ACHB2_RAT
ID ACHB2_RAT Reviewed; 500 AA.
AC P12390; Q53YK1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Neuronal acetylcholine receptor subunit beta-2;
DE AltName: Full=Neuronal acetylcholine receptor non-alpha-1 chain;
DE Short=N-alpha 1;
DE Flags: Precursor;
GN Name=Chrnb2; Synonyms=Acrb2;
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].
RX PubMed=3272154; DOI=10.1016/0896-6273(88)90208-5;
RA Deneris E.S., Connolly J.G., Boulter J., Wada E., Wada K., Swanson L.W.,
RA Patrick J., Heinemann S.F.;
RT "Primary structure and expression of beta 2: a novel subunit of neuronal
RT nicotinic acetylcholine receptors.";
RL Neuron 1:45-54(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2444984; DOI=10.1073/pnas.84.21.7763;
RA Boulter J., Connolly J.G., Deneris E.S., Goldman D.J., Heinemann S.F.,
RA Patrick J.;
RT "Functional expression of two neuronal nicotinic acetylcholine receptors
RT from cDNA clones identifies a gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7763-7767(1987).
RN [3]
RP SEQUENCE REVISION.
RA Hartley M.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Groot-Kormelink P.J.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SYNTHESIS OF 5-16, 3D-STRUCTURE MODELING, AND SUBUNIT.
RX PubMed=15609996; DOI=10.1021/bi048918g;
RA Ellison M., Gao F., Wang H.L., Sine S.M., McIntosh J.M., Olivera B.M.;
RT "Alpha-conotoxins ImI and ImII target distinct regions of the human alpha7
RT nicotinic acetylcholine receptor and distinguish human nicotinic receptor
RT subtypes.";
RL Biochemistry 43:16019-16026(2004).
RN [6]
RP SUBUNIT, AND MUTAGENESIS OF LEU-118; VAL-135 AND PHE-143.
RX PubMed=15929983; DOI=10.1074/jbc.m504229200;
RA Dutertre S., Nicke A., Lewis R.J.;
RT "Beta2 subunit contribution to 4/7 alpha-conotoxin binding to the nicotinic
RT acetylcholine receptor.";
RL J. Biol. Chem. 280:30460-30468(2005).
RN [7]
RP SUBUNIT, MUTAGENESIS OF THR-83; VAL-135 AND PHE-143, AND SITES THR-83;
RP VAL-135 AND PHE-143.
RX PubMed=16964981; DOI=10.1021/bi0611715;
RA Shiembob D.L., Roberts R.L., Luetje C.W., McIntosh J.M.;
RT "Determinants of alpha-conotoxin BuIA selectivity on the nicotinic
RT acetylcholine receptor beta subunit.";
RL Biochemistry 45:11200-11207(2006).
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.
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-conotoxins
CC BuIA, MII, ImI, ImII, PnIA and GID (PubMed:15609996, PubMed:15929983,
CC PubMed:16964981). The heteropentamer alpha-4-beta-2 interacts with the
CC alpha-conotoxins PnIA, GID and MII (PubMed:15929983). {ECO:0000250,
CC ECO:0000250|UniProtKB:P17787, ECO:0000269|PubMed:15609996,
CC ECO:0000269|PubMed:15929983, ECO:0000269|PubMed:16964981}.
CC -!- INTERACTION:
CC P12390; P09483: Chrna4; NbExp=6; IntAct=EBI-9008812, EBI-7842410;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in most regions of the CNS.
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; L31622; AAC78724.1; -; mRNA.
DR EMBL; AY574258; AAS90354.1; -; mRNA.
DR PIR; JH0174; JH0174.
DR RefSeq; NP_062170.1; NM_019297.1.
DR AlphaFoldDB; P12390; -.
DR SMR; P12390; -.
DR ComplexPortal; CPX-170; Neuronal nicotinic acetylcholine receptor complex, 2xalpha4-3xbeta2.
DR ComplexPortal; CPX-171; Neuronal nicotinic acetylcholine receptor complex, 3xalpha4-2xbeta2.
DR ComplexPortal; CPX-178; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2.
DR ComplexPortal; CPX-190; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2.
DR ComplexPortal; CPX-191; Neuronal nicotinic acetylcholine receptor complex, alpha3-beta2.
DR ComplexPortal; CPX-203; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3.
DR ComplexPortal; CPX-215; Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2.
DR ComplexPortal; CPX-237; Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2.
DR CORUM; P12390; -.
DR IntAct; P12390; 6.
DR STRING; 10116.ENSRNOP00000028200; -.
DR BindingDB; P12390; -.
DR ChEMBL; CHEMBL1907587; -.
DR ChEMBL; CHEMBL1907592; -.
DR ChEMBL; CHEMBL1907596; -.
DR ChEMBL; CHEMBL3137275; -.
DR DrugCentral; P12390; -.
DR GlyGen; P12390; 2 sites.
DR SwissPalm; P12390; -.
DR PaxDb; P12390; -.
DR Ensembl; ENSRNOT00000028200; ENSRNOP00000028200; ENSRNOG00000020778.
DR GeneID; 54239; -.
DR KEGG; rno:54239; -.
DR UCSC; RGD:2350; rat.
DR CTD; 1141; -.
DR RGD; 2350; Chrnb2.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000158417; -.
DR HOGENOM; CLU_018074_1_3_1; -.
DR InParanoid; P12390; -.
DR OMA; TWIPEEF; -.
DR OrthoDB; 381858at2759; -.
DR PhylomeDB; P12390; -.
DR TreeFam; TF315605; -.
DR Reactome; R-RNO-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR Reactome; R-RNO-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR Reactome; R-RNO-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR PRO; PR:P12390; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000020778; Expressed in frontal cortex and 7 other tissues.
DR Genevisible; P12390; 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:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0098691; C:dopaminergic synapse; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0044853; C:plasma membrane raft; IGI:ARUK-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0042166; F:acetylcholine binding; IDA:RGD.
DR GO; GO:0015464; F:acetylcholine receptor activity; ISO:RGD.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:RGD.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0050997; F:quaternary ammonium group binding; IDA:RGD.
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; IGI:ARUK-UCL.
DR GO; GO:0001508; P:action potential; ISO:RGD.
DR GO; GO:0008306; P:associative learning; ISO:RGD.
DR GO; GO:0042113; P:B cell activation; ISO:RGD.
DR GO; GO:0035095; P:behavioral response to nicotine; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0021955; P:central nervous system neuron axonogenesis; ISO:RGD.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050890; P:cognition; ISO:RGD.
DR GO; GO:0001661; P:conditioned taste aversion; ISO:RGD.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0021771; P:lateral geniculate nucleus development; ISO:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0051899; P:membrane depolarization; IDA:ComplexPortal.
DR GO; GO:0007613; P:memory; ISO:RGD.
DR GO; GO:0045759; P:negative regulation of action potential; ISO:RGD.
DR GO; GO:0050877; P:nervous system process; ISO:RGD.
DR GO; GO:0021631; P:optic nerve morphogenesis; ISO:RGD.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:RGD.
DR GO; GO:0033603; P:positive regulation of dopamine secretion; ISO:RGD.
DR GO; GO:0032226; P:positive regulation of synaptic transmission, dopaminergic; ISO:RGD.
DR GO; GO:0045188; P:regulation of circadian sleep/wake cycle, non-REM sleep; ISO:RGD.
DR GO; GO:0042320; P:regulation of circadian sleep/wake cycle, REM sleep; ISO:RGD.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; ISO:RGD.
DR GO; GO:0042053; P:regulation of dopamine metabolic process; ISO:RGD.
DR GO; GO:0014059; P:regulation of dopamine secretion; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0051963; P:regulation of synapse assembly; ISO:RGD.
DR GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:1905144; P:response to acetylcholine; IDA:RGD.
DR GO; GO:0042220; P:response to cocaine; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0035094; P:response to nicotine; IMP:RGD.
DR GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0006939; P:smooth muscle contraction; ISO:RGD.
DR GO; GO:0035176; P:social behavior; ISO:RGD.
DR GO; GO:0060084; P:synaptic transmission involved in micturition; ISO:RGD.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:RGD.
DR GO; GO:0021562; P:vestibulocochlear nerve development; ISO:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
DR GO; GO:0007601; P:visual perception; ISO:RGD.
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 1: Evidence at protein 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..500
FT /note="Neuronal acetylcholine receptor subunit beta-2"
FT /id="PRO_0000000381"
FT TOPO_DOM 25..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 83
FT /note="Key residue that may interfere with effective access
FT of the conotoxin BuIA to the channel binding site"
FT /evidence="ECO:0000305|PubMed:16964981"
FT SITE 118
FT /note="Key residue that may play an important stabilizing
FT role for the interaction with alpha-conotoxins PnIA, GID
FT and MII, allowing them to bind deep into the nAChR cleft"
FT /evidence="ECO:0000305|PubMed:15929983"
FT SITE 135
FT /note="Key residue for a rapid dissociation (K(off)) from
FT the conotoxin BuIA"
FT /evidence="ECO:0000305|PubMed:16964981"
FT SITE 143
FT /note="Key residue for a rapid dissociation (K(off)) from
FT the conotoxin BuIA"
FT /evidence="ECO:0000305|PubMed:16964981"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 154..168
FT /evidence="ECO:0000250"
FT MUTAGEN 83
FT /note="T->D: 9-fold increase in affinity to the conotoxin
FT BuIA (15-fold decrease in K(off))."
FT /evidence="ECO:0000269|PubMed:16964981"
FT MUTAGEN 83
FT /note="T->G: 12-fold increase in affinity to the conotoxin
FT BuIA (11-fold decrease in K(off))."
FT /evidence="ECO:0000269|PubMed:16964981"
FT MUTAGEN 83
FT /note="T->K: 20-fold increase in affinity to the conotoxin
FT BuIA (37-fold decrease in K(off)); 2-fold decrease in
FT affinity to the conotoxin MII (no change in K(off), but 2-
FT fold decrease in K(on))."
FT /evidence="ECO:0000269|PubMed:16964981"
FT MUTAGEN 83
FT /note="T->S: 19-fold increase in affinity to the conotoxin
FT BuIA (7-fold decrease in K(off))."
FT /evidence="ECO:0000269|PubMed:16964981"
FT MUTAGEN 83
FT /note="T->V: 3-fold increase in affinity to the conotoxin
FT BuIA (2-fold decrease in K(off))."
FT /evidence="ECO:0000269|PubMed:16964981"
FT MUTAGEN 118
FT /note="L->Q: 40-fold, 165-fold, and 300-fold decrease in
FT inhibition of alpha-3-beta-2(L118Q) nAChR by alpha-
FT conotoxins PnIA, GID and MII, respectively."
FT /evidence="ECO:0000269|PubMed:15929983"
FT MUTAGEN 135
FT /note="V->A: Very small decrease or no change in inhibition
FT of alpha-3-beta-2(V135A) nAChR by alpha-conotoxins PnIA,
FT GID and MII."
FT /evidence="ECO:0000269|PubMed:15929983"
FT MUTAGEN 135
FT /note="V->G: No change in inhibition of alpha-3-beta-
FT 2(V135G) nAChR by alpha-conotoxins GID and MII. 4.4-fold
FT decrease in inhibition of alpha-3-beta-2(V135G) nAChR by
FT alpha-conotoxins PnIA."
FT /evidence="ECO:0000269|PubMed:15929983"
FT MUTAGEN 135
FT /note="V->I: 8.3-fold decrease in affinity to the conotoxin
FT BuIA (4-fold increase in K(off) and a 2-fold decrease in
FT K(on))."
FT /evidence="ECO:0000269|PubMed:16964981"
FT MUTAGEN 143
FT /note="F->A: No change in inhibition of alpha-3-beta-
FT 2(F143A) nAChR by alpha-conotoxins PnIA, GID and MII. 12-
FT fold and 6.6-fold increase in inhibition of alpha-4-beta-
FT 2(F143A) nAChR by alpha-conotoxins GID and MII,
FT respectively, but no change in inhibition of the same
FT receptor by alpha-conotoxin PnIA."
FT /evidence="ECO:0000269|PubMed:15929983"
FT MUTAGEN 143
FT /note="F->Q: 6.6-fold increase in affinity to the conotoxin
FT BuIA (7-fold decrease in K(off))."
FT /evidence="ECO:0000269|PubMed:16964981"
SQ SEQUENCE 500 AA; 56909 MW; 54C007A48225931C CRC64;
MAGHSNSMAL FSFSLLWLCS GVLGTDTEER LVEHLLDPSR YNKLIRPATN GSELVTVQLM
VSLAQLISVH EREQIMTTNV WLTQEWEDYR LTWKPEDFDN MKKVRLPSKH IWLPDVVLYN
NADGMYEVSF YSNAVVSYDG SIFWLPPAIY KSACKIEVKH FPFDQQNCTM KFRSWTYDRT
EIDLVLKSDV ASLDDFTPSG EWDIIALPGR RNENPDDSTY VDITYDFIIR RKPLFYTINL
IIPCVLITSL AILVFYLPSD CGEKMTLCIS VLLALTVFLL LISKIVPPTS LDVPLVGKYL
MFTMVLVTFS IVTSVCVLNV HHRSPTTHTM APWVKVVFLE KLPTLLFLQQ PRHRCARQRL
RLRRRQRERE GAGALFFREG PAADPCTCFV NPASVQGLAG AFRAEPTAAG PGRSVGPCSC
GLREAVDGVR FIADHMRSED DDQSVREDWK YVAMVIDRLF LWIFVFVCVF GTVGMFLQPL
FQNYTATTFL HPDHSAPSSK
