ACHB_RAT
ID ACHB_RAT Reviewed; 501 AA.
AC P25109;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Acetylcholine receptor subunit beta;
DE Flags: Precursor;
GN Name=Chrnb1; Synonyms=Acrb;
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 [MRNA].
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).
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.
CC {ECO:0000250|UniProtKB:P11230}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X74833; CAA52827.1; -; mRNA.
DR PIR; S13873; S13873.
DR RefSeq; NP_036660.1; NM_012528.1.
DR AlphaFoldDB; P25109; -.
DR SMR; P25109; -.
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.ENSRNOP00000019947; -.
DR BindingDB; P25109; -.
DR ChEMBL; CHEMBL3885509; -.
DR ChEMBL; CHEMBL4523658; -.
DR DrugCentral; P25109; -.
DR GlyGen; P25109; 1 site.
DR PaxDb; P25109; -.
DR PRIDE; P25109; -.
DR Ensembl; ENSRNOT00000110050; ENSRNOP00000089285; ENSRNOG00000014698.
DR GeneID; 24261; -.
DR KEGG; rno:24261; -.
DR UCSC; RGD:2349; rat.
DR CTD; 1140; -.
DR RGD; 2349; Chrnb1.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000158661; -.
DR HOGENOM; CLU_018074_1_4_1; -.
DR InParanoid; P25109; -.
DR OMA; PCILITV; -.
DR OrthoDB; 776653at2759; -.
DR PhylomeDB; P25109; -.
DR TreeFam; TF315605; -.
DR PRO; PR:P25109; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000014698; Expressed in skeletal muscle tissue and 16 other tissues.
DR Genevisible; P25109; 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: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:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0042166; F:acetylcholine binding; ISO:RGD.
DR GO; GO:0015464; F:acetylcholine receptor activity; IEA:Ensembl.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:RGD.
DR GO; GO:0015267; F:channel activity; ISO: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: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:0035095; P:behavioral response to nicotine; 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:0055001; P:muscle cell development; ISO:RGD.
DR GO; GO:0006936; P:muscle contraction; ISO:RGD.
DR GO; GO:0050877; P:nervous system process; ISO:RGD.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; ISO:RGD.
DR GO; GO:0001941; P:postsynaptic membrane organization; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0003009; P:skeletal muscle contraction; IDA:RGD.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; 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 2: Evidence at transcript level;
KW Cell membrane; 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..23
FT /evidence="ECO:0000250"
FT CHAIN 24..501
FT /note="Acetylcholine receptor subunit beta"
FT /id="PRO_0000000317"
FT TOPO_DOM 24..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 362..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 390
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 151..165
FT /evidence="ECO:0000250"
SQ SEQUENCE 501 AA; 57027 MW; 2E7DD6AAD1D9364D CRC64;
MALGALLLIL GILGTPLAPG ARGSEAEGQL LKKLFSDYDS SVRPAQEVGD RVGVSIGLTL
AQLISLNEKD EEMSTKVYLD LEWTDYRLSW DPAEHDGIES LRVTAESVWL PDVVLLNNND
GNFDVALDIN VVVSFEGSVR WQPPGLYRSS CSIQVTYFPF DWQNCTMVFS SYSYDSSEVS
LKTGPDPDGQ ERQEIYIHEG TFIENGQWEI IHKPSRLIHL PGDRRGGKEG HREEVIFYLI
IRRKPLFYLV NVIAPCILIT LLAIFVFYLP PDAGEKMGLS IFALLTLTVF LLLLADKVPE
TSLAVPIIIK YLMFTMILVT FSVILSVVVL NLHHRSPHTH QMPFWVRQIF IHKLPPYLGL
KRPKPERDQL PEPHHSFSPR SGWGRGTDEY FIRKPPCDFL FPKLNRFQPE SPAPDLRRFI
DGPPRAVGLP QELREVISSI SYMARQLQEQ EDHDALKEDW QFVAMVVDRL FLWTFIVFTS
VGTLVIFLDA TYHLPPPEPF P
