ACHA7_HUMAN
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 03-AUG-2022, entry version 217.
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;
RA Logel J., Drebing C., Barnhart M., Antle C., Leonard S.;
RT "Nucleotide sequence and transcript size of the alpha-7 neuronal nicotinic
RT acetylcholine receptor in human postmortem brain.";
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; X70297; CAA49778.1; -; mRNA.
DR EMBL; U40583; AAA83561.1; -; 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 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 AlphaFoldDB; P36544; -.
DR SMR; P36544; -.
DR BioGRID; 107561; 25.
DR BioGRID; 124609; 1.
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; 14.
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; 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 GlyGen; P36544; 3 sites.
DR iPTMnet; P36544; -.
DR PhosphoSitePlus; P36544; -.
DR SwissPalm; P36544; -.
DR BioMuta; CHRNA7; -.
DR DMDM; 2506127; -.
DR MassIVE; P36544; -.
DR PeptideAtlas; P36544; -.
DR PRIDE; P36544; -.
DR ProteomicsDB; 55212; -. [P36544-2]
DR Antibodypedia; 9478; 316 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; 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 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; WDLMGIP; -.
DR OrthoDB; 845098at2759; -.
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 1072 CRISPR screens.
DR BioGRID-ORCS; 89832; 23 hits in 987 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 122 other tissues.
DR ExpressionAtlas; P36544; baseline and differential.
DR Genevisible; P36544; 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: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: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 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:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0005216; F:ion channel activity; IDA:ARUK-UCL.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0015643; F:toxic substance binding; IDA:UniProtKB.
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:0006816; P:calcium ion transport; IDA:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
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:0034220; P:ion transmembrane transport; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006811; P:ion transport; NAS:UniProtKB.
DR GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL.
DR GO; GO:0051899; P:membrane depolarization; IDA:ComplexPortal.
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: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:0050877; P:nervous system process; IBA:GO_Central.
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:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:1901214; P:regulation of neuron death; ISS:ARUK-UCL.
DR GO; GO:0080164; P:regulation of nitric oxide metabolic process; IDA:ComplexPortal.
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 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; 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 alpha-
FT conotoxin ImI; but no change in inhibition by the alpha-
FT 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. 2; AAA83561 and 6; AAK68111)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="S -> P (in Ref. 2; AAA83561 and 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 TURN 395..397
FT /evidence="ECO:0007829|PDB:7RPM"
FT TURN 405..408
FT /evidence="ECO:0007829|PDB:7RPM"
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
