ACHD_HUMAN
ID ACHD_HUMAN Reviewed; 517 AA.
AC Q07001; A8K661; B4DT92; Q52LH4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Acetylcholine receptor subunit delta;
DE Flags: Precursor;
GN Name=CHRND; Synonyms=ACHRD;
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=2564429; DOI=10.1523/jneurosci.09-03-01082.1989;
RA Luther M.A., Schoepfer R., Whiting P., Casey B., Blatt Y., Montal M.S.,
RA Montal M., Lindstrom J.;
RT "A muscle acetylcholine receptor is expressed in the human cerebellar
RT medulloblastoma cell line TE671.";
RL J. Neurosci. 9:1082-1096(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Pericardium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart, 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 [6]
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 [7]
RP INVOLVEMENT IN CMS3C, VARIANT CMS3C LYS-402, AND CHARACTERIZATION OF
RP VARIANT CMS3C LYS-402.
RX PubMed=16916845; DOI=10.1093/brain/awl188;
RA Mueller J.S., Baumeister S.K., Schara U., Cossins J., Krause S.,
RA von der Hagen M., Huebner A., Webster R., Beeson D., Lochmueller H.,
RA Abicht A.;
RT "CHRND mutation causes a congenital myasthenic syndrome by impairing co-
RT clustering of the acetylcholine receptor with rapsyn.";
RL Brain 129:2784-2793(2006).
RN [8]
RP INVOLVEMENT IN CMS3C, VARIANTS CMS3B PRO-42 AND LYS-79, VARIANT LEU-114,
RP CHARACTERIZATION OF VARIANTS CMS3B PRO-42 AND LYS-79, AND CHARACTERIZATION
RP OF VARIANT LEU-114.
RX PubMed=18398509; DOI=10.1172/jci34527;
RA Shen X.M., Fukuda T., Ohno K., Sine S.M., Engel A.G.;
RT "Congenital myasthenia-related AChR delta subunit mutation interferes with
RT intersubunit communication essential for channel gating.";
RL J. Clin. Invest. 118:1867-1876(2008).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF VAL-290.
RX PubMed=27375219; DOI=10.1002/humu.23043;
RA Shen X.M., Okuno T., Milone M., Otsuka K., Takahashi K., Komaki H.,
RA Giles E., Ohno K., Engel A.G.;
RT "Mutations causing slow-channel myasthenia reveal that a valine ring in the
RT channel pore of muscle AChR is optimized for stabilizing channel gating.";
RL Hum. Mutat. 37:1051-1059(2016).
RN [10]
RP VARIANT GLU-288.
RX PubMed=8872460; DOI=10.1093/hmg/5.9.1217;
RA Engel A.G., Ohno K., Milone M., Wang H.-L., Nakano S., Bouzat C.,
RA Pruitt J.N. II, Hutchinson D.O., Brengman J.M., Bren N., Sieb J.P.,
RA Sine S.M.;
RT "New mutations in acetylcholine receptor subunit genes reveal heterogeneity
RT in the slow-channel congenital myasthenic syndrome.";
RL Hum. Mol. Genet. 5:1217-1227(1996).
RN [11]
RP VARIANT CMS3A PHE-289, AND CHARACTERIZATION OF VARIANT CMS3A PHE-289.
RX PubMed=11782989; DOI=10.1002/ana.10077;
RA Gomez C.M., Maselli R.A., Vohra B.P.S., Navedo M., Stiles J.R., Charnet P.,
RA Schott K., Rojas L., Keesey J., Verity A., Wollmann R.W.,
RA Lasalde-Dominicci J.;
RT "Novel delta subunit mutation in slow-channel syndrome causes severe
RT weakness by novel mechanisms.";
RL Ann. Neurol. 51:102-112(2002).
RN [12]
RP VARIANT CMS3B LYS-80, AND CHARACTERIZATION OF VARIANT CMS3B LYS-80.
RX PubMed=11435464; DOI=10.1172/jci200112935;
RA Brownlow S., Webster R., Croxen R., Brydson M., Neville B., Lin J.-P.,
RA Vincent A., Newsom-Davis J., Beeson D.;
RT "Acetylcholine receptor delta subunit mutations underlie a fast-channel
RT myasthenic syndrome and arthrogryposis multiplex congenita.";
RL J. Clin. Invest. 108:125-130(2001).
RN [13]
RP VARIANT CMS3B GLN-271, AND CHARACTERIZATION OF VARIANT CMS3B GLN-271.
RX PubMed=12499478; DOI=10.1212/01.wnl.0000042422.87384.2f;
RA Shen X.-M., Ohno K., Fukudome T., Tsujino A., Brengman J.M., De Vivo D.C.,
RA Packer R.J., Engel A.G.;
RT "Congenital myasthenic syndrome caused by low-expressor fast-channel AChR
RT delta subunit mutation.";
RL Neurology 59:1881-1888(2002).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-398.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [15]
RP VARIANT LMPS LEU-95.
RX PubMed=18252226; DOI=10.1016/j.ajhg.2007.11.006;
RA Michalk A., Stricker S., Becker J., Rupps R., Pantzar T., Miertus J.,
RA Botta G., Naretto V.G., Janetzki C., Yaqoob N., Ott C.-E., Seelow D.,
RA Wieczorek D., Fiebig B., Wirth B., Hoopmann M., Walther M., Koerber F.,
RA Blankenburg M., Mundlos S., Heller R., Hoffmann K.;
RT "Acetylcholine receptor pathway mutations explain various fetal akinesia
RT deformation sequence disorders.";
RL Am. J. Hum. Genet. 82:464-476(2008).
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:27375219}.
CC -!- SUBUNIT: Pentamer of two alpha chains, and one each of the beta, delta,
CC and gamma (in immature muscle) or epsilon (in mature muscle) chains.
CC The muscle heteropentamer composed of alpha-1, beta-1, delta, epsilon
CC subunits interacts with the alpha-conotoxin ImII (PubMed:15609996).
CC {ECO:0000269|PubMed:15609996}.
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=Q07001-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q07001-2; Sequence=VSP_046423;
CC -!- DISEASE: Multiple pterygium syndrome, lethal type (LMPS) [MIM:253290]:
CC Multiple pterygia are found infrequently in children with
CC arthrogryposis and in fetuses with fetal akinesia syndrome. In lethal
CC multiple pterygium syndrome there is intrauterine growth retardation,
CC multiple pterygia, and flexion contractures causing severe
CC arthrogryposis and fetal akinesia. Subcutaneous edema can be severe,
CC causing fetal hydrops with cystic hygroma and lung hypoplasia.
CC Oligohydramnios and facial anomalies are frequent.
CC {ECO:0000269|PubMed:18252226}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Myasthenic syndrome, congenital, 3A, slow-channel (CMS3A)
CC [MIM:616321]: A form of congenital myasthenic syndrome, a group of
CC disorders characterized by failure of neuromuscular transmission,
CC including pre-synaptic, synaptic, and post-synaptic disorders that are
CC not of autoimmune origin. Clinical features are easy fatigability and
CC muscle weakness affecting the axial and limb muscles (with hypotonia in
CC early-onset forms), the ocular muscles (leading to ptosis and
CC ophthalmoplegia), and the facial and bulbar musculature (affecting
CC sucking and swallowing, and leading to dysphonia). The symptoms
CC fluctuate and worsen with physical effort. CMS3A is a slow-channel
CC myasthenic syndrome. It is caused by kinetic abnormalities of the AChR,
CC resulting in prolonged AChR channel opening episodes, prolonged
CC endplate currents, and depolarization block. This is associated with
CC calcium overload, which may contribute to subsequent degeneration of
CC the endplate and postsynaptic membrane. {ECO:0000269|PubMed:11782989}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Myasthenic syndrome, congenital, 3B, fast-channel (CMS3B)
CC [MIM:616322]: A form of congenital myasthenic syndrome, a group of
CC disorders characterized by failure of neuromuscular transmission,
CC including pre-synaptic, synaptic, and post-synaptic disorders that are
CC not of autoimmune origin. Clinical features are easy fatigability and
CC muscle weakness affecting the axial and limb muscles (with hypotonia in
CC early-onset forms), the ocular muscles (leading to ptosis and
CC ophthalmoplegia), and the facial and bulbar musculature (affecting
CC sucking and swallowing, and leading to dysphonia). The symptoms
CC fluctuate and worsen with physical effort. CMS3B is a fast-channel
CC myasthenic syndrome. It is caused by kinetic abnormalities of the AChR,
CC resulting in brief opening and activity of the channel, with a rapid
CC decay in endplate current, failure to achieve threshold depolarization
CC of the endplate and consequent failure to fire an action potential.
CC {ECO:0000269|PubMed:11435464, ECO:0000269|PubMed:12499478,
CC ECO:0000269|PubMed:18398509}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Myasthenic syndrome, congenital, 3C, associated with
CC acetylcholine receptor deficiency (CMS3C) [MIM:616323]: A form of
CC congenital myasthenic syndrome, a group of disorders characterized by
CC failure of neuromuscular transmission, including pre-synaptic,
CC synaptic, and post-synaptic disorders that are not of autoimmune
CC origin. Clinical features are easy fatigability and muscle weakness
CC affecting the axial and limb muscles (with hypotonia in early-onset
CC forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and
CC the facial and bulbar musculature (affecting sucking and swallowing,
CC and leading to dysphonia). The symptoms fluctuate and worsen with
CC physical effort. CMS3C is an autosomal recessive disorder of
CC postsynaptic neuromuscular transmission, due to deficiency of AChR at
CC the endplate that results in low amplitude of the miniature endplate
CC potential and current. {ECO:0000269|PubMed:16916845,
CC ECO:0000269|PubMed:18398509}. Note=The disease is caused by variants
CC 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. Delta/CHRND sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X55019; CAA38759.1; -; mRNA.
DR EMBL; AK291526; BAF84215.1; -; mRNA.
DR EMBL; AK300109; BAG61904.1; -; mRNA.
DR EMBL; AK315297; BAG37703.1; -; mRNA.
DR EMBL; AC092165; AAY24102.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW71003.1; -; Genomic_DNA.
DR EMBL; BC093923; AAH93923.1; -; mRNA.
DR EMBL; BC093925; AAH93925.1; -; mRNA.
DR CCDS; CCDS2494.1; -. [Q07001-1]
DR CCDS; CCDS58754.1; -. [Q07001-2]
DR PIR; A60916; A60916.
DR RefSeq; NP_000742.1; NM_000751.2. [Q07001-1]
DR RefSeq; NP_001243586.1; NM_001256657.1. [Q07001-2]
DR RefSeq; NP_001298124.1; NM_001311195.1.
DR RefSeq; NP_001298125.1; NM_001311196.1.
DR AlphaFoldDB; Q07001; -.
DR SMR; Q07001; -.
DR BioGRID; 107566; 66.
DR ComplexPortal; CPX-2179; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma.
DR ComplexPortal; CPX-255; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon.
DR IntAct; Q07001; 52.
DR STRING; 9606.ENSP00000258385; -.
DR BindingDB; Q07001; -.
DR ChEMBL; CHEMBL3011; -.
DR DrugCentral; Q07001; -.
DR GuidetoPHARMACOLOGY; 476; -.
DR TCDB; 1.A.9.1.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR GlyGen; Q07001; 2 sites.
DR iPTMnet; Q07001; -.
DR PhosphoSitePlus; Q07001; -.
DR BioMuta; CHRND; -.
DR DMDM; 543759; -.
DR MaxQB; Q07001; -.
DR PaxDb; Q07001; -.
DR PeptideAtlas; Q07001; -.
DR PRIDE; Q07001; -.
DR Antibodypedia; 20219; 197 antibodies from 26 providers.
DR DNASU; 1144; -.
DR Ensembl; ENST00000258385.8; ENSP00000258385.3; ENSG00000135902.10. [Q07001-1]
DR Ensembl; ENST00000543200.5; ENSP00000438380.1; ENSG00000135902.10. [Q07001-2]
DR GeneID; 1144; -.
DR KEGG; hsa:1144; -.
DR MANE-Select; ENST00000258385.8; ENSP00000258385.3; NM_000751.3; NP_000742.1.
DR UCSC; uc002vsw.5; human. [Q07001-1]
DR CTD; 1144; -.
DR DisGeNET; 1144; -.
DR GeneCards; CHRND; -.
DR GeneReviews; CHRND; -.
DR HGNC; HGNC:1965; CHRND.
DR HPA; ENSG00000135902; Tissue enriched (skeletal).
DR MalaCards; CHRND; -.
DR MIM; 100720; gene.
DR MIM; 253290; phenotype.
DR MIM; 616321; phenotype.
DR MIM; 616322; phenotype.
DR MIM; 616323; phenotype.
DR neXtProt; NX_Q07001; -.
DR OpenTargets; ENSG00000135902; -.
DR Orphanet; 33108; Lethal multiple pterygium syndrome.
DR Orphanet; 98913; Postsynaptic congenital myasthenic syndromes.
DR PharmGKB; PA26497; -.
DR VEuPathDB; HostDB:ENSG00000135902; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000159794; -.
DR HOGENOM; CLU_018074_1_4_1; -.
DR InParanoid; Q07001; -.
DR OMA; NFIVSHM; -.
DR OrthoDB; 588360at2759; -.
DR PhylomeDB; Q07001; -.
DR TreeFam; TF315605; -.
DR PathwayCommons; Q07001; -.
DR Reactome; R-HSA-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR SignaLink; Q07001; -.
DR BioGRID-ORCS; 1144; 24 hits in 1067 CRISPR screens.
DR GeneWiki; CHRND; -.
DR GenomeRNAi; 1144; -.
DR Pharos; Q07001; Tclin.
DR PRO; PR:Q07001; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q07001; protein.
DR Bgee; ENSG00000135902; Expressed in gastrocnemius and 70 other tissues.
DR ExpressionAtlas; Q07001; baseline and differential.
DR Genevisible; Q07001; HS.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; TAS:ProtInc.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045211; C:postsynaptic membrane; NAS:BHF-UCL.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0042166; F:acetylcholine binding; IEA:Ensembl.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IBA:GO_Central.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR GO; GO:0050881; P:musculoskeletal movement; IMP:BHF-UCL.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0050905; P:neuromuscular process; NAS:BHF-UCL.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0003009; P:skeletal muscle contraction; IEA:Ensembl.
DR GO; GO:0048630; P:skeletal muscle tissue growth; IMP:BHF-UCL.
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 Alternative splicing; Cell membrane; Congenital myasthenic syndrome;
KW Disease variant; 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..21
FT /evidence="ECO:0000250"
FT CHAIN 22..517
FT /note="Acetylcholine receptor subunit delta"
FT /id="PRO_0000000322"
FT TOPO_DOM 22..245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 390
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 151..165
FT /evidence="ECO:0000250"
FT VAR_SEQ 67..81
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046423"
FT VARIANT 42
FT /note="L -> P (in CMS3B; results in reduced gating
FT efficiency; slows opening of the channel; decreases
FT probability that the channel will open in response to ACh)"
FT /evidence="ECO:0000269|PubMed:18398509"
FT /id="VAR_073691"
FT VARIANT 79
FT /note="I -> K (in CMS3B; prevents expression of the AChR on
FT the cell surface; is a null mutation; dbSNP:rs121909509)"
FT /evidence="ECO:0000269|PubMed:18398509"
FT /id="VAR_073692"
FT VARIANT 80
FT /note="E -> K (in CMS3B; reduced adult and fetal AChR
FT expression and a reduced probability of both adult and
FT fetal AChR being in the open state; dbSNP:rs121909504)"
FT /evidence="ECO:0000269|PubMed:11435464"
FT /id="VAR_021210"
FT VARIANT 95
FT /note="F -> L (in LMPS; dbSNP:rs121909506)"
FT /evidence="ECO:0000269|PubMed:18252226"
FT /id="VAR_043905"
FT VARIANT 114
FT /note="V -> L (has no appreciable kinetic effects; allows
FT for robust AChR expression; dbSNP:rs760395222)"
FT /evidence="ECO:0000269|PubMed:18398509"
FT /id="VAR_073693"
FT VARIANT 271
FT /note="P -> Q (in CMS3B; burst duration was decreased and
FT disassociation of ACh was increased resulting in brief
FT channel opening episodes; shows abnormal association with
FT alpha CHRNA1 subunit resulting in a decreased number of
FT fully assembled AChRs; dbSNP:rs121909503)"
FT /evidence="ECO:0000269|PubMed:12499478"
FT /id="VAR_021211"
FT VARIANT 288
FT /note="Q -> E (in dbSNP:rs41265127)"
FT /evidence="ECO:0000269|PubMed:8872460"
FT /id="VAR_021212"
FT VARIANT 289
FT /note="S -> F (in CMS3A; delayed closure of AchR ion
FT channels, increasing the propensity for open-channel block,
FT as well as a reduced rate of channel opening;
FT dbSNP:rs121909502)"
FT /evidence="ECO:0000269|PubMed:11782989"
FT /id="VAR_019566"
FT VARIANT 398
FT /note="D -> E (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036031"
FT VARIANT 402
FT /note="E -> K (in CMS3C; results in reduced expression of
FT the AChR at the cell surface; impairs normal clustering of
FT the AChR channel with RAPSN; dbSNP:rs145955590)"
FT /evidence="ECO:0000269|PubMed:16916845"
FT /id="VAR_073694"
FT MUTAGEN 290
FT /note="V->A: Increased length of channel opening."
FT /evidence="ECO:0000269|PubMed:27375219"
SQ SEQUENCE 517 AA; 58895 MW; 195CEF69358758BD CRC64;
MEGPVLTLGL LAALAVCGSW GLNEEERLIR HLFQEKGYNK ELRPVAHKEE SVDVALALTL
SNLISLKEVE ETLTTNVWIE HGWTDNRLKW NAEEFGNISV LRLPPDMVWL PEIVLENNND
GSFQISYSCN VLVYHYGFVY WLPPAIFRSS CPISVTYFPF DWQNCSLKFS SLKYTAKEIT
LSLKQDAKEN RTYPVEWIII DPEGFTENGE WEIVHRPARV NVDPRAPLDS PSRQDITFYL
IIRRKPLFYI INILVPCVLI SFMVNLVFYL PADSGEKTSV AISVLLAQSV FLLLISKRLP
ATSMAIPLIG KFLLFGMVLV TMVVVICVIV LNIHFRTPST HVLSEGVKKL FLETLPELLH
MSRPAEDGPS PGALVRRSSS LGYISKAEEY FLLKSRSDLM FEKQSERHGL ARRLTTARRP
PASSEQAQQE LFNELKPAVD GANFIVNHMR DQNNYNEEKD SWNRVARTVD RLCLFVVTPV
MVVGTAWIFL QGVYNQPPPQ PFPGDPYSYN VQDKRFI
