ID ACHA7_HUMAN Reviewed; 502 AA. AC P36544; A8K7Q4; B4DFS0; Q15826; Q8IUZ4; Q96RH2; Q99555; Q9BXH0; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 5. DT 27-MAR-2024, entry version 226. DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-7; DE Flags: Precursor; GN Name=CHRNA7; Synonyms=NACHRA7; 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). RC TISSUE=Brain; RX PubMed=8145738; RA Peng X., Katz M., Gerzanich V., Anand R., Lindstrom J.; RT "Human alpha 7 acetylcholine receptor: cloning of the alpha 7 subunit from RT the SH-SY5Y cell line and determination of pharmacological properties of RT native receptors and functional alpha 7 homomers expressed in Xenopus RT oocytes."; RL Mol. Pharmacol. 45:546-554(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Hippocampus; RX PubMed=9782083; DOI=10.1006/geno.1998.5363; RA Gault J., Robinson M., Berger R., Drebing C., Logel J., Hopkins J., RA Moore T., Jacobs S., Meriwether J., Choi M.J., Kim E.J., Walton K., RA Buiting K., Davis A., Breese C., Freedman R., Leonard S.; RT "Genomic organization and partial duplication of the human alpha7 neuronal RT nicotinic acetylcholine receptor gene (CHRNA7)."; RL Genomics 52:173-185(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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). 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 SEQUENCE REVISION. RA Groot Kormelink P.J., Luyten W.H.M.L.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala, and Stomach; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). 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] (ISOFORM 3). RC TISSUE=Brain; 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 17-502 (ISOFORM 1). RC TISSUE=Brain; RA Doucette-Stamm L., Monteggia L.M., Donnelly-Roberts D., Wang M.T., Lee J., RA Tian J., Giordano T.; RT "Cloning and sequence of the human alpha-7 nicotinic acetylcholine RT receptor."; RL Drug Dev. Res. 30:252-256(1993). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-502 (ISOFORM 1). RC TISSUE=Retina; RX PubMed=8188270; DOI=10.1006/geno.1994.1075; RA Chini B., Raimondi E., Elgoyhen A.B., Moralli D., Balzaretti M., RA Heinemann S.F.; RT "Molecular cloning and chromosomal localization of the human alpha 7- RT nicotinic receptor subunit gene (CHRNA7)."; RL Genomics 19:379-381(1994). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-129. RX PubMed=11829490; DOI=10.1006/geno.2002.6694; RA Riley B., Williamson M., Collier D., Wilkie H., Makoff A.; RT "A 3-Mb map of a large segmental duplication overlapping the alpha7- RT nicotinic acetylcholine receptor gene (CHRNA7) at human 15q13-q14."; RL Genomics 79:197-209(2002). RN [13] RP SUBUNIT, AND MUTAGENESIS OF GLN-139. 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 [14] RP MASS SPECTROMETRY. RC TISSUE=Mammary cancer; RX PubMed=11840567; RX DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h; RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., RA Zvelebil M.J.; RT "Cluster analysis of an extensive human breast cancer cell line protein RT expression map database."; RL Proteomics 2:212-223(2002). RN [15] RP INTERACTION WITH RIC3. RX PubMed=15504725; DOI=10.1074/jbc.m410039200; RA Williams M.E., Burton B., Urrutia A., Shcherbatko A., Chavez-Noriega L.E., RA Cohen C.J., Aiyar J.; RT "Ric-3 promotes functional expression of the nicotinic acetylcholine RT receptor alpha7 subunit in mammalian cells."; RL J. Biol. Chem. 280:1257-1263(2005). RN [16] 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 [17] 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 [18] RP SUBCELLULAR LOCATION. RX PubMed=27789755; DOI=10.1177/1087057116676086; RA Rex E.B., Shukla N., Gu S., Bredt D., DiSepio D.; RT "A Genome-Wide Arrayed cDNA Screen to Identify Functional Modulators of RT alpha7 Nicotinic Acetylcholine Receptors."; RL SLAS Discovery 22:155-165(2017). RN [19] RP INTERACTION WITH CANX. 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). 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. The CC channel is blocked by alpha-bungarotoxin. CC -!- SUBUNIT: Homopentamer (By similarity). Interacts with RIC3; which is CC required for proper folding and assembly (PubMed:15504725, CC PubMed:16120769). Interacts with LYPD6 (PubMed:27344019). Interacts CC with the alpha-conotoxin RgIA (By similarity). Interacts with alpha- CC conotoxins ImI and ImII (PubMed:15609996). Interacts with CANX CC (PubMed:32783947). {ECO:0000250|UniProtKB:P54131, CC ECO:0000250|UniProtKB:Q05941, ECO:0000269|PubMed:15504725, CC ECO:0000269|PubMed:15609996, ECO:0000269|PubMed:16120769, CC ECO:0000269|PubMed:27344019, ECO:0000269|PubMed:32783947}. CC -!- INTERACTION: CC P36544; P05067: APP; NbExp=4; IntAct=EBI-79333, EBI-77613; CC P36544; PRO_0000000092 [P05067]: APP; NbExp=7; IntAct=EBI-79333, EBI-821758; CC P36544; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-79333, EBI-10693038; CC P36544; Q494W8: CHRFAM7A; NbExp=3; IntAct=EBI-79333, EBI-20798208; CC P36544; Q9UBU7: DBF4; NbExp=3; IntAct=EBI-79333, EBI-372690; CC P36544; Q8N5J2-3: MINDY1; NbExp=3; IntAct=EBI-79333, EBI-12382151; CC P36544; Q09028: RBBP4; NbExp=3; IntAct=EBI-79333, EBI-620823; CC P36544; P55000: SLURP1; NbExp=2; IntAct=EBI-79333, EBI-8830896; CC P36544; Q13573: SNW1; NbExp=3; IntAct=EBI-79333, EBI-632715; CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane CC protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:27789755}; CC Multi-pass membrane protein {ECO:0000255}. Note=TMEM35A/NACHO promotes CC its trafficking to the cell membrane (PubMed:27789755). RIC3 promotes CC its trafficking to the cell membrane (By similarity). CC {ECO:0000250|UniProtKB:Q05941, ECO:0000269|PubMed:27789755}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P36544-1; Sequence=Displayed; CC Name=2; CC IsoId=P36544-2; Sequence=VSP_043019; CC Name=3; CC IsoId=P36544-3; Sequence=VSP_058107, VSP_058108; 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 -!- MASS SPECTROMETRY: Mass=54157.68; Method=MALDI; CC Evidence={ECO:0000269|PubMed:11840567}; CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH37571.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X70297; CAA49778.1; -; mRNA. DR EMBL; U40583; AAA83561.2; -; mRNA. DR EMBL; U62436; AAB40114.1; -; mRNA. DR EMBL; Y08420; CAA69697.1; -; mRNA. DR EMBL; AF385585; AAK68111.1; -; mRNA. DR EMBL; AK292069; BAF84758.1; -; mRNA. DR EMBL; AK294229; BAG57531.1; -; mRNA. DR EMBL; AC004460; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC009562; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC012236; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC021316; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC026150; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC026951; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC058803; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC068448; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC079969; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC087481; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC090829; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC091057; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104266; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104759; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC037571; AAH37571.1; ALT_SEQ; mRNA. DR EMBL; BC101345; AAI01346.1; -; mRNA. DR EMBL; L25827; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; Z23141; CAA80672.1; -; mRNA. DR EMBL; AF332758; AAK19515.1; -; Genomic_DNA. DR CCDS; CCDS10027.1; -. [P36544-1] DR CCDS; CCDS53924.1; -. [P36544-2] DR PIR; G02259; G02259. DR PIR; I37185; ACHUA7. DR RefSeq; NP_000737.1; NM_000746.5. [P36544-1] DR RefSeq; NP_001177384.1; NM_001190455.2. [P36544-2] DR RefSeq; NP_683709.1; NM_148911.1. DR RefSeq; XP_005254807.1; XM_005254750.2. DR RefSeq; XP_016877373.1; XM_017021884.1. DR PDB; 2MAW; NMR; -; A=228-326, A=467-495. DR PDB; 5AFH; X-ray; 2.40 A; A/B/C/D/E=23-227. DR PDB; 5AFJ; X-ray; 2.20 A; A/B/C/D/E=23-227. DR PDB; 5AFK; X-ray; 2.38 A; A/B/C/D/E=23-227. DR PDB; 5AFL; X-ray; 2.38 A; A/B/C/D/E=23-227. DR PDB; 5AFM; X-ray; 2.85 A; A/B/C/D/E=23-227. DR PDB; 5AFN; X-ray; 2.15 A; A/B/C/D/E=23-227. DR PDB; 7EKI; EM; 3.18 A; A/B/C/D/E=1-502. DR PDB; 7EKP; EM; 2.85 A; A/B/C/D/E=1-502. DR PDB; 7EKT; EM; 3.02 A; A/B/C/D/E=1-502. DR PDB; 7KOO; EM; 3.00 A; A/B/C/D/E=24-371, A/B/C/D/E=407-502. DR PDB; 7KOQ; EM; 3.60 A; A/B/C/D/E=24-371, A/B/C/D/E=407-502. DR PDB; 7KOX; EM; 2.70 A; A/B/C/D/E=24-371, A/B/C/D/E=407-502. DR PDB; 7RPM; NMR; -; A/B/C/D/E=231-496. DR PDB; 8C9X; EM; 2.30 A; A/B/C/D/E=24-347, A/B/C/D/E=455-502. DR PDB; 8CAU; EM; 3.40 A; A/B/C/D/E=24-502. DR PDB; 8CE4; EM; 2.70 A; A/B/C/D/E=24-347, A/B/C/D/E=455-502. DR PDB; 8CI1; EM; 2.80 A; A/B/C/D/E=24-347, A/B/C/D/E=455-502. DR PDB; 8CI2; EM; 4.40 A; A/B/C/D/E=24-347, A/B/C/D/E=455-502. DR PDB; 8F4V; NMR; -; A/B/C/D/E=231-496. DR PDB; 8P1H; X-ray; 1.95 A; A/B=361-372. DR PDBsum; 2MAW; -. DR PDBsum; 5AFH; -. DR PDBsum; 5AFJ; -. DR PDBsum; 5AFK; -. DR PDBsum; 5AFL; -. DR PDBsum; 5AFM; -. DR PDBsum; 5AFN; -. DR PDBsum; 7EKI; -. DR PDBsum; 7EKP; -. DR PDBsum; 7EKT; -. DR PDBsum; 7KOO; -. DR PDBsum; 7KOQ; -. DR PDBsum; 7KOX; -. DR PDBsum; 7RPM; -. DR PDBsum; 8C9X; -. DR PDBsum; 8CAU; -. DR PDBsum; 8CE4; -. DR PDBsum; 8CI1; -. DR PDBsum; 8CI2; -. DR PDBsum; 8F4V; -. DR PDBsum; 8P1H; -. DR AlphaFoldDB; P36544; -. DR EMDB; EMD-16513; -. DR EMDB; EMD-16534; -. DR EMDB; EMD-16598; -. DR EMDB; EMD-16665; -. DR EMDB; EMD-16666; -. DR EMDB; EMD-22979; -. DR EMDB; EMD-22980; -. DR EMDB; EMD-22983; -. DR EMDB; EMD-31168; -. DR EMDB; EMD-31172; -. DR EMDB; EMD-31176; -. DR SMR; P36544; -. DR BioGRID; 107561; 26. DR BioGRID; 124609; 2. DR ComplexPortal; CPX-236; Neuronal nicotinic acetylcholine receptor complex, alpha7. DR ComplexPortal; CPX-240; Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2. DR CORUM; P36544; -. DR IntAct; P36544; 15. DR MINT; P36544; -. DR STRING; 9606.ENSP00000407546; -. DR BindingDB; P36544; -. DR ChEMBL; CHEMBL2492; -. DR DrugBank; DB03128; Acetylcholine. DR DrugBank; DB00915; Amantadine. DR DrugBank; DB01351; Amobarbital. DR DrugBank; DB01352; Aprobarbital. DR DrugBank; DB01483; Barbital. DR DrugBank; DB00237; Butabarbital. DR DrugBank; DB00241; Butalbital. DR DrugBank; DB01353; Butobarbital. DR DrugBank; DB09061; Cannabidiol. DR DrugBank; DB00122; Choline. DR DrugBank; DB14006; Choline salicylate. DR DrugBank; DB00565; Cisatracurium. DR DrugBank; DB09028; Cytisine. DR DrugBank; DB00514; Dextromethorphan. DR DrugBank; DB01496; Dihydro-2-thioxo-5-((5-(2-(trifluoromethyl)phenyl)-2-furanyl)methyl)-4,6(1H,5H)-pyrimidinedione. DR DrugBank; DB11726; Encenicline. DR DrugBank; DB07720; Epibatidine. DR DrugBank; DB00898; Ethanol. DR DrugBank; DB00674; Galantamine. DR DrugBank; DB05708; GTS-21. DR DrugBank; DB01354; Heptabarbital. DR DrugBank; DB01355; Hexobarbital. DR DrugBank; DB05137; Lobeline. DR DrugBank; DB00657; Mecamylamine. DR DrugBank; DB14009; Medical Cannabis. DR DrugBank; DB00333; Methadone. DR DrugBank; DB00463; Metharbital. DR DrugBank; DB00849; Methylphenobarbital. DR DrugBank; DB14011; Nabiximols. DR DrugBank; DB00184; Nicotine. DR DrugBank; DB00312; Pentobarbital. DR DrugBank; DB01174; Phenobarbital. DR DrugBank; DB00794; Primidone. DR DrugBank; DB05740; RPI-78M. DR DrugBank; DB00418; Secobarbital. DR DrugBank; DB00202; Succinylcholine. DR DrugBank; DB00306; Talbutal. DR DrugBank; DB00599; Thiopental. DR DrugBank; DB01199; Tubocurarine. DR DrugBank; DB01273; Varenicline. DR DrugCentral; P36544; -. DR GuidetoPHARMACOLOGY; 468; -. DR TCDB; 1.A.9.1.7; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family. DR GlyCosmos; P36544; 3 sites, No reported glycans. DR GlyGen; P36544; 3 sites. DR iPTMnet; P36544; -. DR PhosphoSitePlus; P36544; -. DR SwissPalm; P36544; -. DR BioMuta; CHRNA7; -. DR DMDM; 2506127; -. DR MassIVE; P36544; -. DR PaxDb; 9606-ENSP00000407546; -. DR PeptideAtlas; P36544; -. DR ProteomicsDB; 55212; -. [P36544-2] DR Antibodypedia; 9478; 350 antibodies from 33 providers. DR DNASU; 89832; -. DR Ensembl; ENST00000306901.9; ENSP00000303727.2; ENSG00000175344.19. [P36544-1] DR Ensembl; ENST00000437966.3; ENSP00000399087.3; ENSG00000175344.19. [P36544-3] DR Ensembl; ENST00000454250.7; ENSP00000407546.3; ENSG00000175344.19. [P36544-2] DR Ensembl; ENST00000455693.3; ENSP00000405989.3; ENSG00000274542.1. [P36544-1] DR Ensembl; ENST00000675428.1; ENSP00000502560.1; ENSG00000175344.19. [P36544-2] DR GeneID; 1139; -. DR GeneID; 89832; -. DR KEGG; hsa:1139; -. DR MANE-Select; ENST00000306901.9; ENSP00000303727.2; NM_000746.6; NP_000737.1. DR UCSC; uc001zft.5; human. [P36544-1] DR AGR; HGNC:15781; -. DR AGR; HGNC:1960; -. DR CTD; 1139; -. DR CTD; 89832; -. DR DisGeNET; 1139; -. DR DisGeNET; 89832; -. DR GeneCards; CHRNA7; -. DR GeneReviews; CHRNA7; -. DR HGNC; HGNC:1960; CHRNA7. DR HPA; ENSG00000175344; Tissue enhanced (adrenal gland, intestine). DR MalaCards; CHRNA7; -. DR MIM; 118511; gene. DR neXtProt; NX_P36544; -. DR OpenTargets; ENSG00000175344; -. DR Orphanet; 199318; 15q13.3 microdeletion syndrome. DR PharmGKB; PA114; -. DR PharmGKB; PA26483; -. DR VEuPathDB; HostDB:ENSG00000175344; -. DR eggNOG; KOG3646; Eukaryota. DR GeneTree; ENSGT00940000154617; -. DR HOGENOM; CLU_018074_0_3_1; -. DR InParanoid; P36544; -. DR OMA; QTDWRFA; -. DR OrthoDB; 5489962at2759; -. DR PhylomeDB; P36544; -. DR TreeFam; TF315605; -. DR PathwayCommons; P36544; -. DR Reactome; R-HSA-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors. DR SignaLink; P36544; -. DR SIGNOR; P36544; -. DR BioGRID-ORCS; 1139; 14 hits in 1156 CRISPR screens. DR BioGRID-ORCS; 89832; 23 hits in 1038 CRISPR screens. DR ChiTaRS; CHRNA7; human. DR GeneWiki; CHRFAM7A; -. DR GeneWiki; CHRNA7; -. DR Pharos; P36544; Tchem. DR PRO; PR:P36544; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; P36544; Protein. DR Bgee; ENSG00000175344; Expressed in adrenal tissue and 123 other cell types or tissues. DR ExpressionAtlas; P36544; baseline and differential. DR GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0044853; C:plasma membrane raft; ISS:ARUK-UCL. DR GO; GO:0098794; C:postsynapse; TAS:ARUK-UCL. 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; IDA:UniProtKB. DR GO; GO:0015464; F:acetylcholine receptor activity; IDA:UniProtKB. DR GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IDA:UniProtKB. DR GO; GO:0001540; F:amyloid-beta binding; IPI:UniProtKB. DR GO; GO:0005262; F:calcium channel activity; TAS:ARUK-UCL. DR GO; GO:0017081; F:chloride channel regulator activity; IDA:UniProtKB. DR GO; GO:0005216; F:monoatomic ion channel activity; IDA:ARUK-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0015643; F:toxic substance binding; IDA:UniProtKB. DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISS:ARUK-UCL. DR GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB. DR GO; GO:0050890; P:cognition; IMP:UniProtKB. DR GO; GO:0140059; P:dendrite arborization; ISS:ParkinsonsUK-UCL. DR GO; GO:0097061; P:dendritic spine organization; ISS:ParkinsonsUK-UCL. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IMP:UniProtKB. DR GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL. DR GO; GO:0007613; P:memory; ISS:ARUK-UCL. DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; ISS:ARUK-UCL. DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IDA:ParkinsonsUK-UCL. DR GO; GO:0006811; P:monoatomic ion transport; NAS:UniProtKB. DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IGI:ARUK-UCL. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:MGI. DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISS:ARUK-UCL. DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB. DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; ISS:ARUK-UCL. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:ARUK-UCL. DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:ARUK-UCL. DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISS:ARUK-UCL. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB. DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISS:ARUK-UCL. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:ARUK-UCL. DR GO; GO:1905906; P:regulation of amyloid fibril formation; ISS:ARUK-UCL. DR GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; IGI:ARUK-UCL. DR GO; GO:1905144; P:response to acetylcholine; IDA:ARUK-UCL. DR GO; GO:1904645; P:response to amyloid-beta; ISS:ARUK-UCL. DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB. DR GO; GO:0035094; P:response to nicotine; IDA:UniProtKB. DR GO; GO:0050893; P:sensory processing; ISS:ARUK-UCL. DR GO; GO:0007614; P:short-term memory; ISS:ARUK-UCL. DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB. DR GO; GO:0050808; P:synapse organization; ISS:ARUK-UCL. DR GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central. DR CDD; cd19020; LGIC_ECD_nAChR_A7; 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:SF907; CHRNA7-FAM7A FUSION PROTEIN-RELATED; 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. DR Genevisible; P36544; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond; KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel; KW Membrane; Postsynaptic cell membrane; Receptor; Reference proteome; Signal; KW Synapse; Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1..22 FT /evidence="ECO:0000250" FT CHAIN 23..502 FT /note="Neuronal acetylcholine receptor subunit alpha-7" FT /id="PRO_0000000366" FT TOPO_DOM 23..230 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 231..255 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 262..280 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 296..317 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 318..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 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" FT DISULFID 212..213 FT /note="Associated with receptor activation" FT /evidence="ECO:0000250" FT VAR_SEQ 18 FT /note="H -> HGKATASPPSTPPWDPGHIPGASVRPAPGP (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043019" FT VAR_SEQ 81..102 FT /note="SWTDHYLQWNVSEYPGVKTVRF -> AYSRVPATSMYAGFPLMCSTAN (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_058107" FT VAR_SEQ 103..502 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_058108" FT MUTAGEN 139 FT /note="Q->S: 115-fold more potently inhibited by the FT alpha-conotoxin ImI; but no change in inhibition by the FT alpha-conotoxin ImII." FT /evidence="ECO:0000269|PubMed:15609996" FT CONFLICT 11 FT /note="A -> G (in Ref. 1; CAA49778)" FT /evidence="ECO:0000305" FT CONFLICT 58 FT /note="S -> N (in Ref. 6; AAK68111)" FT /evidence="ECO:0000305" FT CONFLICT 134 FT /note="S -> P (in Ref. 6; AAK68111)" FT /evidence="ECO:0000305" FT CONFLICT 364 FT /note="C -> S (in Ref. 11; CAA80672)" FT /evidence="ECO:0000305" FT CONFLICT 375 FT /note="A -> G (in Ref. 1; CAA49778)" FT /evidence="ECO:0000305" FT CONFLICT 409..413 FT /note="RMACS -> AWPAP (in Ref. 11; CAA80672)" FT /evidence="ECO:0000305" FT HELIX 24..34 FT /evidence="ECO:0007829|PDB:5AFN" FT STRAND 45..49 FT /evidence="ECO:0007829|PDB:7EKI" FT STRAND 52..66 FT /evidence="ECO:0007829|PDB:5AFN" FT TURN 67..70 FT /evidence="ECO:0007829|PDB:5AFN" FT STRAND 78..83 FT /evidence="ECO:0007829|PDB:5AFN" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:5AFN" FT TURN 91..93 FT /evidence="ECO:0007829|PDB:5AFN" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:5AFM" FT STRAND 99..102 FT /evidence="ECO:0007829|PDB:7KOX" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:7KOX" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:7KOX" FT STRAND 119..122 FT /evidence="ECO:0007829|PDB:7KOX" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:5AFN" FT STRAND 137..140 FT /evidence="ECO:0007829|PDB:7KOX" FT STRAND 143..149 FT /evidence="ECO:0007829|PDB:7KOX" FT TURN 155..158 FT /evidence="ECO:0007829|PDB:7KOX" FT STRAND 165..171 FT /evidence="ECO:0007829|PDB:5AFN" FT TURN 175..177 FT /evidence="ECO:0007829|PDB:7KOX" FT STRAND 178..182 FT /evidence="ECO:0007829|PDB:5AFN" FT STRAND 198..200 FT /evidence="ECO:0007829|PDB:5AFN" FT STRAND 205..208 FT /evidence="ECO:0007829|PDB:5AFN" FT TURN 211..213 FT /evidence="ECO:0007829|PDB:7EKI" FT STRAND 217..225 FT /evidence="ECO:0007829|PDB:5AFN" FT HELIX 231..236 FT /evidence="ECO:0007829|PDB:7KOX" FT HELIX 238..253 FT /evidence="ECO:0007829|PDB:7KOX" FT STRAND 256..259 FT /evidence="ECO:0007829|PDB:7EKP" FT HELIX 261..282 FT /evidence="ECO:0007829|PDB:7KOX" FT STRAND 287..289 FT /evidence="ECO:0007829|PDB:7KOO" FT HELIX 292..316 FT /evidence="ECO:0007829|PDB:7KOX" FT STRAND 318..320 FT /evidence="ECO:0007829|PDB:7KOX" FT STRAND 322..324 FT /evidence="ECO:0007829|PDB:7EKP" FT HELIX 329..342 FT /evidence="ECO:0007829|PDB:7KOX" FT TURN 348..352 FT /evidence="ECO:0007829|PDB:7RPM" FT STRAND 353..355 FT /evidence="ECO:0007829|PDB:7RPM" FT HELIX 360..362 FT /evidence="ECO:0007829|PDB:7RPM" FT TURN 366..368 FT /evidence="ECO:0007829|PDB:7RPM" FT TURN 371..373 FT /evidence="ECO:0007829|PDB:7RPM" FT TURN 380..383 FT /evidence="ECO:0007829|PDB:7RPM" FT HELIX 384..389 FT /evidence="ECO:0007829|PDB:7RPM" FT STRAND 392..394 FT /evidence="ECO:0007829|PDB:8F4V" FT TURN 395..397 FT /evidence="ECO:0007829|PDB:7RPM" FT TURN 405..408 FT /evidence="ECO:0007829|PDB:7RPM" FT STRAND 411..413 FT /evidence="ECO:0007829|PDB:8F4V" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:8F4V" FT HELIX 437..454 FT /evidence="ECO:0007829|PDB:7KOX" FT HELIX 459..487 FT /evidence="ECO:0007829|PDB:7KOX" FT HELIX 493..500 FT /evidence="ECO:0007829|PDB:7KOX" SQ SEQUENCE 502 AA; 56449 MW; D94B3A482EAA0E42 CRC64; MRCSPGGVWL ALAASLLHVS LQGEFQRKLY KELVKNYNPL ERPVANDSQP LTVYFSLSLL QIMDVDEKNQ VLTTNIWLQM SWTDHYLQWN VSEYPGVKTV RFPDGQIWKP DILLYNSADE RFDATFHTNV LVNSSGHCQY LPPGIFKSSC YIDVRWFPFD VQHCKLKFGS WSYGGWSLDL QMQEADISGY IPNGEWDLVG IPGKRSERFY ECCKEPYPDV TFTVTMRRRT LYYGLNLLIP CVLISALALL VFLLPADSGE KISLGITVLL SLTVFMLLVA EIMPATSDSV PLIAQYFAST MIIVGLSVVV TVIVLQYHHH DPDGGKMPKW TRVILLNWCA WFLRMKRPGE DKVRPACQHK QRRCSLASVE MSAVAPPPAS NGNLLYIGFR GLDGVHCVPT PDSGVVCGRM ACSPTHDEHL LHGGQPPEGD PDLAKILEEV RYIANRFRCQ DESEAVCSEW KFAACVVDRL CLMAFSVFTI ICTIGILMSA PNFVEAVSKD FA //