ID A0A1B0GV43_HUMAN Unreviewed; 423 AA. AC A0A1B0GV43; DT 05-OCT-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 1. DT 24-JUL-2024, entry version 38. DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-7 {ECO:0000256|ARBA:ARBA00040003}; GN Name=CHRNA7 {ECO:0000313|Ensembl:ENSP00000490365.1}; 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 {ECO:0000313|Ensembl:ENSP00000490365.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Proteomes:UP000005640} 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., Stewart S., RA Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., RA 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 [2] {ECO:0000313|Ensembl:ENSP00000490365.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2024) to UniProtKB. 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 {ECO:0000256|ARBA:ARBA00037502}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic cell membrane CC {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00034104}. Synaptic cell membrane CC {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00034099}. 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:0000256|ARBA:ARBA00037939}. 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; ABBA01038340; -; 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; KF456018; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF456023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF573652; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; A0A1B0GV43; -. DR SMR; A0A1B0GV43; -. DR MassIVE; A0A1B0GV43; -. DR PeptideAtlas; A0A1B0GV43; -. DR Antibodypedia; 9478; 326 antibodies from 33 providers. DR Ensembl; ENST00000637183.1; ENSP00000490365.1; ENSG00000175344.19. DR HGNC; HGNC:1960; CHRNA7. DR VEuPathDB; HostDB:ENSG00000175344; -. DR GeneTree; ENSGT00940000154617; -. DR OMA; QTDWRFA; -. DR ChiTaRS; CHRNA7; human. DR Proteomes; UP000005640; Chromosome 15. DR Bgee; ENSG00000175344; Expressed in adrenal tissue and 123 other cell types or tissues. DR ExpressionAtlas; A0A1B0GV43; baseline and differential. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IEA:InterPro. DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro. 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. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU000687}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, KW ECO:0000256|RuleBase:RU000687}; KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687}; KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257}; KW Receptor {ECO:0000256|ARBA:ARBA00023170}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Synapse {ECO:0000256|ARBA:ARBA00023018}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000687}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU000687}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000687}. FT TRANSMEM 152..177 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU000687" FT TRANSMEM 183..201 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU000687" FT TRANSMEM 213..236 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU000687" FT TRANSMEM 391..411 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU000687" FT DOMAIN 1..151 FT /note="Neurotransmitter-gated ion-channel ligand-binding" FT /evidence="ECO:0000259|Pfam:PF02931" FT DOMAIN 158..407 FT /note="Neurotransmitter-gated ion-channel transmembrane" FT /evidence="ECO:0000259|Pfam:PF02932" SQ SEQUENCE 423 AA; 47434 MW; 38D69334AE8BAF63 CRC64; MSWTDHYLQW NVSEYPGVKT VRFPDGQIWK PDILLYNSAD ERFDATFHTN VLVNSSGHCQ YLPPGIFKSS CYIDVRWFPF DVQHCKLKFG SWSYGGWSLD LQMQEADISG YIPNGEWDLV GIPGKRSERF YECCKEPYPD VTFTVTMRRR TLYYGLNLLI PCVLISALAL LVFLLPADSG EKISLGITVL LSLTVFMLLV AEIMPATSDS VPLIAQYFAS TMIIVGLSVV VTVIVLQYHH HDPDGGKMPK WTRVILLNWC AWFLRMKRPG EDKVRPACQH KQRRCSLASV EMSAVAPPPA SNGNLLYIGF RGLDGVHCVP TPDSGVVCGR MACSPTHDEH LLHGGQPPEG DPDLAKILEE VRYIANRFRC QDESEAVCSE WKFAACVVDR LCLMAFSVFT IICTIGILMS APNFVEAVSK DFA //