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Acetylcholine receptor subunit delta

 ACHD_HUMAN              Reviewed;         517 AA.
Q07001; A8K661; B4DT92; Q52LH4;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
25-OCT-2017, entry version 173.
RecName: Full=Acetylcholine receptor subunit delta;
Flags: Precursor;
Name=CHRND; Synonyms=ACHRD;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2564429;
Luther M.A., Schoepfer R., Whiting P., Casey B., Blatt Y.,
Montal M.S., Montal M., Lindstrom J.;
"A muscle acetylcholine receptor is expressed in the human cerebellar
medulloblastoma cell line TE671.";
J. Neurosci. 9:1082-1096(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Pericardium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Heart, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
SUBUNIT.
PubMed=15609996; DOI=10.1021/bi048918g;
Ellison M., Gao F., Wang H.L., Sine S.M., McIntosh J.M., Olivera B.M.;
"Alpha-conotoxins ImI and ImII target distinct regions of the human
alpha7 nicotinic acetylcholine receptor and distinguish human
nicotinic receptor subtypes.";
Biochemistry 43:16019-16026(2004).
[7]
INVOLVEMENT IN CMS3C, VARIANT CMS3C LYS-402, AND CHARACTERIZATION OF
VARIANT CMS3C LYS-402.
PubMed=16916845; DOI=10.1093/brain/awl188;
Mueller J.S., Baumeister S.K., Schara U., Cossins J., Krause S.,
von der Hagen M., Huebner A., Webster R., Beeson D., Lochmueller H.,
Abicht A.;
"CHRND mutation causes a congenital myasthenic syndrome by impairing
co-clustering of the acetylcholine receptor with rapsyn.";
Brain 129:2784-2793(2006).
[8]
INVOLVEMENT IN CMS3C, VARIANTS CMS3B PRO-42 AND LYS-79, VARIANT
LEU-114, CHARACTERIZATION OF VARIANTS CMS3B PRO-42 AND LYS-79, AND
CHARACTERIZATION OF VARIANT LEU-114.
PubMed=18398509; DOI=10.1172/JCI34527;
Shen X.M., Fukuda T., Ohno K., Sine S.M., Engel A.G.;
"Congenital myasthenia-related AChR delta subunit mutation interferes
with intersubunit communication essential for channel gating.";
J. Clin. Invest. 118:1867-1876(2008).
[9]
FUNCTION, AND MUTAGENESIS OF VAL-290.
PubMed=27375219; DOI=10.1002/humu.23043;
Shen X.M., Okuno T., Milone M., Otsuka K., Takahashi K., Komaki H.,
Giles E., Ohno K., Engel A.G.;
"Mutations causing slow-channel myasthenia reveal that a valine ring
in the channel pore of muscle AChR is optimized for stabilizing
channel gating.";
Hum. Mutat. 37:1051-1059(2016).
[10]
VARIANT CMS3A GLU-288.
PubMed=8872460; DOI=10.1093/hmg/5.9.1217;
Engel A.G., Ohno K., Milone M., Wang H.-L., Nakano S., Bouzat C.,
Pruitt J.N. II, Hutchinson D.O., Brengman J.M., Bren N., Sieb J.P.,
Sine S.M.;
"New mutations in acetylcholine receptor subunit genes reveal
heterogeneity in the slow-channel congenital myasthenic syndrome.";
Hum. Mol. Genet. 5:1217-1227(1996).
[11]
VARIANT CMS3A PHE-289, AND CHARACTERIZATION OF VARIANT CMS3A PHE-289.
PubMed=11782989; DOI=10.1002/ana.10077;
Gomez C.M., Maselli R.A., Vohra B.P.S., Navedo M., Stiles J.R.,
Charnet P., Schott K., Rojas L., Keesey J., Verity A., Wollmann R.W.,
Lasalde-Dominicci J.;
"Novel delta subunit mutation in slow-channel syndrome causes severe
weakness by novel mechanisms.";
Ann. Neurol. 51:102-112(2002).
[12]
VARIANT CMS3B LYS-80, AND CHARACTERIZATION OF VARIANT CMS3B LYS-80.
PubMed=11435464; DOI=10.1172/JCI200112935;
Brownlow S., Webster R., Croxen R., Brydson M., Neville B., Lin J.-P.,
Vincent A., Newsom-Davis J., Beeson D.;
"Acetylcholine receptor delta subunit mutations underlie a fast-
channel myasthenic syndrome and arthrogryposis multiplex congenita.";
J. Clin. Invest. 108:125-130(2001).
[13]
VARIANT CMS3B GLN-271, AND CHARACTERIZATION OF VARIANT CMS3B GLN-271.
PubMed=12499478; DOI=10.1212/01.WNL.0000042422.87384.2F;
Shen X.-M., Ohno K., Fukudome T., Tsujino A., Brengman J.M.,
De Vivo D.C., Packer R.J., Engel A.G.;
"Congenital myasthenic syndrome caused by low-expressor fast-channel
AChR delta subunit mutation.";
Neurology 59:1881-1888(2002).
[14]
VARIANT [LARGE SCALE ANALYSIS] GLU-398.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[15]
VARIANT LMPS LEU-95.
PubMed=18252226; DOI=10.1016/j.ajhg.2007.11.006;
Michalk A., Stricker S., Becker J., Rupps R., Pantzar T., Miertus J.,
Botta G., Naretto V.G., Janetzki C., Yaqoob N., Ott C.-E., Seelow D.,
Wieczorek D., Fiebig B., Wirth B., Hoopmann M., Walther M.,
Koerber F., Blankenburg M., Mundlos S., Heller R., Hoffmann K.;
"Acetylcholine receptor pathway mutations explain various fetal
akinesia deformation sequence disorders.";
Am. J. Hum. Genet. 82:464-476(2008).
-!- FUNCTION: After binding acetylcholine, the AChR responds by an
extensive change in conformation that affects all subunits and
leads to opening of an ion-conducting channel across the plasma
membrane. {ECO:0000269|PubMed:27375219}.
-!- SUBUNIT: Pentamer of two alpha chains, and one each of the beta,
delta, and gamma (in immature muscle) or epsilon (in mature
muscle) chains. The muscle heteropentamer composed of alpha-1,
beta-1, delta, epsilon subunits interacts with the alpha-conotoxin
ImII (PubMed:15609996). {ECO:0000269|PubMed:15609996}.
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q07001-1; Sequence=Displayed;
Name=2;
IsoId=Q07001-2; Sequence=VSP_046423;
Note=No experimental confirmation available.;
-!- DISEASE: Multiple pterygium syndrome, lethal type (LMPS)
[MIM:253290]: Multiple pterygia are found infrequently in children
with arthrogryposis and in fetuses with fetal akinesia syndrome.
In lethal multiple pterygium syndrome there is intrauterine growth
retardation, multiple pterygia, and flexion contractures causing
severe arthrogryposis and fetal akinesia. Subcutaneous edema can
be severe, causing fetal hydrops with cystic hygroma and lung
hypoplasia. Oligohydramnios and facial anomalies are frequent.
{ECO:0000269|PubMed:18252226}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Myasthenic syndrome, congenital, 3A, slow-channel (CMS3A)
[MIM:616321]: A form of congenital myasthenic syndrome, a group of
disorders characterized by failure of neuromuscular transmission,
including pre-synaptic, synaptic, and post-synaptic disorders that
are not of autoimmune origin. Clinical features are easy
fatigability and muscle weakness affecting the axial and limb
muscles (with hypotonia in early-onset forms), the ocular muscles
(leading to ptosis and ophthalmoplegia), and the facial and bulbar
musculature (affecting sucking and swallowing, and leading to
dysphonia). The symptoms fluctuate and worsen with physical
effort. CMS3A is a slow-channel myasthenic syndrome. It is caused
by kinetic abnormalities of the AChR, resulting in prolonged AChR
channel opening episodes, prolonged endplate currents, and
depolarization block. This is associated with calcium overload,
which may contribute to subsequent degeneration of the endplate
and postsynaptic membrane. {ECO:0000269|PubMed:11782989,
ECO:0000269|PubMed:8872460}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Myasthenic syndrome, congenital, 3B, fast-channel (CMS3B)
[MIM:616322]: A form of congenital myasthenic syndrome, a group of
disorders characterized by failure of neuromuscular transmission,
including pre-synaptic, synaptic, and post-synaptic disorders that
are not of autoimmune origin. Clinical features are easy
fatigability and muscle weakness affecting the axial and limb
muscles (with hypotonia in early-onset forms), the ocular muscles
(leading to ptosis and ophthalmoplegia), and the facial and bulbar
musculature (affecting sucking and swallowing, and leading to
dysphonia). The symptoms fluctuate and worsen with physical
effort. CMS3B is a fast-channel myasthenic syndrome. It is caused
by kinetic abnormalities of the AChR, resulting in brief opening
and activity of the channel, with a rapid decay in endplate
current, failure to achieve threshold depolarization of the
endplate and consequent failure to fire an action potential.
{ECO:0000269|PubMed:11435464, ECO:0000269|PubMed:12499478,
ECO:0000269|PubMed:18398509}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Myasthenic syndrome, congenital, 3C, associated with
acetylcholine receptor deficiency (CMS3C) [MIM:616323]: A form of
congenital myasthenic syndrome, a group of disorders characterized
by failure of neuromuscular transmission, including pre-synaptic,
synaptic, and post-synaptic disorders that are not of autoimmune
origin. Clinical features are easy fatigability and muscle
weakness affecting the axial and limb muscles (with hypotonia in
early-onset forms), the ocular muscles (leading to ptosis and
ophthalmoplegia), and the facial and bulbar musculature (affecting
sucking and swallowing, and leading to dysphonia). The symptoms
fluctuate and worsen with physical effort. CMS3C is an autosomal
recessive disorder of postsynaptic neuromuscular transmission, due
to deficiency of AChR at the endplate that results in low
amplitude of the miniature endplate potential and current.
{ECO:0000269|PubMed:16916845, ECO:0000269|PubMed:18398509}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Delta/CHRND
sub-subfamily. {ECO:0000305}.
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EMBL; X55019; CAA38759.1; -; mRNA.
EMBL; AK291526; BAF84215.1; -; mRNA.
EMBL; AK300109; BAG61904.1; -; mRNA.
EMBL; AK315297; BAG37703.1; -; mRNA.
EMBL; AC092165; AAY24102.1; -; Genomic_DNA.
EMBL; CH471063; EAW71003.1; -; Genomic_DNA.
EMBL; BC093923; AAH93923.1; -; mRNA.
EMBL; BC093925; AAH93925.1; -; mRNA.
CCDS; CCDS2494.1; -. [Q07001-1]
CCDS; CCDS58754.1; -. [Q07001-2]
PIR; A60916; A60916.
RefSeq; NP_000742.1; NM_000751.2. [Q07001-1]
RefSeq; NP_001243586.1; NM_001256657.1. [Q07001-2]
RefSeq; NP_001298124.1; NM_001311195.1.
RefSeq; NP_001298125.1; NM_001311196.1.
UniGene; Hs.156289; -.
ProteinModelPortal; Q07001; -.
BioGrid; 107566; 61.
IntAct; Q07001; 1.
STRING; 9606.ENSP00000258385; -.
BindingDB; Q07001; -.
ChEMBL; CHEMBL3011; -.
DrugBank; DB00674; Galantamine.
GuidetoPHARMACOLOGY; 476; -.
TCDB; 1.A.9.1.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
iPTMnet; Q07001; -.
PhosphoSitePlus; Q07001; -.
BioMuta; CHRND; -.
DMDM; 543759; -.
MaxQB; Q07001; -.
PaxDb; Q07001; -.
PeptideAtlas; Q07001; -.
PRIDE; Q07001; -.
Ensembl; ENST00000258385; ENSP00000258385; ENSG00000135902. [Q07001-1]
Ensembl; ENST00000543200; ENSP00000438380; ENSG00000135902. [Q07001-2]
GeneID; 1144; -.
KEGG; hsa:1144; -.
UCSC; uc002vsw.5; human. [Q07001-1]
CTD; 1144; -.
DisGeNET; 1144; -.
EuPathDB; HostDB:ENSG00000135902.9; -.
GeneCards; CHRND; -.
GeneReviews; CHRND; -.
HGNC; HGNC:1965; CHRND.
MalaCards; CHRND; -.
MIM; 100720; gene.
MIM; 253290; phenotype.
MIM; 616321; phenotype.
MIM; 616322; phenotype.
MIM; 616323; phenotype.
neXtProt; NX_Q07001; -.
OpenTargets; ENSG00000135902; -.
Orphanet; 33108; Lethal multiple pterygium syndrome.
Orphanet; 98913; Postsynaptic congenital myasthenic syndromes.
PharmGKB; PA26497; -.
eggNOG; KOG3645; Eukaryota.
eggNOG; ENOG410XQGR; LUCA.
GeneTree; ENSGT00760000118930; -.
HOGENOM; HOG000006757; -.
HOVERGEN; HBG003756; -.
InParanoid; Q07001; -.
KO; K04816; -.
OMA; VLISFMI; -.
OrthoDB; EOG091G0R20; -.
PhylomeDB; Q07001; -.
TreeFam; TF315605; -.
Reactome; R-HSA-629587; Highly sodium permeable acetylcholine nicotinic receptors.
GeneWiki; CHRND; -.
GenomeRNAi; 1144; -.
PRO; PR:Q07001; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000135902; -.
CleanEx; HS_CHRND; -.
ExpressionAtlas; Q07001; baseline and differential.
Genevisible; Q07001; HS.
GO; GO:0005892; C:acetylcholine-gated channel complex; IBA:GO_Central.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0045211; C:postsynaptic membrane; NAS:BHF-UCL.
GO; GO:0042166; F:acetylcholine binding; IEA:Ensembl.
GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; TAS:ProtInc.
GO; GO:0015276; F:ligand-gated ion channel activity; TAS:Reactome.
GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
GO; GO:0050881; P:musculoskeletal movement; IMP:BHF-UCL.
GO; GO:0050905; P:neuromuscular process; NAS:BHF-UCL.
GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
GO; GO:0035094; P:response to nicotine; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0003009; P:skeletal muscle contraction; IEA:Ensembl.
GO; GO:0048630; P:skeletal muscle tissue growth; IMP:BHF-UCL.
GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
GO; GO:0006810; P:transport; TAS:ProtInc.
Gene3D; 1.20.58.390; -; 1.
Gene3D; 2.70.170.10; -; 1.
InterPro; IPR006202; Neur_chan_lig-bd.
InterPro; IPR036734; Neur_chan_lig-bd_sf.
InterPro; IPR006201; Neur_channel.
InterPro; IPR036719; Neuro-gated_channel_TM_sf.
InterPro; IPR006029; Neurotrans-gated_channel_TM.
InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
PANTHER; PTHR18945; PTHR18945; 1.
Pfam; PF02931; Neur_chan_LBD; 1.
Pfam; PF02932; Neur_chan_memb; 1.
PRINTS; PR00254; NICOTINICR.
PRINTS; PR00252; NRIONCHANNEL.
SUPFAM; SSF63712; SSF63712; 1.
SUPFAM; SSF90112; SSF90112; 1.
TIGRFAMs; TIGR00860; LIC; 1.
PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Complete proteome;
Congenital myasthenic syndrome; Disease mutation; Disulfide bond;
Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
Membrane; Phosphoprotein; Polymorphism; Postsynaptic cell membrane;
Receptor; Reference proteome; Signal; Synapse; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 21 {ECO:0000250}.
CHAIN 22 517 Acetylcholine receptor subunit delta.
/FTId=PRO_0000000322.
TOPO_DOM 22 245 Extracellular. {ECO:0000255}.
TRANSMEM 246 270 Helical. {ECO:0000255}.
TRANSMEM 278 299 Helical. {ECO:0000255}.
TRANSMEM 312 333 Helical. {ECO:0000255}.
TOPO_DOM 334 471 Cytoplasmic. {ECO:0000255}.
TRANSMEM 472 490 Helical. {ECO:0000255}.
MOD_RES 390 390 Phosphotyrosine; by Tyr-kinases.
{ECO:0000250}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 151 165 {ECO:0000250}.
VAR_SEQ 67 81 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046423.
VARIANT 42 42 L -> P (in CMS3B; results in reduced
gating efficiency; slows opening of the
channel; decreases probability that the
channel will open in response to ACh).
{ECO:0000269|PubMed:18398509}.
/FTId=VAR_073691.
VARIANT 79 79 I -> K (in CMS3B; prevents expression of
the AChR on the cell surface; is a null
mutation; dbSNP:rs121909509).
{ECO:0000269|PubMed:18398509}.
/FTId=VAR_073692.
VARIANT 80 80 E -> K (in CMS3B; reduced adult and fetal
AChR expression and a reduced probability
of both adult and fetal AChR being in the
open state; dbSNP:rs121909504).
{ECO:0000269|PubMed:11435464}.
/FTId=VAR_021210.
VARIANT 95 95 F -> L (in LMPS; dbSNP:rs121909506).
{ECO:0000269|PubMed:18252226}.
/FTId=VAR_043905.
VARIANT 114 114 V -> L (polymorphism; has no appreciable
kinetic effects; allows for robust AChR
expression; dbSNP:rs760395222).
{ECO:0000269|PubMed:18398509}.
/FTId=VAR_073693.
VARIANT 271 271 P -> Q (in CMS3B; burst duration was
decreased and disassociation of ACh was
increased resulting in brief channel
opening episodes; shows abnormal
association with alpha CHRNA1 subunit
resulting in a decreased number of fully
assembled AChRs; dbSNP:rs121909503).
{ECO:0000269|PubMed:12499478}.
/FTId=VAR_021211.
VARIANT 288 288 Q -> E (in CMS3A; a benign mutation or a
rare polymorphism; dbSNP:rs41265127).
{ECO:0000269|PubMed:8872460}.
/FTId=VAR_021212.
VARIANT 289 289 S -> F (in CMS3A; delayed closure of AchR
ion channels, increasing the propensity
for open-channel block, as well as a
reduced rate of channel opening;
dbSNP:rs121909502).
{ECO:0000269|PubMed:11782989}.
/FTId=VAR_019566.
VARIANT 398 398 D -> E (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036031.
VARIANT 402 402 E -> K (in CMS3C; results in reduced
expression of the AChR at the cell
surface; impairs normal clustering of the
AChR channel with RAPSN;
dbSNP:rs145955590).
{ECO:0000269|PubMed:16916845}.
/FTId=VAR_073694.
MUTAGEN 290 290 V->A: Increased length of channel
opening. {ECO:0000269|PubMed:27375219}.
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


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