR   GO; GO:0042698; P:ovulation cycle; ISO:RGD.
DR   GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:RGD.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:ARUK-UCL.
DR   GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:RGD.
DR   GO; GO:0001988; P:positive regulation of heart rate involved in baroreceptor response to decreased systemic arterial blood pressure; ISO:RGD.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:RGD.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR   GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:RGD.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:1905906; P:regulation of amyloid fibril formation; ISO:RGD.
DR   GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; ISO:RGD.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR   GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR   GO; GO:0080164; P:regulation of nitric oxide metabolic process; ISO:RGD.
DR   GO; GO:0014061; P:regulation of norepinephrine secretion; ISO:RGD.
DR   GO; GO:0051823; P:regulation of synapse structural plasticity; ISO:RGD.
DR   GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; ISO:RGD.
DR   GO; GO:1905144; P:response to acetylcholine; IDA:ARUK-UCL.
DR   GO; GO:1904645; P:response to amyloid-beta; ISO:RGD.
DR   GO; GO:0046681; P:response to carbamate; IEP:RGD.
DR   GO; GO:0009409; P:response to cold; ISO:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0032094; P:response to food; ISO:RGD.
DR   GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR   GO; GO:0035094; P:response to nicotine; IDA:RGD.
DR   GO; GO:0050893; P:sensory processing; IDA:ARUK-UCL.
DR   GO; GO:0007165; P:signal transduction; ISO:RGD.
DR   GO; GO:0050808; P:synapse organization; ISO:RGD.
DR   GO; GO:0060084; P:synaptic transmission involved in micturition; IDA:UniProt.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IDA:UniProtKB.
DR   GO; GO:0042110; P:T cell activation; ISO:RGD.
DR   CDD; cd19020; LGIC_ECD_nAChR_A7; 1.
DR   CDD; cd19051; LGIC_TM_cation; 1.
DR   FunFam; 1.20.58.390:FF:000007; Neuronal acetylcholine receptor subunit alpha-7; 1.
DR   FunFam; 2.70.170.10:FF:000009; Neuronal acetylcholine receptor subunit alpha-7; 1.
DR   FunFam; 1.20.58.390:FF:000011; neuronal acetylcholine receptor subunit alpha-7; 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   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   1: Evidence at protein level;
KW   Calcium; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW   Ion transport; Ligand-gated ion channel; Membrane; Metal-binding;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..502
FT                   /note="Neuronal acetylcholine receptor subunit alpha-7"
FT                   /id="PRO_0000000369"
FT   TOPO_DOM        23..233
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        316..469
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        470..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          260..267
FT                   /note="Essential for TMEM35A/NACHO-mediated proper subunit
FT                   assembly and trafficking to cell membrane"
FT                   /evidence="ECO:0000250|UniProtKB:P49582"
FT   BINDING         42
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P36544"
FT   BINDING         44
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P36544"
FT   BINDING         172
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P36544"
FT   BINDING         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P36544"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        150..164
FT                   /evidence="ECO:0000250|UniProtKB:P36544"
FT   DISULFID        212..213
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250|UniProtKB:P36544"
FT   MUTAGEN         81
FT                   /note="S->T: 10-fold more potently inhibited by the
FT                   alpha-conotoxin RgIA."
FT                   /evidence="ECO:0000269|PubMed:25740413"
FT   MUTAGEN         141
FT                   /note="L->D: No change in inhibition by the alpha-conotoxin
FT                   RgIA."
FT                   /evidence="ECO:0000269|PubMed:25740413"
FT   MUTAGEN         433
FT                   /note="L->A: Abolishes dependency on RIC3 for functional
FT                   expression."
FT                   /evidence="ECO:0000269|PubMed:15927954"
FT   MUTAGEN         435
FT                   /note="K->A: No effect on dependency on RIC3 for functional
FT                   expression."
FT                   /evidence="ECO:0000269|PubMed:15927954"
FT   MUTAGEN         440
FT                   /note="V->A: Impairs dependency on RIC3 for functional
FT                   expression."
FT                   /evidence="ECO:0000269|PubMed:15927954"
FT   MUTAGEN         445
FT                   /note="N->A: Slightly impairs dependency on RIC3 for
FT                   functional expression."
FT                   /evidence="ECO:0000269|PubMed:15927954"
FT   MUTAGEN         446
FT                   /note="R->A: Impairs dependency on RIC3 for functional
FT                   expression."
FT                   /evidence="ECO:0000269|PubMed:15927954"
FT   MUTAGEN         447
FT                   /note="F->A: Impairs dependency on RIC3 for functional
FT                   expression."
FT                   /evidence="ECO:0000269|PubMed:15927954"
FT   MUTAGEN         448
FT                   /note="R->A: Impairs dependency on RIC3 for functional
FT                   expression."
FT                   /evidence="ECO:0000269|PubMed:15927954"
FT   CONFLICT        447
FT                   /note="F -> N (in Ref. 1; AAB25224)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        469
FT                   /note="R -> P (in Ref. 1; AAB25224)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   502 AA;  56503 MW;  289A30498C7B9A58 CRC64;
     MCGGRGGIWL ALAAALLHVS LQGEFQRRLY KELVKNYNPL ERPVANDSQP LTVYFSLSLL
     QIMDVDEKNQ VLTTNIWLQM SWTDHYLQWN MSEYPGVKNV RFPDGQIWKP DILLYNSADE
     RFDATFHTNV LVNASGHCQY LPPGIFKSSC YIDVRWFPFD VQQCKLKFGS WSYGGWSLDL
     QMQEADISSY IPNGEWDLMG IPGKRNEKFY ECCKEPYPDV TYTVTMRRRT LYYGLNLLIP
     CVLISALALL VFLLPADSGE KISLGITVLL SLTVFMLLVA EIMPATSDSV PLIAQYFAST
     MIIVGLSVVV TVIVLRYHHH DPDGGKMPKW TRIILLNWCA WFLRMKRPGE DKVRPACQHK
     PRRCSLASVE LSAGAGPPTS NGNLLYIGFR GLEGMHCAPT PDSGVVCGRL ACSPTHDEHL
     MHGAHPSDGD PDLAKILEEV RYIANRFRCQ DESEVICSEW KFAACVVDRL CLMAFSVFTI
     ICTIGILMSA PNFVEAVSKD FA
//