ID   ACHA7_MOUSE             Reviewed;         502 AA.
AC   P49582;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   04-NOV-2026, entry version 204.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=7601470; DOI=10.1016/0888-7543(95)80228-e;
RA   Orr-Urtreger A., Seldin M.F., Baldini A., Beaudet A.L.;
RT   "Cloning and mapping of the mouse alpha 7-neuronal nicotinic acetylcholine
RT   receptor.";
RL   Genomics 26:399-402(1995).
RN   [2]
RP   FUNCTION, TISSUE SPECIFICITY, AND ACTIVITY REGULATION.
RX   PubMed=12508119; DOI=10.1038/nature01339;
RA   Wang H., Yu M., Ochani M., Amella C.A., Tanovic M., Susarla S., Li J.H.,
RA   Wang H., Yang H., Ulloa L., Al-Abed Y., Czura C.J., Tracey K.J.;
RT   "Nicotinic acetylcholine receptor alpha7 subunit is an essential regulator
RT   of inflammation.";
RL   Nature 421:384-388(2003).
RN   [3]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=15502843; DOI=10.1038/nm1124;
RA   Wang H., Liao H., Ochani M., Justiniani M., Lin X., Yang L., Al-Abed Y.,
RA   Wang H., Metz C., Miller E.J., Tracey K.J., Ulloa L.;
RT   "Cholinergic agonists inhibit HMGB1 release and improve survival in
RT   experimental sepsis.";
RL   Nat. Med. 10:1216-1221(2004).
RN   [4]
RP   FUNCTION, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RX   PubMed=16025117; DOI=10.1038/ni1229;
RA   de Jonge W.J., van der Zanden E.P., The F.O., Bijlsma M.F.,
RA   van Westerloo D.J., Bennink R.J., Berthoud H.R., Uematsu S., Akira S.,
RA   van den Wijngaard R.M., Boeckxstaens G.E.;
RT   "Stimulation of the vagus nerve attenuates macrophage activation by
RT   activating the Jak2-STAT3 signaling pathway.";
RL   Nat. Immunol. 6:844-851(2005).
RN   [5]
RP   FUNCTION.
RX   PubMed=21083424; DOI=10.1089/ars.2010.3555;
RA   Tsoyi K., Jang H.J., Kim J.W., Chang H.K., Lee Y.S., Pae H.O., Kim H.J.,
RA   Seo H.G., Lee J.H., Chung H.T., Chang K.C.;
RT   "Stimulation of alpha7 nicotinic acetylcholine receptor by nicotine
RT   attenuates inflammatory response in macrophages and improves survival in
RT   experimental model of sepsis through heme oxygenase-1 induction.";
RL   Antioxid. Redox Signal. 14:2057-2070(2011).
RN   [6]
RP   FUNCTION.
RX   PubMed=24298024; DOI=10.1093/infdis/jit669;
RA   Kim T.H., Kim S.J., Lee S.M.;
RT   "Stimulation of the alpha7 nicotinic acetylcholine receptor protects
RT   against sepsis by inhibiting Toll-like receptor via phosphoinositide 3-
RT   kinase activation.";
RL   J. Infect. Dis. 209:1668-1677(2014).
RN   [7]
RP   FUNCTION.
RX   PubMed=25259522; DOI=10.1371/journal.pone.0108397;
RA   Maldifassi M.C., Atienza G., Arnalich F., Lopez-Collazo E., Cedillo J.L.,
RA   Martin-Sanchez C., Bordas A., Renart J., Montiel C.;
RT   "A new IRAK-M-mediated mechanism implicated in the anti-inflammatory effect
RT   of nicotine via alpha7 nicotinic receptors in human macrophages.";
RL   PLoS ONE 9:e108397-e108397(2014).
RN   [8]
RP   SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-46; ASN-90 AND ASN-133,
RP   MUTAGENESIS OF ASN-46; ASN-90 AND ASN-133, AND REGION.
RX   PubMed=32783947; DOI=10.1016/j.celrep.2020.108025;
RA   Kweon H.J., Gu S., Witham E., Dhara M., Yu H., Mandon E.D., Jawhari A.,
RA   Bredt D.S.;
RT   "NACHO Engages N-Glycosylation ER Chaperone Pathways for alpha7 Nicotinic
RT   Receptor Assembly.";
RL   Cell Rep. 32:108025-108025(2020).
RN   [9]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=33239400; DOI=10.1523/jneurosci.0876-20.2020;
RA   George A.A., Vieira J.M., Xavier-Jackson C., Gee M.T., Cirrito J.R.,
RA   Bimonte-Nelson H.A., Picciotto M.R., Lukas R.J., Whiteaker P.;
RT   "Implications of Oligomeric Amyloid-Beta (oAbeta42) Signaling through
RT   alpha7beta2-Nicotinic Acetylcholine Receptors (nAChRs) on Basal Forebrain
RT   Cholinergic Neuronal Intrinsic Excitability and Cognitive Decline.";
RL   J. Neurosci. 41:555-575(2021).
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. CHRNA7 forms homopentameric neuronal
CC       acetylcholine receptors abundantly expressed in the central nervous
CC       system, characterized by fast desensitization and high calcium
CC       permeability. Also forms heteropentamers with CHRNB2, mainly expressed
CC       in basal forebrain cholinergic neurons. Involved in the modulation of
CC       calcium-dependent signaling pathways and influences the release of
CC       neurotransmitters, including dopamine, glutamate and GABA. Involved in
CC       the modulation of calcium-dependent signaling pathways and influences
CC       the release of neurotransmitters, including dopamine, glutamate and
CC       GABA (PubMed:33239400). Also expressed in non-neuronal cells such as
CC       immune cells like lymphocytes, monocytes and macrophages
CC       (PubMed:12508119). In T cells, activation induces metabotropic
CC       signaling that results in an increase of intracellular Ca2+
CC       concentrations, independent of ionotropic receptor functions (By
CC       similarity). In macrophages, required for acetylcholine-mediated
CC       inhibition of TNF and other inflammatory cytokine release. Once
CC       activated by acetylcholine, nicotine or other agonists, selectively
CC       inhibits production of pro-inflammatory cytokines while leaving anti-
CC       inflammatory cytokines undisturbed (PubMed:12508119, PubMed:21083424,
CC       PubMed:24298024, PubMed:25259522). Stimulates the cholinergic anti-
CC       inflammatory pathway, controlling inflammation by inhibiting NFKB
CC       nuclear translocation and activating the JAK2-STAT3 pathway,
CC       independently of ion channel activity (PubMed:15502843,
CC       PubMed:16025117, PubMed:25259522). Also expressed in the urothelium
CC       where it modulates reflex bladder activity by increasing intracellular
CC       calcium through internal stores and decreasing basal ATP release (By
CC       similarity). {ECO:0000250|UniProtKB:P36544,
CC       ECO:0000250|UniProtKB:Q05941, ECO:0000269|PubMed:12508119,
CC       ECO:0000269|PubMed:15502843, ECO:0000269|PubMed:16025117,
CC       ECO:0000269|PubMed:21083424, ECO:0000269|PubMed:24298024,
CC       ECO:0000269|PubMed:25259522, ECO:0000269|PubMed:33239400}.
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=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671,
CC         ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P36544};
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; Evidence={ECO:0000250|UniProtKB:P36544};
CC   -!- ACTIVITY REGULATION: Activated by a myriad of ligands such as
CC       acetylcholine, cytisine, nicotine, choline and epibatidine
CC       (PubMed:12508119, PubMed:15502843, PubMed:16025117). Oligomeric
CC       amyloid-beta protein 42 activates specifially CHRNA7:CHRNB2 nAchRs
CC       (PubMed:33239400). Activity is modulated by positive allosteric
CC       modulators (PAMs), such as flavonoids, with a wide range of chemical
CC       diversity, pharmacological sensitivity and efficacy. AChR activity is
CC       inhibited by the antagonists alpha-conotoxons RgIA, ImI and ImII, small
CC       disulfide-constrained peptides from cone snails (By similarity).
CC       {ECO:0000250|UniProtKB:P36544, ECO:0000269|PubMed:12508119,
CC       ECO:0000269|PubMed:15502843, ECO:0000269|PubMed:16025117,
CC       ECO:0000269|PubMed:33239400}.
CC   -!- SUBUNIT: Homopentamer (PubMed:32783947). Can also form heteropentamers
CC       with CHRNB2, mainly found in basal forebrain cholinergic neurons.
CC       Interacts with RIC3; which is required for proper folding and assembly.
CC       Interacts with LYPD6. Interacts with CANX (By similarity).
CC       {ECO:0000250|UniProtKB:P36544, ECO:0000250|UniProtKB:P54131,
CC       ECO:0000250|UniProtKB:Q05941, ECO:0000269|PubMed:32783947}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000250|UniProtKB:Q05941}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:32783947}; Multi-pass
CC       membrane protein {ECO:0000255}. Note=TMEM35A/NACHO promotes its
CC       trafficking to the cell membrane (PubMed:32783947). RIC3 promotes its
CC       trafficking to the cell membrane (By similarity).
CC       {ECO:0000250|UniProtKB:Q05941, ECO:0000269|PubMed:32783947}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain. ALso expressed in immune
CC       cells sucha as macrophages. {ECO:0000269|PubMed:12508119,
CC       ECO:0000269|PubMed:16025117}.
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:0000269|PubMed:32783947}.
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; L37663; AAC42053.1; -; mRNA.
DR   CCDS; CCDS21329.1; -.
DR   PIR; A57175; A57175.
DR   RefSeq; NP_031416.3; NM_007390.3.
DR   AlphaFoldDB; P49582; -.
DR   SMR; P49582; -.
DR   BioGRID; 197934; 2.
DR   ComplexPortal; CPX-234; Neuronal nicotinic acetylcholine receptor complex, alpha7.
DR   ComplexPortal; CPX-238; Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2.
DR   DIP; DIP-48732N; -.
DR   FunCoup; P49582; 875.
DR   IntAct; P49582; 4.
DR   STRING; 10090.ENSMUSP00000032738; -.
DR   BindingDB; P49582; -.
DR   ChEMBL; CHEMBL3365; -.
DR   DrugCentral; P49582; -.
DR   GlyCosmos; P49582; 3 sites, No reported glycans.
DR   GlyGen; P49582; 3 sites.
DR   iPTMnet; P49582; -.
DR   PhosphoSitePlus; P49582; -.
DR   PaxDb; 10090-ENSMUSP00000032738; -.
DR   ProteomicsDB; 286067; -.
DR   DNASU; 11441; -.
DR   Ensembl; ENSMUST00000032738.7; ENSMUSP00000032738.6; ENSMUSG00000030525.9.
DR   GeneID; 11441; -.
DR   KEGG; mmu:11441; -.
DR   UCSC; uc009vel.1; mouse.
DR   AGR; MGI:99779; -.
DR   CTD; 1139; -.
DR   MGI; MGI:99779; Chrna7.
DR   VEuPathDB; HostDB:ENSMUSG00000030525; -.
DR   eggNOG; KOG3646; Eukaryota.
DR   GeneTree; ENSGT00940000154617; -.
DR   HOGENOM; CLU_018074_0_3_1; -.
DR   InParanoid; P49582; -.
DR   OMA; ACHNAPK; -.
DR   OrthoDB; 5975154at2759; -.
DR   PhylomeDB; P49582; -.
DR   Reactome; R-MMU-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR   BioGRID-ORCS; 11441; 5 hits in 77 CRISPR screens.
DR   PRO; PR:P49582; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P49582; protein.
DR   Bgee; ENSMUSG00000030525; Expressed in cerebral cortex marginal layer and 59 other cell types or tissues.
DR   ExpressionAtlas; P49582; baseline and differential.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; ISO:GO_Central.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0032279; C:asymmetric synapse; ISO:GO_Central.
DR   GO; GO:0030673; C:axolemma; IDA:MGI.
DR   GO; GO:0030424; C:axon; ISO:GO_Central.
DR   GO; GO:0034703; C:cation channel complex; ISO:GO_Central.
DR   GO; GO:0009986; C:cell surface; ISO:GO_Central.
DR   GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0043198; C:dendritic shaft; ISO:GO_Central.
DR   GO; GO:0043197; C:dendritic spine; ISO:GO_Central.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0098690; C:glycinergic synapse; ISO:GO_Central.
DR   GO; GO:0030426; C:growth cone; ISO:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:GO_Central.
DR   GO; GO:0098878; C:neurotransmitter receptor complex; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProt.
DR   GO; GO:0044853; C:plasma membrane raft; ISO:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; IDA:SynGO.
DR   GO; GO:0098793; C:presynapse; TAS:ARUK-UCL.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR   GO; GO:0098897; C:spine apparatus membrane; ISO:GO_Central.
DR   GO; GO:0042166; F:acetylcholine binding; ISO:GO_Central.
DR   GO; GO:0015464; F:acetylcholine receptor activity; IDA:ARUK-UCL.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IDA:MGI.
DR   GO; GO:0008179; F:adenylate cyclase binding; ISO:GO_Central.
DR   GO; GO:0001540; F:amyloid-beta binding; ISO:GO_Central.
DR   GO; GO:0051117; F:ATPase binding; ISO:GO_Central.
DR   GO; GO:0017081; F:chloride channel regulator activity; ISO:GO_Central.
DR   GO; GO:0005216; F:monoatomic ion channel activity; ISO:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; ISO:GO_Central.
DR   GO; GO:0097110; F:scaffold protein binding; ISO:GO_Central.
DR   GO; GO:0015643; F:toxic substance binding; ISO:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:UniProtKB.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; ISO:GO_Central.
DR   GO; GO:0095500; P:acetylcholine receptor signaling pathway; IDA:ARUK-UCL.
DR   GO; GO:1990051; P:activation of protein kinase C activity; IDA:UniProt.
DR   GO; GO:0008306; P:associative learning; IMP:MGI.
DR   GO; GO:0042113; P:B cell activation; IMP:MGI.
DR   GO; GO:0048149; P:behavioral response to ethanol; IMP:MGI.
DR   GO; GO:0035095; P:behavioral response to nicotine; IGI:MGI.
DR   GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR   GO; GO:0140059; P:dendrite arborization; IMP:ARUK-UCL.
DR   GO; GO:0097061; P:dendritic spine organization; IMP:ARUK-UCL.
DR   GO; GO:0006897; P:endocytosis; IMP:MGI.
DR   GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR   GO; GO:0060112; P:generation of ovulation cycle rhythm; IMP:MGI.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0007611; P:learning or memory; IGI:ARUK-UCL.
DR   GO; GO:1990806; P:ligand-gated ion channel signaling pathway; ISO:GO_Central.
DR   GO; GO:0051899; P:membrane depolarization; ISO:GO_Central.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IGI:ARUK-UCL.
DR   GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IDA:ARUK-UCL.
DR   GO; GO:0006812; P:monoatomic cation transport; ISO:GO_Central.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; ISO:GO_Central.
DR   GO; GO:0006811; P:monoatomic ion transport; IMP:MGI.
DR   GO; GO:1902430; P:negative regulation of amyloid-beta formation; IEA:Ensembl.
DR   GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IDA:UniProtKB.
DR   GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IDA:UniProtKB.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:GO_Central.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR   GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IMP:MGI.
DR   GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:MGI.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:MGI.
DR   GO; GO:0019228; P:neuronal action potential; ISO:GO_Central.
DR   GO; GO:0042698; P:ovulation cycle; IMP:MGI.
DR   GO; GO:1902004; P:positive regulation of amyloid-beta formation; IGI:ARUK-UCL.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
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; IGI:ARUK-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:GO_Central.
DR   GO; GO:0001988; P:positive regulation of heart rate involved in baroreceptor response to decreased systemic arterial blood pressure; IMP:MGI.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IDA:ARUK-UCL.
DR   GO; GO:0051247; P:positive regulation of protein metabolic process; IGI:ARUK-UCL.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:GO_Central.
DR   GO; GO:1905906; P:regulation of amyloid fibril formation; IGI:ARUK-UCL.
DR   GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR   GO; GO:0014061; P:regulation of norepinephrine secretion; IMP:MGI.
DR   GO; GO:2001023; P:regulation of response to drug; ISO:GO_Central.
DR   GO; GO:0051823; P:regulation of synapse structural plasticity; IMP:ARUK-UCL.
DR   GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; IMP:MGI.
DR   GO; GO:1905144; P:response to acetylcholine; ISO:GO_Central.
DR   GO; GO:1904645; P:response to amyloid-beta; IMP:ARUK-UCL.
DR   GO; GO:0009409; P:response to cold; IDA:ARUK-UCL.
DR   GO; GO:0045471; P:response to ethanol; IMP:MGI.
DR   GO; GO:0032094; P:response to food; IMP:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0035094; P:response to nicotine; IMP:MGI.
DR   GO; GO:0050893; P:sensory processing; IDA:ARUK-UCL.
DR   GO; GO:0050808; P:synapse organization; IGI:ARUK-UCL.
DR   GO; GO:0060084; P:synaptic transmission involved in micturition; ISO:GO_Central.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:MGI.
DR   GO; GO:0042110; P:T cell activation; IMP:MGI.
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_0000000368"
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:0000269|PubMed:32783947"
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, ECO:0000305|PubMed:32783947"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:32783947"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:32783947"
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         46
FT                   /note="N->A: Impairs TMEM35A/NACHO-mediated proper subunit
FT                   assembly and trafficking to cell membrane."
FT                   /evidence="ECO:0000269|PubMed:32783947"
FT   MUTAGEN         90
FT                   /note="N->A: Impairs TMEM35A/NACHO-mediated proper subunit
FT                   assembly and trafficking to cell membrane."
FT                   /evidence="ECO:0000269|PubMed:32783947"
FT   MUTAGEN         133
FT                   /note="N->A: Impairs TMEM35A/NACHO-mediated proper subunit
FT                   assembly and trafficking to cell membrane."
FT                   /evidence="ECO:0000269|PubMed:32783947"
SQ   SEQUENCE   502 AA;  56632 MW;  C9312E5226D120E3 CRC64;
     MCGRRGGIWL 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
     MHGTHPSDGD PDLAKILEEV RYIANRFRCQ DESEVICSEW KFAACVVDRL CLMAFSVFTI
     ICTIGILMSA PNFVEAVSKD FA
//