ACHD_RAT
ID ACHD_RAT Reviewed; 517 AA.
AC P25110;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Acetylcholine receptor subunit delta;
DE Flags: Precursor;
GN Name=Chrnd; Synonyms=Acrd;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Muscle;
RX PubMed=1702709; DOI=10.1111/j.1432-1033.1990.tb15637.x;
RA Witzemann V., Stein E., Barg B., Konno T., Koenen M., Kues W., Criado M.,
RA Hofmann M., Sakmann B.;
RT "Primary structure and functional expression of the alpha-, beta-, gamma-,
RT delta- and epsilon-subunits of the acetylcholine receptor from rat
RT muscle.";
RL Eur. J. Biochem. 194:437-448(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 1-17.
RX PubMed=1638981; DOI=10.1242/dev.115.1.213;
RA Chahine K.G., Walke W., Goldman D.J.;
RT "A 102 base pair sequence of the nicotinic acetylcholine receptor delta-
RT subunit gene confers regulation by muscle electrical activity.";
RL Development 115:213-219(1992).
RN [3]
RP STRUCTURE BY NMR OF 276-298.
RX PubMed=10201407; DOI=10.1038/7610;
RA Opella S.J., Marassi F.M., Gesell J.J., Valente A.P., Kim Y.,
RA Oblatt-Montal M., Montal M.;
RT "Structures of the M2 channel-lining segments from nicotinic acetylcholine
RT and NMDA receptors by NMR spectroscopy.";
RL Nat. Struct. Biol. 6:374-379(1999).
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: 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q07001}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
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; X74835; CAA52829.1; -; mRNA.
DR EMBL; X66531; CAA47142.1; -; Genomic_DNA.
DR PIR; S13875; S13875.
DR RefSeq; NP_062171.1; NM_019298.1.
DR PDB; 1A11; NMR; -; A=276-298.
DR PDB; 1CEK; NMR; -; A=276-298.
DR PDBsum; 1A11; -.
DR PDBsum; 1CEK; -.
DR AlphaFoldDB; P25110; -.
DR SMR; P25110; -.
DR ComplexPortal; CPX-253; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma.
DR ComplexPortal; CPX-258; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon.
DR STRING; 10116.ENSRNOP00000026504; -.
DR BindingDB; P25110; -.
DR ChEMBL; CHEMBL3885509; -.
DR ChEMBL; CHEMBL4523658; -.
DR GlyGen; P25110; 3 sites.
DR iPTMnet; P25110; -.
DR PhosphoSitePlus; P25110; -.
DR PaxDb; P25110; -.
DR Ensembl; ENSRNOT00000026504; ENSRNOP00000026504; ENSRNOG00000019527.
DR GeneID; 54240; -.
DR KEGG; rno:54240; -.
DR UCSC; RGD:2352; rat.
DR CTD; 1144; -.
DR RGD; 2352; Chrnd.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000159794; -.
DR HOGENOM; CLU_018074_1_4_1; -.
DR InParanoid; P25110; -.
DR OMA; NFIVSHM; -.
DR OrthoDB; 588360at2759; -.
DR PhylomeDB; P25110; -.
DR Reactome; R-RNO-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR EvolutionaryTrace; P25110; -.
DR PRO; PR:P25110; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000019527; Expressed in skeletal muscle tissue and 4 other tissues.
DR Genevisible; P25110; RN.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISO:RGD.
DR GO; GO:0006812; P:cation transport; IDA:RGD.
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:0050881; P:musculoskeletal movement; ISO:RGD.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0003009; P:skeletal muscle contraction; IDA:RGD.
DR GO; GO:0048630; P:skeletal muscle tissue growth; ISO:RGD.
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; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; 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_0000000324"
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..296
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 CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 151..165
FT /evidence="ECO:0000250"
FT HELIX 275..297
FT /evidence="ECO:0007829|PDB:1A11"
SQ SEQUENCE 517 AA; 58884 MW; 2E561B527788AE9B CRC64;
MAGPVPTLGL LAALVVCGSW GLNEEQRLIQ HLFEEKGYNK ELRPVARKED IVDVALSLTL
SNLISLKEVE ETLTTNVWID HAWIDSRLQW NANEFGNITV LRLPSDMVWL PEIVLENNND
GSFQISYACN VLVSDSGHVT WLPPAIFRSS CPISVTYFPF DWQNCSLKFS SLKYTAKEIR
LSLKQEEEDN RSYPIEWIII DPEGFTENGE WEIVHRAAKV NVDPSVPMDS TNHQDVTFYL
IIRRKPLFYI INILVPCVLI SFMINLVFYL PGDCGEKTSV AISVLLAQSV FLLLISKRLP
ATSMAIPLVG KFLLFGMVLV TMVVVICVIV LNIHFRTPST HVLSEGVKKF FLETLPKLLH
MSRPEEEDPG PRALIRRTSS LGYISKAEEY FSLKSRSDLM FEKQSERHGL ARRLTTARKP
PASSEQVQQE LFNEMKPAVD GANFIVNHMR DQNSYNEEKD NWNQVARTVD RLCLFVVTPV
MVVGTAWIFL QGVYNQPPPQ PFPGDPFSYD EQDRRFI
