ACHB2_MOUSE
ID ACHB2_MOUSE Reviewed; 501 AA.
AC Q9ERK7; Q8BGP7;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Neuronal acetylcholine receptor subunit beta-2;
DE Flags: Precursor;
GN Name=Chrnb2;
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].
RC STRAIN=Long sleep selected line;
RX PubMed=11434511; DOI=10.1097/00008571-200106000-00008;
RA Stitzel J.A., Dobelis P., Jimenez M., Collins A.C.;
RT "Long sleep and short sleep mice differ in nicotine-stimulated 86Rb+ efflux
RT and alpha4 nicotinic receptor subunit cDNA sequence.";
RL Pharmacogenetics 11:331-339(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Groot-Kormelink P.J.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal cord, and Spinal ganglion;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 permeable to sodiun ions. {ECO:0000250}.
CC -!- SUBUNIT: Neuronal AChR is composed of two different types of subunits:
CC alpha and beta. Beta-2 subunit can be combined to alpha-2, alpha-3 or
CC alpha-4 to give rise to functional receptors, complexes with beta-2 may
CC be heteropentamers. Alpha-2/4:beta-2 nAChR complexes are proposed to
CC exist in two subtypes: LS (low agonist sensitivity) with a (alpha-
CC 2/4)3:(beta-2)2 and HS (high agonist sensitivity) with a (alpha-
CC 2/4)2:(beta-2)3 stoichiometry; the subtypes differ in their subunit
CC binding interfaces which are involved in ligand binding. Interacts with
CC RIC3; which is required for proper folding and assembly. Interacts with
CC LYPD6. The heteropentamer alpha3-beta-2 interacts with alpha-
CC cconotoxins BuIA, MII, ImI, ImII, PnIA and GID (By similarity). The
CC heteropentamer alpha-4-beta-2 interacts with the alpha-conotoxins PnIA,
CC GID and MII (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P12390, ECO:0000250|UniProtKB:P17787}.
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-2/CHRNB2 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; AF299083; AAG23697.1; -; mRNA.
DR EMBL; AY574267; AAS90363.1; -; mRNA.
DR EMBL; AK049722; BAC33893.1; -; mRNA.
DR EMBL; AK051742; BAC34749.1; -; mRNA.
DR EMBL; AC102392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466547; EDL15184.1; -; Genomic_DNA.
DR EMBL; BC065103; AAH65103.1; -; mRNA.
DR CCDS; CCDS17515.1; -.
DR RefSeq; NP_033732.2; NM_009602.4.
DR AlphaFoldDB; Q9ERK7; -.
DR SMR; Q9ERK7; -.
DR ComplexPortal; CPX-167; Neuronal nicotinic acetylcholine receptor complex, 3xalpha4-2xbeta2.
DR ComplexPortal; CPX-169; Neuronal nicotinic acetylcholine receptor complex, 2xalpha4-3xbeta2.
DR ComplexPortal; CPX-174; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2.
DR ComplexPortal; CPX-188; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2.
DR ComplexPortal; CPX-189; Neuronal nicotinic acetylcholine receptor complex, alpha3-beta2.
DR ComplexPortal; CPX-202; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3.
DR ComplexPortal; CPX-216; Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2.
DR ComplexPortal; CPX-238; Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2.
DR DIP; DIP-48730N; -.
DR IntAct; Q9ERK7; 4.
DR STRING; 10090.ENSMUSP00000029562; -.
DR BindingDB; Q9ERK7; -.
DR ChEMBL; CHEMBL3301382; -.
DR ChEMBL; CHEMBL3883314; -.
DR ChEMBL; CHEMBL3885610; -.
DR ChEMBL; CHEMBL3885611; -.
DR GlyGen; Q9ERK7; 2 sites.
DR iPTMnet; Q9ERK7; -.
DR PhosphoSitePlus; Q9ERK7; -.
DR MaxQB; Q9ERK7; -.
DR PaxDb; Q9ERK7; -.
DR PRIDE; Q9ERK7; -.
DR ProteomicsDB; 285921; -.
DR Antibodypedia; 20401; 272 antibodies from 33 providers.
DR DNASU; 11444; -.
DR Ensembl; ENSMUST00000029562; ENSMUSP00000029562; ENSMUSG00000027950.
DR GeneID; 11444; -.
DR KEGG; mmu:11444; -.
DR UCSC; uc008qaa.2; mouse.
DR CTD; 1141; -.
DR MGI; MGI:87891; Chrnb2.
DR VEuPathDB; HostDB:ENSMUSG00000027950; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000158417; -.
DR HOGENOM; CLU_018074_1_0_1; -.
DR InParanoid; Q9ERK7; -.
DR OMA; TWIPEEF; -.
DR OrthoDB; 381858at2759; -.
DR PhylomeDB; Q9ERK7; -.
DR TreeFam; TF315605; -.
DR Reactome; R-MMU-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR Reactome; R-MMU-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR Reactome; R-MMU-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR BioGRID-ORCS; 11444; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q9ERK7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9ERK7; protein.
DR Bgee; ENSMUSG00000027950; Expressed in medial dorsal nucleus of thalamus and 190 other tissues.
DR ExpressionAtlas; Q9ERK7; baseline and differential.
DR Genevisible; Q9ERK7; 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:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0098691; C:dopaminergic synapse; IDA:SynGO.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
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:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0042166; F:acetylcholine binding; ISO:MGI.
DR GO; GO:0015464; F:acetylcholine receptor activity; ISO:MGI.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:MGI.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0050997; F:quaternary ammonium group binding; ISO:MGI.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IDA:MGI.
DR GO; GO:0001508; P:action potential; IMP:MGI.
DR GO; GO:0008306; P:associative learning; IGI:MGI.
DR GO; GO:0042113; P:B cell activation; IMP:MGI.
DR GO; GO:0042100; P:B cell proliferation; IGI:MGI.
DR GO; GO:0035095; P:behavioral response to nicotine; IMP:MGI.
DR GO; GO:0006816; P:calcium ion transport; IGI:MGI.
DR GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:MGI.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0001661; P:conditioned taste aversion; IMP:MGI.
DR GO; GO:0014046; P:dopamine secretion; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0021771; P:lateral geniculate nucleus development; IMP:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0051899; P:membrane depolarization; IDA:ComplexPortal.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:1904456; P:negative regulation of neuronal action potential; IMP:MGI.
DR GO; GO:0050877; P:nervous system process; ISO:MGI.
DR GO; GO:0019228; P:neuronal action potential; IMP:MGI.
DR GO; GO:0021631; P:optic nerve morphogenesis; IMP:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IGI:MGI.
DR GO; GO:0033603; P:positive regulation of dopamine secretion; IMP:MGI.
DR GO; GO:0032226; P:positive regulation of synaptic transmission, dopaminergic; IMP:MGI.
DR GO; GO:0045188; P:regulation of circadian sleep/wake cycle, non-REM sleep; IMP:MGI.
DR GO; GO:0042320; P:regulation of circadian sleep/wake cycle, REM sleep; IMP:MGI.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:MGI.
DR GO; GO:0042053; P:regulation of dopamine metabolic process; IMP:MGI.
DR GO; GO:0014059; P:regulation of dopamine secretion; IMP:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR GO; GO:0051963; P:regulation of synapse assembly; IMP:MGI.
DR GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; IMP:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:1905144; P:response to acetylcholine; ISO:MGI.
DR GO; GO:0042220; P:response to cocaine; IMP:MGI.
DR GO; GO:0045471; P:response to ethanol; IMP:MGI.
DR GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR GO; GO:0035094; P:response to nicotine; IMP:MGI.
DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0006939; P:smooth muscle contraction; IGI:MGI.
DR GO; GO:0035176; P:social behavior; IMP:MGI.
DR GO; GO:0060084; P:synaptic transmission involved in micturition; IGI:MGI.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; ISO:MGI.
DR GO; GO:0021562; P:vestibulocochlear nerve development; IMP:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR Gene3D; 1.20.58.390; -; 2.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR032932; CHRNB2.
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 PANTHER; PTHR18945:SF80; PTHR18945:SF80; 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; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..501
FT /note="Neuronal acetylcholine receptor subunit beta-2"
FT /id="PRO_0000000380"
FT TOPO_DOM 26..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 84
FT /note="Key residue that may interfere with effective access
FT of the conotoxin BuIA to the channel binding site"
FT /evidence="ECO:0000250|UniProtKB:P12390"
FT SITE 136
FT /note="Key residue for a rapid dissociation (K(off)) from
FT the conotoxin BuIA"
FT /evidence="ECO:0000250|UniProtKB:P12390"
FT SITE 144
FT /note="Key residue for a rapid dissociation (K(off)) from
FT the conotoxin BuIA"
FT /evidence="ECO:0000250|UniProtKB:P12390"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 155..169
FT /evidence="ECO:0000250"
FT CONFLICT 380
FT /note="E -> K (in Ref. 1; AAG23697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 57113 MW; 7FFAD47BD86B4493 CRC64;
MARCSNSMAL LFSFGLLWLC SGVLGTDTEE RLVEHLLDPS RYNKLIRPAT NGSELVTVQL
MVSLAQLISV HEREQIMTTN VWLTQEWEDY RLTWKPEDFD NMKKVRLPSK HIWLPDVVLY
NNADGMYEVS FYSNAVVSYD GSIFWLPPAI YKSACKIEVK HFPFDQQNCT MKFRSWTYDR
TEIDLVLKSD VASLDDFTPS GEWDIIALPG RRNENPDDST YVDITYDFII RRKPLFYTIN
LIIPCVLITS LAILVFYLPS DCGEKMTLCI SVLLALTVFL LLISKIVPPT SLDVPLVGKY
LMFTMVLVTF SIVTSVCVLN VHHRSPTTHT MAPWVKVVFL EKLPTLLFLQ QPRHRCARQR
LRLRRRQRER EGAGTLFFRE GPAADPCTCF VNPASMQGLA GAFQAEPAAA GLGRSMGPCS
CGLREAVDGV RFIADHMRSE DDDQSVREDW KYVAMVIDRL FLWIFVFVCV FGTIGMFLQP
LFQNYTATTF LHSDHSAPSS K
