ACHB_MOUSE
ID ACHB_MOUSE Reviewed; 501 AA.
AC P09690; Q5F292;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Acetylcholine receptor subunit beta;
DE Flags: Precursor;
GN Name=Chrnb1; Synonyms=Acrb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3782129; DOI=10.1016/s0021-9258(18)66587-1;
RA Buonanno A., Mudd J., Shah V., Merlie J.P.;
RT "A universal oligonucleotide probe for acetylcholine receptor genes.
RT Selection and sequencing of cDNA clones for the mouse muscle beta
RT subunit.";
RL J. Biol. Chem. 261:16451-16458(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2708381; DOI=10.1016/s0021-9258(18)83278-1;
RA Buonanno A., Mudd J., Merlie J.P.;
RT "Isolation and characterization of the beta and epsilon subunit genes of
RT mouse muscle acetylcholine receptor.";
RL J. Biol. Chem. 264:7611-7616(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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}.
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DR EMBL; M14537; AAA37154.1; -; mRNA.
DR EMBL; J04699; AAA37156.1; -; Genomic_DNA.
DR EMBL; AK087554; BAC39924.1; -; mRNA.
DR EMBL; AL603707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24910.1; -.
DR PIR; A33358; A25338.
DR RefSeq; NP_033731.3; NM_009601.4.
DR AlphaFoldDB; P09690; -.
DR SMR; P09690; -.
DR BioGRID; 197935; 2.
DR ComplexPortal; CPX-252; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma.
DR ComplexPortal; CPX-257; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon.
DR IntAct; P09690; 4.
DR MINT; P09690; -.
DR STRING; 10090.ENSMUSP00000047270; -.
DR BindingDB; P09690; -.
DR ChEMBL; CHEMBL3038460; -.
DR ChEMBL; CHEMBL3137264; -.
DR GlyGen; P09690; 1 site.
DR iPTMnet; P09690; -.
DR PhosphoSitePlus; P09690; -.
DR SwissPalm; P09690; -.
DR PaxDb; P09690; -.
DR PRIDE; P09690; -.
DR ProteomicsDB; 286069; -.
DR Antibodypedia; 992; 267 antibodies from 35 providers.
DR DNASU; 11443; -.
DR Ensembl; ENSMUST00000045971; ENSMUSP00000047270; ENSMUSG00000041189.
DR GeneID; 11443; -.
DR KEGG; mmu:11443; -.
DR UCSC; uc007jrq.2; mouse.
DR CTD; 1140; -.
DR MGI; MGI:87890; Chrnb1.
DR VEuPathDB; HostDB:ENSMUSG00000041189; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000158661; -.
DR HOGENOM; CLU_018074_1_4_1; -.
DR InParanoid; P09690; -.
DR OMA; PCILITV; -.
DR OrthoDB; 776653at2759; -.
DR PhylomeDB; P09690; -.
DR TreeFam; TF315605; -.
DR BioGRID-ORCS; 11443; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Chrnb1; mouse.
DR PRO; PR:P09690; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P09690; protein.
DR Bgee; ENSMUSG00000041189; Expressed in hindlimb stylopod muscle and 144 other tissues.
DR Genevisible; P09690; MM.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:MGI.
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; IDA:SynGO.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0042166; F:acetylcholine binding; IMP:UniProtKB.
DR GO; GO:0015464; F:acetylcholine receptor activity; ISO:MGI.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IGI:MGI.
DR GO; GO:0015267; F:channel activity; ISO:MGI.
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; ISO:MGI.
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:MGI.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IDA:ComplexPortal.
DR GO; GO:0035095; P:behavioral response to nicotine; ISO:MGI.
DR GO; GO:0006812; P:cation transport; ISO:MGI.
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:MGI.
DR GO; GO:0006936; P:muscle contraction; ISO:MGI.
DR GO; GO:0050877; P:nervous system process; ISO:MGI.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; ISO:MGI.
DR GO; GO:0001941; P:postsynaptic membrane organization; ISO:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0003009; P:skeletal muscle contraction; ISO:MGI.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; ISO:MGI.
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 CHAIN 24..501
FT /note="Acetylcholine receptor subunit beta"
FT /id="PRO_0000000316"
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..382
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; 56931 MW; 787BDDA90EBB0EF2 CRC64;
MALGALLLLL GVLGTPLAPG ARGSEAEGQL IKKLFSNYDS SVRPAREVGD RVGVSIGLTL
AQLISLNEKD EEMSTKVYLD LEWTDYRLSW DPAEHDGIDS LRITAESVWL PDVVLLNNND
GNFDVALDIN VVVSFEGSVR WQPPGLYRSS CSIQVTYFPF DWQNCTMVFS SYSYDSSEVS
LKTGLDPEGE ERQEVYIHEG TFIENGQWEI IHKPSRLIQL PGDQRGGKEG HHEEVIFYLI
IRRKPLFYLV NVIAPCILIT LLAIFVFYLP PDAGEKMGLS IFALLTLTVF LLLLADKVPE
TSLAVPIIIK YLMFTMVLVT FSVILSVVVL NLHHRSPHTH QMPFWVRQIF IHKLPPYLGL
KRPKPERDQL PEPHHSLSPR SGWGRGTDEY FIRKPPSDFL FPKLNRFQPE SSAPDLRRFI
DGPTRAVGLP QELREVISSI SYMARQLQEQ EDHDALKEDW QFVAMVVDRL FLWTFIVFTS
VGTLVIFLDA TYHLPPPEPF P
