ACHD_TETCF
ID ACHD_TETCF Reviewed; 522 AA.
AC P02718;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Acetylcholine receptor subunit delta;
DE Flags: Precursor;
GN Name=chrnd;
OS Tetronarce californica (Pacific electric ray) (Torpedo californica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
OX NCBI_TaxID=7787;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6687403; DOI=10.1038/301251a0;
RA Noda M., Takahashi H., Tanabe T., Toyosato M., Kikyotani S., Hirose T.,
RA Asai M., Takashima H., Inayama S., Miyata T., Numa S.;
RT "Primary structures of beta- and delta-subunit precursors of Torpedo
RT californica acetylcholine receptor deduced from cDNA sequences.";
RL Nature 301:251-255(1983).
RN [2]
RP PROTEIN SEQUENCE OF 125-134 AND 139-145, GLYCOSYLATION AT ASN-164, AND
RP DISULFIDE BOND.
RX PubMed=2742850; DOI=10.1021/bi00434a048;
RA Kellaris K.V., Ware D.K., Smith S., Kyte J.;
RT "Assessment of the number of free cysteines and isolation and
RT identification of cystine-containing peptides from acetylcholine
RT receptor.";
RL Biochemistry 28:3469-3482(1989).
RN [3]
RP PHOSPHORYLATION AT TYR-393.
RX PubMed=1721053; DOI=10.1016/s0021-9258(18)54351-9;
RA Wagner K., Edson K., Heginbotham L., Post M., Huganir R.L., Czernik A.J.;
RT "Determination of the tyrosine phosphorylation sites of the nicotinic
RT acetylcholine receptor.";
RL J. Biol. Chem. 266:23784-23789(1991).
RN [4]
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 chains.
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. {ECO:0000305}.
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DR EMBL; J00965; AAA49275.1; -; mRNA.
DR PIR; A03177; ACRYD1.
DR PDB; 1EQ8; NMR; -; A/B/C/D/E=276-298.
DR PDB; 1OED; EM; 4.00 A; C=246-505.
DR PDB; 6UWZ; EM; 2.69 A; B=22-522.
DR PDB; 7QKO; EM; 2.90 A; C=22-522.
DR PDB; 7QL5; EM; 2.50 A; C=22-522.
DR PDB; 7QL6; EM; 3.23 A; C=22-522.
DR PDB; 7SMM; EM; 2.50 A; B=22-522.
DR PDB; 7SMQ; EM; 2.70 A; B=22-522.
DR PDB; 7SMR; EM; 2.77 A; B=22-522.
DR PDB; 7SMS; EM; 3.18 A; B=22-522.
DR PDB; 7SMT; EM; 2.56 A; B=22-522.
DR PDBsum; 1EQ8; -.
DR PDBsum; 1OED; -.
DR PDBsum; 6UWZ; -.
DR PDBsum; 7QKO; -.
DR PDBsum; 7QL5; -.
DR PDBsum; 7QL6; -.
DR PDBsum; 7SMM; -.
DR PDBsum; 7SMQ; -.
DR PDBsum; 7SMR; -.
DR PDBsum; 7SMS; -.
DR PDBsum; 7SMT; -.
DR AlphaFoldDB; P02718; -.
DR SMR; P02718; -.
DR ComplexPortal; CPX-2187; Acetylcholine receptor, alpha1-beta1-gamma-delta.
DR ELM; P02718; -.
DR IntAct; P02718; 3.
DR MINT; P02718; -.
DR BindingDB; P02718; -.
DR ChEMBL; CHEMBL3916; -.
DR DrugCentral; P02718; -.
DR TCDB; 1.A.9.1.9; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR GlyConnect; 7; 35 N-Linked glycans.
DR iPTMnet; P02718; -.
DR SwissPalm; P02718; -.
DR EvolutionaryTrace; P02718; -.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IPI:ComplexPortal.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IMP:ComplexPortal.
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; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor; Signal;
KW Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..21
FT CHAIN 22..522
FT /note="Acetylcholine receptor subunit delta"
FT /id="PRO_0000000326"
FT TOPO_DOM 22..245
FT /note="Extracellular"
FT TRANSMEM 246..270
FT /note="Helical"
FT TRANSMEM 278..295
FT /note="Helical"
FT TRANSMEM 312..333
FT /note="Helical"
FT TOPO_DOM 334..476
FT /note="Cytoplasmic"
FT TRANSMEM 477..497
FT /note="Helical"
FT MOD_RES 393
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000269|PubMed:1721053"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2742850"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 151..165
FT /evidence="ECO:0000269|PubMed:2742850"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 52..67
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 72..84
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 228..244
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 254..266
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 277..296
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 308..334
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 345..351
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 354..359
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 438..498
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:6UWZ"
SQ SEQUENCE 522 AA; 59891 MW; 568CF9C3D3E91E28 CRC64;
MGNIHFVYLL ISCLYYSGCS GVNEEERLIN DLLIVNKYNK HVRPVKHNNE VVNIALSLTL
SNLISLKETD ETLTSNVWMD HAWYDHRLTW NASEYSDISI LRLPPELVWI PDIVLQNNND
GQYHVAYFCN VLVRPNGYVT WLPPAIFRSS CPINVLYFPF DWQNCSLKFT ALNYDANEIT
MDLMTDTIDG KDYPIEWIII DPEAFTENGE WEIIHKPAKK NIYPDKFPNG TNYQDVTFYL
IIRRKPLFYV INFITPCVLI SFLASLAFYL PAESGEKMST AISVLLAQAV FLLLTSQRLP
ETALAVPLIG KYLMFIMSLV TGVIVNCGIV LNFHFRTPST HVLSTRVKQI FLEKLPRILH
MSRADESEQP DWQNDLKLRR SSSVGYISKA QEYFNIKSRS ELMFEKQSER HGLVPRVTPR
IGFGNNNENI AASDQLHDEI KSGIDSTNYI VKQIKEKNAY DEEVGNWNLV GQTIDRLSMF
IITPVMVLGT IFIFVMGNFN HPPAKPFEGD PFDYSSDHPR CA
