ACHB_TETCF
ID ACHB_TETCF Reviewed; 493 AA.
AC P02712;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Acetylcholine receptor subunit beta;
DE Flags: Precursor;
GN Name=CHRNB1;
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 25-78.
RX PubMed=7384786; DOI=10.1126/science.7384786;
RA Raftery M.A., Hunkapiller M.W., Strader C.D., Hood L.E.;
RT "Acetylcholine receptor: complex of homologous subunits.";
RL Science 208:1454-1457(1980).
RN [3]
RP PROTEIN SEQUENCE OF 126-147, GLYCOSYLATION AT ASN-165, AND 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 [4]
RP PHOSPHORYLATION AT TYR-379.
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).
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. Beta-1/CHRNB1 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; J00964; AAA49274.1; -; mRNA.
DR PIR; A93294; ACRYB1.
DR PDB; 1OED; EM; 4.00 A; B=241-490.
DR PDB; 6UWZ; EM; 2.69 A; C=25-493.
DR PDB; 7QKO; EM; 2.90 A; B=25-493.
DR PDB; 7QL5; EM; 2.50 A; B=25-493.
DR PDB; 7QL6; EM; 3.23 A; B=25-493.
DR PDB; 7SMM; EM; 2.50 A; C=25-493.
DR PDB; 7SMQ; EM; 2.70 A; C=25-493.
DR PDB; 7SMR; EM; 2.77 A; C=25-493.
DR PDB; 7SMS; EM; 3.18 A; C=25-493.
DR PDB; 7SMT; EM; 2.56 A; C=25-493.
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; P02712; -.
DR SMR; P02712; -.
DR ComplexPortal; CPX-2187; Acetylcholine receptor, alpha1-beta1-gamma-delta.
DR IntAct; P02712; 2.
DR BindingDB; P02712; -.
DR ChEMBL; CHEMBL2096975; -.
DR DrugCentral; P02712; -.
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; P02712; -.
DR SwissPalm; P02712; -.
DR EvolutionaryTrace; P02712; -.
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..24
FT /evidence="ECO:0000269|PubMed:7384786"
FT CHAIN 25..493
FT /note="Acetylcholine receptor subunit beta"
FT /id="PRO_0000000319"
FT TOPO_DOM 25..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 379
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000269|PubMed:1721053"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2742850"
FT DISULFID 152..166
FT /evidence="ECO:0000269|PubMed:2742850"
FT VARIANT 3
FT /note="N -> D (in a second clone)"
FT VARIANT 11
FT /note="L -> V (in a second clone)"
FT CONFLICT 75
FT /note="T -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 53..66
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 73..90
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 242..261
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 272..291
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 303..329
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 340..347
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 350..354
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 423..483
FT /evidence="ECO:0007829|PDB:6UWZ"
SQ SEQUENCE 493 AA; 56156 MW; 4E145192584D8F5F CRC64;
MENVRRMALG LVVMMALALS GVGASVMEDT LLSVLFETYN PKVRPAQTVG DKVTVRVGLT
LTNLLILNEK IEEMTTNVFL NLAWTDYRLQ WDPAAYEGIK DLRIPSSDVW QPDIVLMNNN
DGSFEITLHV NVLVQHTGAV SWQPSAIYRS SCTIKVMYFP FDWQNCTMVF KSYTYDTSEV
TLQHALDAKG EREVKEIVIN KDAFTENGQW SIEHKPSRKN WRSDDPSYED VTFYLIIQRK
PLFYIVYTII PCILISILAI LVFYLPPDAG EKMSLSISAL LAVTVFLLLL ADKVPETSLS
VPIIIRYLMF IMILVAFSVI LSVVVLNLHH RSPNTHTMPN WIRQIFIETL PPFLWIQRPV
TTPSPDSKPT IISRANDEYF IRKPAGDFVC PVDNARVAVQ PERLFSEMKW HLNGLTQPVT
LPQDLKEAVE AIKYIAEQLE SASEFDDLKK DWQYVAMVAD RLFLYVFFVI CSIGTFSIFL
DASHNVPPDN PFA
