ID   ACHA2_HUMAN             Reviewed;         529 AA.
AC   Q15822; A8KAX3; B4DK19; J3KMY9; Q9HAQ3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   24-JAN-2024, entry version 202.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-2;
DE   Flags: Precursor;
GN   Name=CHRNA2;
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), AND VARIANT ALA-125.
RC   TISSUE=Hypothalamus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-125.
RA   Groot Kormelink P.J.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-125.
RC   TISSUE=Thalamus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 59-265, SUBUNIT, AND MUTAGENESIS
RP   OF TRP-115 AND TYR-225.
RX   PubMed=27493220; DOI=10.1073/pnas.1602619113;
RA   Kouvatsos N., Giastas P., Chroni-Tzartou D., Poulopoulou C., Tzartos S.J.;
RT   "Crystal structure of a human neuronal nAChR extracellular domain in
RT   pentameric assembly: Ligand-bound alpha2 homopentamer.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9635-9640(2016).
RN   [7]
RP   VARIANT ENFL4 ASN-279, AND CHARACTERIZATION OF VARIANT ENFL4 ASN-279.
RX   PubMed=16826524; DOI=10.1086/506459;
RA   Aridon P., Marini C., Di Resta C., Brilli E., De Fusco M., Politi F.,
RA   Parrini E., Manfredi I., Pisano T., Pruna D., Curia G., Cianchetti C.,
RA   Pasqualetti M., Becchetti A., Guerrini R., Casari G.;
RT   "Increased sensitivity of the neuronal nicotinic receptor alpha2 subunit
RT   causes familial epilepsy with nocturnal wandering and ictal fear.";
RL   Am. J. Hum. Genet. 79:342-350(2006).
RN   [8]
RP   VARIANT BFIS6 TRP-376.
RX   PubMed=25847220; DOI=10.1111/epi.12967;
RA   Trivisano M., Terracciano A., Milano T., Cappelletti S., Pietrafusa N.,
RA   Bertini E.S., Vigevano F., Specchio N.;
RT   "Mutation of CHRNA2 in a family with benign familial infantile seizures:
RT   Potential role of nicotinic acetylcholine receptor in various phenotypes of
RT   epilepsy.";
RL   Epilepsia 56:E53-E57(2015).
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   -!- SUBUNIT: Neuronal AChR seems to be composed of two different types of
CC       subunits: alpha and non-alpha (beta). Alpha-2 subunit can be combined
CC       to beta-2 or beta-4 to give rise to functional receptors. The alpha-
CC       2:beta-2 nAChR complex is proposed to be a heteropentamer with two
CC       subtypes: LS (low agonist sensitivity) with a (alpha-2)3:(beta-2)2 and
CC       HS (high agonist sensitivity) with a (alpha-2)2:(beta-2)3
CC       stoichiometry; the subtypes differ in their subunit binding interfaces
CC       which are involved in ligand binding. {ECO:0000305|PubMed:27493220}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q15822-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15822-2; Sequence=VSP_055156;
CC   -!- DISEASE: Epilepsy, nocturnal frontal lobe, 4 (ENFL4) [MIM:610353]: An
CC       autosomal dominant focal epilepsy characterized by nocturnal seizures
CC       associated with fear sensation, tongue movements, and nocturnal
CC       wandering, closely resembling nightmares and sleep walking.
CC       {ECO:0000269|PubMed:16826524}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Seizures, benign familial infantile, 6 (BFIS6) [MIM:610353]: A
CC       form of benign familial infantile epilepsy, a neurologic disorder
CC       characterized by afebrile seizures occurring in clusters during the
CC       first year of life, without neurologic sequelae. BFIS6 inheritance is
CC       autosomal dominant. {ECO:0000269|PubMed:25847220}. Note=The disease may
CC       be 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-2/CHRNA2 sub-
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: With the use of epibatidine as high affinity ligand, an alpha-
CC       2 homopentamer has been purified and crystallized. Its physiological
CC       relevance has not been proven. {ECO:0000305|PubMed:27493220}.
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DR   EMBL; U62431; AAB40109.1; -; mRNA.
DR   EMBL; Y16281; CAA76154.1; -; mRNA.
DR   EMBL; AK296348; BAG59031.1; -; mRNA.
DR   EMBL; AF311103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC153866; AAI53867.1; -; mRNA.
DR   CCDS; CCDS6059.1; -. [Q15822-1]
DR   CCDS; CCDS64856.1; -. [Q15822-2]
DR   RefSeq; NP_000733.2; NM_000742.3. [Q15822-1]
DR   RefSeq; NP_001269384.1; NM_001282455.1. [Q15822-2]
DR   RefSeq; XP_006716345.1; XM_006716282.1.
DR   RefSeq; XP_011542690.1; XM_011544388.1.
DR   PDB; 5FJV; X-ray; 3.20 A; A/B/C/D/E=59-265.
DR   PDBsum; 5FJV; -.
DR   AlphaFoldDB; Q15822; -.
DR   SMR; Q15822; -.
DR   ComplexPortal; CPX-2170; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2.
DR   ComplexPortal; CPX-2190; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta4.
DR   CORUM; Q15822; -.
DR   STRING; 9606.ENSP00000385026; -.
DR   BindingDB; Q15822; -.
DR   ChEMBL; CHEMBL2109230; -.
DR   ChEMBL; CHEMBL2109236; -.
DR   DrugBank; DB00732; Atracurium besylate.
DR   DrugBank; DB00237; Butabarbital.
DR   DrugBank; DB00411; Carbamoylcholine.
DR   DrugBank; DB00565; Cisatracurium.
DR   DrugBank; DB01245; Decamethonium.
DR   DrugBank; DB00514; Dextromethorphan.
DR   DrugBank; DB01135; Doxacurium.
DR   DrugBank; DB07720; Epibatidine.
DR   DrugBank; DB00898; Ethanol.
DR   DrugBank; DB00472; Fluoxetine.
DR   DrugBank; DB00483; Gallamine triethiodide.
DR   DrugBank; DB08960; Hexamethonium.
DR   DrugBank; DB00657; Mecamylamine.
DR   DrugBank; DB01336; Metocurine.
DR   DrugBank; DB00416; Metocurine iodide.
DR   DrugBank; DB01226; Mivacurium.
DR   DrugBank; DB00184; Nicotine.
DR   DrugBank; DB01337; Pancuronium.
DR   DrugBank; DB01338; Pipecuronium.
DR   DrugBank; DB00721; Procaine.
DR   DrugBank; DB00728; Rocuronium.
DR   DrugBank; DB05740; RPI-78M.
DR   DrugBank; DB00202; Succinylcholine.
DR   DrugBank; DB01199; Tubocurarine.
DR   DrugBank; DB01339; Vecuronium.
DR   DrugCentral; Q15822; -.
DR   GuidetoPHARMACOLOGY; 463; -.
DR   GlyCosmos; Q15822; 3 sites, No reported glycans.
DR   GlyGen; Q15822; 3 sites.
DR   iPTMnet; Q15822; -.
DR   PhosphoSitePlus; Q15822; -.
DR   BioMuta; CHRNA2; -.
DR   DMDM; 308153405; -.
DR   MaxQB; Q15822; -.
DR   PaxDb; 9606-ENSP00000385026; -.
DR   PeptideAtlas; Q15822; -.
DR   ProteomicsDB; 60776; -. [Q15822-1]
DR   Antibodypedia; 10197; 195 antibodies from 24 providers.
DR   DNASU; 1135; -.
DR   Ensembl; ENST00000240132.7; ENSP00000240132.2; ENSG00000120903.13. [Q15822-2]
DR   Ensembl; ENST00000407991.3; ENSP00000385026.1; ENSG00000120903.13. [Q15822-1]
DR   GeneID; 1135; -.
DR   KEGG; hsa:1135; -.
DR   MANE-Select; ENST00000407991.3; ENSP00000385026.1; NM_000742.4; NP_000733.2.
DR   UCSC; uc010lur.4; human. [Q15822-1]
DR   AGR; HGNC:1956; -.
DR   CTD; 1135; -.
DR   DisGeNET; 1135; -.
DR   GeneCards; CHRNA2; -.
DR   GeneReviews; CHRNA2; -.
DR   HGNC; HGNC:1956; CHRNA2.
DR   HPA; ENSG00000120903; Tissue enriched (prostate).
DR   MalaCards; CHRNA2; -.
DR   MIM; 118502; gene.
DR   MIM; 610353; phenotype.
DR   neXtProt; NX_Q15822; -.
DR   OpenTargets; ENSG00000120903; -.
DR   Orphanet; 98784; Autosomal dominant nocturnal frontal lobe epilepsy.
DR   PharmGKB; PA26489; -.
DR   VEuPathDB; HostDB:ENSG00000120903; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000158299; -.
DR   HOGENOM; CLU_018074_1_0_1; -.
DR   InParanoid; Q15822; -.
DR   OMA; SSYHWLE; -.
DR   OrthoDB; 5489962at2759; -.
DR   PhylomeDB; Q15822; -.
DR   TreeFam; TF315605; -.
DR   PathwayCommons; Q15822; -.
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; Q15822; -.
DR   BioGRID-ORCS; 1135; 15 hits in 1164 CRISPR screens.
DR   ChiTaRS; CHRNA2; human.
DR   GeneWiki; CHRNA2; -.
DR   GenomeRNAi; 1135; -.
DR   Pharos; Q15822; Tchem.
DR   PRO; PR:Q15822; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q15822; Protein.
DR   Bgee; ENSG00000120903; Expressed in primordial germ cell in gonad and 139 other cell types or tissues.
DR   ExpressionAtlas; Q15822; baseline and differential.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:UniProtKB.
DR   GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0120111; C:neuron projection cytoplasm; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
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:1901363; F:heterocyclic compound binding; IEA:Ensembl.
DR   GO; GO:0050997; F:quaternary ammonium group binding; IEA:Ensembl.
DR   GO; GO:0071316; P:cellular response to nicotine; IEA:Ensembl.
DR   GO; GO:0098828; P:modulation of inhibitory postsynaptic potential; IEA:Ensembl.
DR   GO; GO:0006811; P:monoatomic ion transport; NAS:UniProtKB.
DR   GO; GO:1905144; P:response to acetylcholine; IEA:Ensembl.
DR   GO; GO:0035094; P:response to nicotine; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
DR   CDD; cd19015; LGIC_ECD_nAChR_A2; 1.
DR   CDD; cd19064; LGIC_TM_nAChR; 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:SF757; NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-2; 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; Q15822; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW   Disulfide bond; Epilepsy; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW   Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..529
FT                   /note="Neuronal acetylcholine receptor subunit alpha-2"
FT                   /id="PRO_0000000340"
FT   TOPO_DOM        27..264
FT                   /note="Extracellular"
FT   TRANSMEM        265..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        353..502
FT                   /note="Cytoplasmic"
FT   TRANSMEM        503..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          27..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        183..197
FT                   /evidence="ECO:0000250"
FT   DISULFID        247..248
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         82..96
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055156"
FT   VARIANT         22
FT                   /note="T -> I (in dbSNP:rs2472553)"
FT                   /id="VAR_027639"
FT   VARIANT         125
FT                   /note="T -> A (in dbSNP:rs891398)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:8906617, ECO:0000269|Ref.2"
FT                   /id="VAR_027640"
FT   VARIANT         279
FT                   /note="I -> N (in ENFL4; markedly increases receptor
FT                   sensitivity to acetylcholine; dbSNP:rs104894063)"
FT                   /evidence="ECO:0000269|PubMed:16826524"
FT                   /id="VAR_027641"
FT   VARIANT         376
FT                   /note="R -> W (in BFIS6; uncertain significance;
FT                   dbSNP:rs1018084204)"
FT                   /evidence="ECO:0000269|PubMed:25847220"
FT                   /id="VAR_076498"
FT   MUTAGEN         115
FT                   /note="W->A: Changes ligand activation kinetics in a
FT                   alpha-2(+):alpha-2(-) subunit interface (in LS nAChR
FT                   subtype)."
FT                   /evidence="ECO:0000269|PubMed:27493220"
FT   MUTAGEN         225
FT                   /note="Y->F: Decreases ligand activation in LS nAChR
FT                   subtype; no effect in HS nAChR subtype."
FT                   /evidence="ECO:0000269|PubMed:27493220"
FT   HELIX           61..69
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   STRAND          84..99
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   TURN            100..103
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   STRAND          104..116
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   TURN            124..129
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   STRAND          131..136
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   TURN            137..139
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   TURN            148..150
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   STRAND          162..166
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   TURN            167..169
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   STRAND          170..173
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   STRAND          176..182
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   STRAND          198..205
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   TURN            208..210
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   STRAND          211..215
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   TURN            217..219
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   STRAND          237..245
FT                   /evidence="ECO:0007829|PDB:5FJV"
FT   STRAND          248..258
FT                   /evidence="ECO:0007829|PDB:5FJV"
SQ   SEQUENCE   529 AA;  59765 MW;  E47062A1145E8BCC CRC64;
     MGPSCPVFLS FTKLSLWWLL LTPAGGEEAK RPPPRAPGDP LSSPSPTALP QGGSHTETED
     RLFKHLFRGY NRWARPVPNT SDVVIVRFGL SIAQLIDVDE KNQMMTTNVW LKQEWSDYKL
     RWNPTDFGNI TSLRVPSEMI WIPDIVLYNN ADGEFAVTHM TKAHLFSTGT VHWVPPAIYK
     SSCSIDVTFF PFDQQNCKMK FGSWTYDKAK IDLEQMEQTV DLKDYWESGE WAIVNATGTY
     NSKKYDCCAE IYPDVTYAFV IRRLPLFYTI NLIIPCLLIS CLTVLVFYLP SDCGEKITLC
     ISVLLSLTVF LLLITEIIPS TSLVIPLIGE YLLFTMIFVT LSIVITVFVL NVHHRSPSTH
     TMPHWVRGAL LGCVPRWLLM NRPPPPVELC HPLRLKLSPS YHWLESNVDA EEREVVVEEE
     DRWACAGHVA PSVGTLCSHG HLHSGASGPK AEALLQEGEL LLSPHMQKAL EGVHYIADHL
     RSEDADSSVK EDWKYVAMVI DRIFLWLFII VCFLGTIGLF LPPFLAGMI
//