ACHA3_HUMAN
ID ACHA3_HUMAN Reviewed; 505 AA.
AC P32297; Q15823; Q4KMN8; Q86U77; Q96RH3; Q99553; Q9BQ93; Q9BRR4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 4.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-3;
DE Flags: Precursor;
GN Name=CHRNA3; Synonyms=NACHRA3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2336208; DOI=10.1016/0304-3940(90)90287-j;
RA Fornasari D., Chini B., Tarroni P., Clementi F.;
RT "Molecular cloning of human neuronal nicotinic receptor alpha 3-subunit.";
RL Neurosci. Lett. 111:351-356(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
RX PubMed=1989896; DOI=10.1016/0014-4886(91)90004-v;
RA Mihovilovic M., Roses A.D.;
RT "Expression of mRNAs in human thymus coding for the alpha 3 subunit of a
RT neuronal acetylcholine receptor.";
RL Exp. Neurol. 111:175-180(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT LEU-23 DEL.
RX PubMed=8906617; DOI=10.1007/bf02736842;
RA Elliott K.J., Ellis S.B., Berckhan K.J., Urrutia A., Chavez-Noriega L.E.,
RA Johnson E.C., Velicelebi G., Harpold M.M.;
RT "Comparative structure of human neuronal alpha 2-alpha 7 and beta 2-beta 4
RT nicotinic acetylcholine receptor subunits and functional expression of the
RT alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and beta 4 subunits.";
RL J. Mol. Neurosci. 7:217-228(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-23 DEL.
RX PubMed=9009220; DOI=10.1016/s0014-5793(96)01383-x;
RA Groot Kormelink P.J., Luyten W.H.M.L.;
RT "Cloning and sequence of full-length cDNAs encoding the human neuronal
RT nicotinic acetylcholine receptor (nAChR) subunits beta3 and beta4 and
RT expression of seven nAChR subunits in the human neuroblastoma cell line SH-
RT SY5Y and/or IMR-32.";
RL FEBS Lett. 400:309-314(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND VARIANT LEU-23 DEL.
RX PubMed=9921897; DOI=10.1007/s004390050885;
RA Rempel N., Heyers S., Engels H., Sleegers E., Steinlein O.K.;
RT "The structures of the human neuronal nicotinic acetylcholine receptor
RT beta2- and alpha3-subunit genes (CHRNB2 and CHRNA3).";
RL Hum. Genet. 103:645-653(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11450844; DOI=10.1007/pl00010921;
RA Lev-Lehman E., Bercovich D., Xu W., Stockton D.W., Beaudet A.L.;
RT "Characterization of the human beta4 nAChR gene and polymorphisms in CHRNA3
RT and CHRNB4.";
RL J. Hum. Genet. 46:362-366(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP LEU-23 DEL.
RC TISSUE=Brain, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-495 (ISOFORMS 1/2).
RC TISSUE=Keratinocyte;
RA Arredondo J., Grando S.A.;
RT "Cloning cholinergic receptors in human keratinocytes.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-505 (ISOFORMS 1/2).
RC TISSUE=Brain;
RA Anand R., Lindstrom J.;
RL Submitted (JUN-1990) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP SUBUNIT.
RX PubMed=15609996; DOI=10.1021/bi048918g;
RA Ellison M., Gao F., Wang H.L., Sine S.M., McIntosh J.M., Olivera B.M.;
RT "Alpha-conotoxins ImI and ImII target distinct regions of the human alpha7
RT nicotinic acetylcholine receptor and distinguish human nicotinic receptor
RT subtypes.";
RL Biochemistry 43:16019-16026(2004).
RN [13]
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 [14]
RP INVOLVEMENT IN SQTL3 AND LUNG CANCER.
RX PubMed=18385720; DOI=10.1038/452537a;
RA Chanock S.J., Hunter D.J.;
RT "Genomics: when the smoke clears.";
RL Nature 452:537-538(2008).
RN [15]
RP INVOLVEMENT IN SQTL3 AND LUNG CANCER.
RX PubMed=18385738; DOI=10.1038/nature06885;
RA Hung R.J., McKay J.D., Gaborieau V., Boffetta P., Hashibe M., Zaridze D.,
RA Mukeria A., Szeszenia-Dabrowska N., Lissowska J., Rudnai P., Fabianova E.,
RA Mates D., Bencko V., Foretova L., Janout V., Chen C., Goodman G.,
RA Field J.K., Liloglou T., Xinarianos G., Cassidy A., McLaughlin J., Liu G.,
RA Narod S., Krokan H.E., Skorpen F., Elvestad M.B., Hveem K., Vatten L.,
RA Linseisen J., Clavel-Chapelon F., Vineis P., Bueno-de-Mesquita H.B.,
RA Lund E., Martinez C., Bingham S., Rasmuson T., Hainaut P., Riboli E.,
RA Ahrens W., Benhamou S., Lagiou P., Trichopoulos D., Holcatova I.,
RA Merletti F., Kjaerheim K., Agudo A., Macfarlane G., Talamini R.,
RA Simonato L., Lowry R., Conway D.I., Znaor A., Healy C., Zelenika D.,
RA Boland A., Delepine M., Foglio M., Lechner D., Matsuda F., Blanche H.,
RA Gut I., Heath S., Lathrop M., Brennan P.;
RT "A susceptibility locus for lung cancer maps to nicotinic acetylcholine
RT receptor subunit genes on 15q25.";
RL Nature 452:633-637(2008).
RN [16]
RP INVOLVEMENT IN SQTL3 AND LUNG CANCER.
RX PubMed=18385739; DOI=10.1038/nature06846;
RA Thorgeirsson T.E., Geller F., Sulem P., Rafnar T., Wiste A.,
RA Magnusson K.P., Manolescu A., Thorleifsson G., Stefansson H., Ingason A.,
RA Stacey S.N., Bergthorsson J.T., Thorlacius S., Gudmundsson J., Jonsson T.,
RA Jakobsdottir M., Saemundsdottir J., Olafsdottir O., Gudmundsson L.J.,
RA Bjornsdottir G., Kristjansson K., Skuladottir H., Isaksson H.J.,
RA Gudbjartsson T., Jones G.T., Mueller T., Gottsaeter A., Flex A.,
RA Aben K.K.H., de Vegt F., Mulders P.F.A., Isla D., Vidal M.J., Asin L.,
RA Saez B., Murillo L., Blondal T., Kolbeinsson H., Stefansson J.G.,
RA Hansdottir I., Runarsdottir V., Pola R., Lindblad B., van Rij A.M.,
RA Dieplinger B., Haltmayer M., Mayordomo J.I., Kiemeney L.A.,
RA Matthiasson S.E., Oskarsson H., Tyrfingsson T., Gudbjartsson D.F.,
RA Gulcher J.R., Jonsson S., Thorsteinsdottir U., Kong A., Stefansson K.;
RT "A variant associated with nicotine dependence, lung cancer and peripheral
RT arterial disease.";
RL Nature 452:638-642(2008).
RN [17]
RP INVOLVEMENT IN SQTL3 AND LUNG CANCER.
RX PubMed=18385676; DOI=10.1038/ng.109;
RA Amos C.I., Wu X., Broderick P., Gorlov I.P., Gu J., Eisen T., Dong Q.,
RA Zhang Q., Gu X., Vijayakrishnan J., Sullivan K., Matakidou A., Wang Y.,
RA Mills G., Doheny K., Tsai Y.-Y., Chen W.V., Shete S., Spitz M.R.,
RA Houlston R.S.;
RT "Genome-wide association scan of tag SNPs identifies a susceptibility locus
RT for lung cancer at 15q25.1.";
RL Nat. Genet. 40:616-622(2008).
RN [18]
RP INTERACTION WITH LYPD6.
RX PubMed=27344019; DOI=10.1111/jnc.13718;
RA Arvaniti M., Jensen M.M., Soni N., Wang H., Klein A.B., Thiriet N.,
RA Pinborg L.H., Muldoon P.P., Wienecke J., Imad Damaj M., Kohlmeier K.A.,
RA Gondre-Lewis M.C., Mikkelsen J.D., Thomsen M.S.;
RT "Functional interaction between Lypd6 and nicotinic acetylcholine
RT receptors.";
RL J. Neurochem. 138:806-820(2016).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN BAIPRCK, VARIANT BAIPRCK
RP 340-SER--ALA-505 DEL, AND CHARACTERIZATION OF VARIANT BAIPRCK
RP 340-SER--ALA-505 DEL.
RX PubMed=31708116; DOI=10.1016/j.ajhg.2019.10.004;
RA Mann N., Kause F., Henze E.K., Gharpure A., Shril S., Connaughton D.M.,
RA Nakayama M., Klaembt V., Majmundar A.J., Wu C.W., Kolvenbach C.M., Dai R.,
RA Chen J., van der Ven A.T., Ityel H., Tooley M.J., Kari J.A., Bownass L.,
RA El Desoky S., De Franco E., Shalaby M., Tasic V., Bauer S.B., Lee R.S.,
RA Beckel J.M., Yu W., Mane S.M., Lifton R.P., Reutter H., Ellard S.,
RA Hibbs R.E., Kawate T., Hildebrandt F.;
RT "CAKUT and autonomic dysfunction caused by acetylcholine receptor
RT mutations.";
RL Am. J. Hum. Genet. 105:1286-1293(2019).
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:0000269|PubMed:31708116}.
CC -!- SUBUNIT: Neuronal AChR is composed of two different types of subunits:
CC alpha and beta. Alpha-3 subunit can be combined to beta-2 or beta-4 to
CC give rise to functional receptors. Interacts with RIC3; which is
CC required for proper folding and assembly (PubMed:16120769). Interacts
CC with LYPD6 (PubMed:27344019). The heteropentamer alpha-3-beta-2
CC interacts with alpha-conotoxins ImI and ImII (PubMed:15609996). The
CC heteropentamer alpha-3-beta-2 interacts with alpha-conotoxins ImI,
CC ImII, PnIA, GID and MII (By similarity). The heteropentamer alpha-3-
CC beta-4 interacts with the alpha-conotoxin ImI (PubMed:15609996).
CC {ECO:0000250|UniProtKB:P04757, ECO:0000269|PubMed:15609996,
CC ECO:0000269|PubMed:16120769, ECO:0000269|PubMed:27344019}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane {ECO:0000269|PubMed:31708116}; Multi-pass
CC membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2;
CC IsoId=P32297-2; Sequence=Displayed;
CC Name=1;
CC IsoId=P32297-1; Sequence=VSP_037750;
CC Name=3;
CC IsoId=P32297-3; Sequence=VSP_037751;
CC -!- POLYMORPHISM: Genetic variations in CHRNA3 have been associated with
CC susceptibility to smoking-related behavioral traits and lung cancer,
CC contributing to the smoking quantitative trait locus 3 (SQTL3)
CC [MIM:612052].
CC -!- DISEASE: Bladder dysfunction, autonomic, with impaired pupillary reflex
CC and secondary CAKUT (BAIPRCK) [MIM:191800]: An autosomal recessive
CC disease characterized by impaired innervation and autonomic dysfunction
CC of the urinary bladder, hydronephrosis, vesicoureteral reflux, small
CC kidneys, recurrent urinary tract infections, and progressive renal
CC insufficiency. Additional autonomic features are impaired pupillary
CC reflex and orthostatic hypotension. The disease manifests in utero or
CC early childhood. {ECO:0000269|PubMed:31708116}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-3/CHRNA3 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; M86383; AAC84176.1; -; mRNA.
DR EMBL; M37981; AAA59942.1; -; mRNA.
DR EMBL; U62432; AAB40110.1; -; mRNA.
DR EMBL; Y08418; CAA69695.1; -; mRNA.
DR EMBL; AJ007783; CAA07682.1; -; Genomic_DNA.
DR EMBL; AJ007784; CAA07682.1; JOINED; Genomic_DNA.
DR EMBL; AJ007785; CAA07682.1; JOINED; Genomic_DNA.
DR EMBL; AJ007786; CAA07682.1; JOINED; Genomic_DNA.
DR EMBL; AJ007787; CAA07682.1; JOINED; Genomic_DNA.
DR EMBL; BT006646; AAP35292.1; -; mRNA.
DR EMBL; BT006897; AAP35543.1; -; mRNA.
DR EMBL; AC027228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC067863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000513; AAH00513.1; -; mRNA.
DR EMBL; BC001642; AAH01642.1; -; mRNA.
DR EMBL; BC002996; AAH02996.1; -; mRNA.
DR EMBL; BC006114; AAH06114.1; -; mRNA.
DR EMBL; BC098443; AAH98443.1; -; mRNA.
DR EMBL; AF385584; AAK68110.1; -; mRNA.
DR EMBL; X53559; CAA37625.1; -; mRNA.
DR CCDS; CCDS10305.1; -. [P32297-2]
DR CCDS; CCDS53964.1; -. [P32297-3]
DR PIR; A37040; A37040.
DR PIR; A53956; A53956.
DR RefSeq; NP_000734.2; NM_000743.4. [P32297-2]
DR RefSeq; NP_001160166.1; NM_001166694.1. [P32297-3]
DR PDB; 4ZK4; X-ray; 1.90 A; A/B/C/D/E=215-230.
DR PDB; 5SYO; X-ray; 2.00 A; A/B/C/D/E=215-230.
DR PDB; 5TVC; X-ray; 1.93 A; A/B/C/D/E=215-230.
DR PDB; 6PV7; EM; 3.34 A; A/D=32-378, A/D=434-505.
DR PDB; 6PV8; EM; 3.87 A; A/D=32-378, A/D=434-505.
DR PDBsum; 4ZK4; -.
DR PDBsum; 5SYO; -.
DR PDBsum; 5TVC; -.
DR PDBsum; 6PV7; -.
DR PDBsum; 6PV8; -.
DR AlphaFoldDB; P32297; -.
DR SMR; P32297; -.
DR BioGRID; 107558; 36.
DR ComplexPortal; CPX-187; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2.
DR ComplexPortal; CPX-210; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4.
DR ComplexPortal; CPX-213; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta4.
DR ComplexPortal; CPX-2192; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3.
DR ComplexPortal; CPX-2193; Neuronal nicotinic acetylcholine receptor complex, alpha3-beta2.
DR ComplexPortal; CPX-2200; Neuronal nicotinic acetylcholine receptor complex, alpha3-beta4.
DR IntAct; P32297; 31.
DR STRING; 9606.ENSP00000315602; -.
DR BindingDB; P32297; -.
DR ChEMBL; CHEMBL3068; -.
DR DrugBank; DB00915; Amantadine.
DR DrugBank; DB01156; Bupropion.
DR DrugBank; DB00237; Butabarbital.
DR DrugBank; DB09028; Cytisine.
DR DrugBank; DB00514; Dextromethorphan.
DR DrugBank; DB07720; Epibatidine.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB00472; Fluoxetine.
DR DrugBank; DB05710; Gantacurium.
DR DrugBank; DB01227; Levacetylmethadol.
DR DrugBank; DB00848; Levamisole.
DR DrugBank; DB00333; Methadone.
DR DrugBank; DB00184; Nicotine.
DR DrugBank; DB01090; Pentolinium.
DR DrugBank; DB00202; Succinylcholine.
DR DrugBank; DB01273; Varenicline.
DR DrugCentral; P32297; -.
DR GuidetoPHARMACOLOGY; 464; -.
DR GlyGen; P32297; 2 sites.
DR iPTMnet; P32297; -.
DR PhosphoSitePlus; P32297; -.
DR BioMuta; CHRNA3; -.
DR DMDM; 254763435; -.
DR MassIVE; P32297; -.
DR PaxDb; P32297; -.
DR PeptideAtlas; P32297; -.
DR PRIDE; P32297; -.
DR ProteomicsDB; 54858; -. [P32297-2]
DR ProteomicsDB; 54859; -. [P32297-1]
DR ProteomicsDB; 54860; -. [P32297-3]
DR Antibodypedia; 15113; 304 antibodies from 33 providers.
DR DNASU; 1136; -.
DR Ensembl; ENST00000326828.6; ENSP00000315602.5; ENSG00000080644.16. [P32297-2]
DR Ensembl; ENST00000348639.7; ENSP00000267951.4; ENSG00000080644.16. [P32297-3]
DR Ensembl; ENST00000559658.5; ENSP00000452896.1; ENSG00000080644.16. [P32297-2]
DR GeneID; 1136; -.
DR KEGG; hsa:1136; -.
DR MANE-Select; ENST00000326828.6; ENSP00000315602.5; NM_000743.5; NP_000734.2.
DR UCSC; uc002beb.4; human. [P32297-2]
DR CTD; 1136; -.
DR DisGeNET; 1136; -.
DR GeneCards; CHRNA3; -.
DR HGNC; HGNC:1957; CHRNA3.
DR HPA; ENSG00000080644; Group enriched (adrenal gland, lymphoid tissue, retina).
DR MalaCards; CHRNA3; -.
DR MIM; 118503; gene.
DR MIM; 191800; phenotype.
DR MIM; 612052; phenotype.
DR neXtProt; NX_P32297; -.
DR OpenTargets; ENSG00000080644; -.
DR PharmGKB; PA113; -.
DR VEuPathDB; HostDB:ENSG00000080644; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000158487; -.
DR HOGENOM; CLU_018074_1_0_1; -.
DR InParanoid; P32297; -.
DR OMA; AEHRLYA; -.
DR OrthoDB; 381858at2759; -.
DR PhylomeDB; P32297; -.
DR TreeFam; TF315605; -.
DR PathwayCommons; P32297; -.
DR Reactome; R-HSA-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR Reactome; R-HSA-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR Reactome; R-HSA-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR SignaLink; P32297; -.
DR BioGRID-ORCS; 1136; 12 hits in 1069 CRISPR screens.
DR ChiTaRS; CHRNA3; human.
DR GeneWiki; CHRNA3; -.
DR GenomeRNAi; 1136; -.
DR Pharos; P32297; Tclin.
DR PRO; PR:P32297; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P32297; protein.
DR Bgee; ENSG00000080644; Expressed in pigmented layer of retina and 138 other tissues.
DR ExpressionAtlas; P32297; baseline and differential.
DR Genevisible; P32297; HS.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0044853; C:plasma membrane raft; ISS:ARUK-UCL.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0042166; F:acetylcholine binding; IC:UniProtKB.
DR GO; GO:0015464; F:acetylcholine receptor activity; IDA:UniProtKB.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:UniProtKB.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0015276; F:ligand-gated ion channel activity; TAS:DFLAT.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISS:ARUK-UCL.
DR GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0035095; P:behavioral response to nicotine; IMP:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; NAS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
DR GO; GO:0051899; P:membrane depolarization; IDA:ComplexPortal.
DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0014056; P:regulation of acetylcholine secretion, neurotransmission; ISS:UniProtKB.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; ISS:UniProtKB.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; ISS:UniProtKB.
DR GO; GO:1905144; P:response to acetylcholine; ISS:ARUK-UCL.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR GO; GO:0060084; P:synaptic transmission involved in micturition; IMP:UniProtKB.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; ISS:UniProtKB.
DR Gene3D; 1.20.58.390; -; 2.
DR Gene3D; 2.70.170.10; -; 1.
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 PANTHER; PTHR18945; PTHR18945; 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; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..505
FT /note="Neuronal acetylcholine receptor subunit alpha-3"
FT /id="PRO_0000000346"
FT TOPO_DOM 32..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04757"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04757"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 159..173
FT /evidence="ECO:0000250"
FT DISULFID 223..224
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..6
FT /note="MGSGPL -> MALAV (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:1989896,
FT ECO:0000303|PubMed:2336208, ECO:0000303|PubMed:9009220"
FT /id="VSP_037750"
FT VAR_SEQ 464..505
FT /note="IQDDWKYVAMVIDRIFLWVFTLVCILGTAGLFLQPLMAREDA -> EQKAQE
FT IQQLKRKEKSTETSDQEPGL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.7"
FT /id="VSP_037751"
FT VARIANT 23
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8906617, ECO:0000269|PubMed:9009220,
FT ECO:0000269|PubMed:9921897"
FT /id="VAR_013240"
FT VARIANT 37
FT /note="R -> H (in dbSNP:rs8192475)"
FT /id="VAR_059110"
FT VARIANT 340..505
FT /note="Missing (in BAIPRCK; loss-of-function variant
FT affecting ion transmembrane transport in response to
FT acetylcholine; does not localize to plasma membrane)"
FT /evidence="ECO:0000269|PubMed:31708116"
FT /id="VAR_083543"
FT CONFLICT 5..14
FT /note="PLSLPLALSP -> ALAAPGAVA (in Ref. 2; AAA59942)"
FT /evidence="ECO:0000305"
FT CONFLICT 12..15
FT /note="LSPP -> CRA (in Ref. 1; AAC84176)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="D -> G (in Ref. 1; AAC84176)"
FT /evidence="ECO:0000305"
FT CONFLICT 134..135
FT /note="DD -> TT (in Ref. 1; AAC84176)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="I -> S (in Ref. 1; AAC84176)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="L -> V (in Ref. 1; AAC84176)"
FT /evidence="ECO:0000305"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:6PV7"
FT STRAND 60..75
FT /evidence="ECO:0007829|PDB:6PV7"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:6PV7"
FT STRAND 80..92
FT /evidence="ECO:0007829|PDB:6PV7"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6PV7"
FT TURN 100..105
FT /evidence="ECO:0007829|PDB:6PV7"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:6PV7"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:6PV7"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:6PV7"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:6PV7"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:6PV7"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:6PV7"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:6PV7"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:6PV7"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6PV7"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:6PV7"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:6PV7"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:6PV7"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:4ZK4"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:4ZK4"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:6PV7"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:6PV7"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:6PV7"
FT HELIX 272..293
FT /evidence="ECO:0007829|PDB:6PV7"
FT HELIX 303..329
FT /evidence="ECO:0007829|PDB:6PV7"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:6PV7"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:6PV7"
FT HELIX 345..349
FT /evidence="ECO:0007829|PDB:6PV7"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:6PV7"
FT HELIX 442..493
FT /evidence="ECO:0007829|PDB:6PV7"
FT TURN 494..499
FT /evidence="ECO:0007829|PDB:6PV7"
SQ SEQUENCE 505 AA; 57480 MW; 478D7712D59ACB2D CRC64;
MGSGPLSLPL ALSPPRLLLL LLLSLLPVAR ASEAEHRLFE RLFEDYNEII RPVANVSDPV
IIHFEVSMSQ LVKVDEVNQI METNLWLKQI WNDYKLKWNP SDYGGAEFMR VPAQKIWKPD
IVLYNNAVGD FQVDDKTKAL LKYTGEVTWI PPAIFKSSCK IDVTYFPFDY QNCTMKFGSW
SYDKAKIDLV LIGSSMNLKD YWESGEWAII KAPGYKHDIK YNCCEEIYPD ITYSLYIRRL
PLFYTINLII PCLLISFLTV LVFYLPSDCG EKVTLCISVL LSLTVFLLVI TETIPSTSLV
IPLIGEYLLF TMIFVTLSIV ITVFVLNVHY RTPTTHTMPS WVKTVFLNLL PRVMFMTRPT
SNEGNAQKPR PLYGAELSNL NCFSRAESKG CKEGYPCQDG MCGYCHHRRI KISNFSANLT
RSSSSESVDA VLSLSALSPE IKEAIQSVKY IAENMKAQNE AKEIQDDWKY VAMVIDRIFL
WVFTLVCILG TAGLFLQPLM AREDA
