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Neuronal acetylcholine receptor subunit beta-2 (Neuronal acetylcholine receptor non-alpha-1 chain) (N-alpha 1)

 ACHB2_RAT               Reviewed;         500 AA.
P12390; Q53YK1;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
27-SEP-2017, entry version 155.
RecName: Full=Neuronal acetylcholine receptor subunit beta-2;
AltName: Full=Neuronal acetylcholine receptor non-alpha-1 chain;
Short=N-alpha 1;
Flags: Precursor;
Name=Chrnb2; Synonyms=Acrb2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3272154; DOI=10.1016/0896-6273(88)90208-5;
Deneris E.S., Connolly J.G., Boulter J., Wada E., Wada K.,
Swanson L.W., Patrick J., Heinemann S.F.;
"Primary structure and expression of beta 2: a novel subunit of
neuronal nicotinic acetylcholine receptors.";
Neuron 1:45-54(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2444984; DOI=10.1073/pnas.84.21.7763;
Boulter J., Connolly J.G., Deneris E.S., Goldman D.J., Heinemann S.F.,
Patrick J.;
"Functional expression of two neuronal nicotinic acetylcholine
receptors from cDNA clones identifies a gene family.";
Proc. Natl. Acad. Sci. U.S.A. 84:7763-7767(1987).
[3]
SEQUENCE REVISION.
Hartley M.;
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
Groot-Kormelink P.J.;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, SYNTHESIS OF 5-16, 3D-STRUCTURE MODELING, AND SUBUNIT.
PubMed=15609996; DOI=10.1021/bi048918g;
Ellison M., Gao F., Wang H.L., Sine S.M., McIntosh J.M., Olivera B.M.;
"Alpha-conotoxins ImI and ImII target distinct regions of the human
alpha7 nicotinic acetylcholine receptor and distinguish human
nicotinic receptor subtypes.";
Biochemistry 43:16019-16026(2004).
[6]
SUBUNIT, AND MUTAGENESIS OF LEU-118; VAL-135 AND PHE-143.
PubMed=15929983; DOI=10.1074/jbc.M504229200;
Dutertre S., Nicke A., Lewis R.J.;
"Beta2 subunit contribution to 4/7 alpha-conotoxin binding to the
nicotinic acetylcholine receptor.";
J. Biol. Chem. 280:30460-30468(2005).
[7]
SUBUNIT, MUTAGENESIS OF THR-83; VAL-135 AND PHE-143, AND SITES THR-83;
VAL-135 AND PHE-143.
PubMed=16964981; DOI=10.1021/bi0611715;
Shiembob D.L., Roberts R.L., Luetje C.W., McIntosh J.M.;
"Determinants of alpha-conotoxin BuIA selectivity on the nicotinic
acetylcholine receptor beta subunit.";
Biochemistry 45:11200-11207(2006).
-!- FUNCTION: After binding acetylcholine, the AChR responds by an
extensive change in conformation that affects all subunits and
leads to opening of an ion-conducting channel across the plasma
membrane permeable to sodiun ions.
-!- SUBUNIT: Neuronal AChR is composed of two different types of
subunits: alpha and beta. Beta-2 subunit can be combined to alpha-
2, alpha-3 or alpha-4 to give rise to functional receptors,
complexes with beta-2 may be heteropentamers. Alpha-2/4:beta-2
nAChR complexes are proposed to exist in two subtypes: LS (low
agonist sensitivity) with a (alpha-2/4)3:(beta-2)2 and HS (high
agonist sensitivity) with a (alpha-2/4)2:(beta-2)3 stoichiometry;
the subtypes differ in their subunit binding interfaces which are
involved in ligand binding. Interacts with RIC3; which is required
for proper folding and assembly. Interacts with LYPD6. The
heteropentamer alpha3-beta-2 interacts with alpha-conotoxins BuIA,
MII, ImI, ImII, PnIA and GID (PubMed:15609996, PubMed:15929983,
PubMed:16964981). The heteropentamer alpha-4-beta-2 interacts with
the alpha-conotoxins PnIA, GID and MII (PubMed:15929983).
{ECO:0000250, ECO:0000250|UniProtKB:P17787,
ECO:0000269|PubMed:15609996, ECO:0000269|PubMed:15929983,
ECO:0000269|PubMed:16964981}.
-!- INTERACTION:
P09483:Chrna4; NbExp=6; IntAct=EBI-9008812, EBI-7842410;
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
membrane protein.
-!- TISSUE SPECIFICITY: Expressed in most regions of the CNS.
-!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Beta-
2/CHRNB2 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L31622; AAC78724.1; -; mRNA.
EMBL; AY574258; AAS90354.1; -; mRNA.
PIR; JH0174; JH0174.
RefSeq; NP_062170.1; NM_019297.1.
UniGene; Rn.53978; -.
PDB; 1OLE; Model; -; B/D/E=27-233.
PDB; 1OLF; Model; -; B/D/E=27-233.
PDBsum; 1OLE; -.
PDBsum; 1OLF; -.
ProteinModelPortal; P12390; -.
SMR; P12390; -.
CORUM; P12390; -.
IntAct; P12390; 4.
STRING; 10116.ENSRNOP00000028200; -.
BindingDB; P12390; -.
ChEMBL; CHEMBL3137275; -.
SwissPalm; P12390; -.
PaxDb; P12390; -.
PRIDE; P12390; -.
Ensembl; ENSRNOT00000028200; ENSRNOP00000028200; ENSRNOG00000020778.
GeneID; 54239; -.
KEGG; rno:54239; -.
UCSC; RGD:2350; rat.
CTD; 1141; -.
RGD; 2350; Chrnb2.
eggNOG; KOG3645; Eukaryota.
eggNOG; ENOG410XQGR; LUCA.
GeneTree; ENSGT00760000118930; -.
HOGENOM; HOG000006757; -.
HOVERGEN; HBG003756; -.
InParanoid; P12390; -.
KO; K04813; -.
OMA; TTHTMPP; -.
OrthoDB; EOG091G0R20; -.
PhylomeDB; P12390; -.
TreeFam; TF315605; -.
Reactome; R-RNO-629587; Highly sodium permeable acetylcholine nicotinic receptors.
Reactome; R-RNO-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
Reactome; R-RNO-629597; Highly calcium permeable nicotinic acetylcholine receptors.
PRO; PR:P12390; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000020778; -.
Genevisible; P12390; RN.
GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0044853; C:plasma membrane raft; IGI:ARUK-UCL.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042166; F:acetylcholine binding; IDA:RGD.
GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:RGD.
GO; GO:0008144; F:drug binding; IDA:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
GO; GO:0095500; P:acetylcholine receptor signaling pathway; IGI:ARUK-UCL.
GO; GO:0001508; P:action potential; IEA:Ensembl.
GO; GO:0042113; P:B cell activation; IEA:Ensembl.
GO; GO:0035095; P:behavioral response to nicotine; IEA:Ensembl.
GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IEA:Ensembl.
GO; GO:0001661; P:conditioned taste aversion; IEA:Ensembl.
GO; GO:0021771; P:lateral geniculate nucleus development; IEA:Ensembl.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0045759; P:negative regulation of action potential; IEA:Ensembl.
GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
GO; GO:0021631; P:optic nerve morphogenesis; IEA:Ensembl.
GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0033603; P:positive regulation of dopamine secretion; IDA:RGD.
GO; GO:0032226; P:positive regulation of synaptic transmission, dopaminergic; IEA:Ensembl.
GO; GO:0051291; P:protein heterooligomerization; IDA:RGD.
GO; GO:0045188; P:regulation of circadian sleep/wake cycle, non-REM sleep; IEA:Ensembl.
GO; GO:0042320; P:regulation of circadian sleep/wake cycle, REM sleep; IEA:Ensembl.
GO; GO:0048814; P:regulation of dendrite morphogenesis; IEA:Ensembl.
GO; GO:0042053; P:regulation of dopamine metabolic process; IEA:Ensembl.
GO; GO:0051963; P:regulation of synapse assembly; IEA:Ensembl.
GO; GO:1905144; P:response to acetylcholine; IGI:ARUK-UCL.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; IMP:RGD.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
GO; GO:0006939; P:smooth muscle contraction; IEA:Ensembl.
GO; GO:0035176; P:social behavior; IEA:Ensembl.
GO; GO:0060084; P:synaptic transmission involved in micturition; IEA:Ensembl.
GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:RGD.
GO; GO:0021562; P:vestibulocochlear nerve development; IEA:Ensembl.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
GO; GO:0007601; P:visual perception; IEA:Ensembl.
Gene3D; 2.70.170.10; -; 1.
InterPro; IPR032932; CHRNB2.
InterPro; IPR006202; Neur_chan_lig-bd.
InterPro; IPR006201; Neur_channel.
InterPro; IPR006029; Neurotrans-gated_channel_TM.
InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
PANTHER; PTHR18945; PTHR18945; 1.
PANTHER; PTHR18945:SF730; PTHR18945:SF730; 1.
Pfam; PF02931; Neur_chan_LBD; 1.
Pfam; PF02932; Neur_chan_memb; 1.
PRINTS; PR00254; NICOTINICR.
PRINTS; PR00252; NRIONCHANNEL.
SUPFAM; SSF63712; SSF63712; 1.
SUPFAM; SSF90112; SSF90112; 1.
TIGRFAMs; TIGR00860; LIC; 1.
PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Ion channel; Ion transport;
Ligand-gated ion channel; Membrane; Postsynaptic cell membrane;
Receptor; Reference proteome; Signal; Synapse; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 500 Neuronal acetylcholine receptor subunit
beta-2.
/FTId=PRO_0000000381.
TOPO_DOM 25 237 Extracellular. {ECO:0000255}.
TRANSMEM 238 258 Helical. {ECO:0000255}.
TOPO_DOM 259 266 Cytoplasmic. {ECO:0000255}.
TRANSMEM 267 287 Helical. {ECO:0000255}.
TOPO_DOM 288 299 Extracellular. {ECO:0000255}.
TRANSMEM 300 320 Helical. {ECO:0000255}.
TOPO_DOM 321 458 Cytoplasmic. {ECO:0000255}.
TRANSMEM 459 479 Helical. {ECO:0000255}.
SITE 83 83 Key residue that may interfere with
effective access of the conotoxin BuIA to
the channel binding site.
{ECO:0000305|PubMed:16964981}.
SITE 118 118 Key residue that may play an important
stabilizing role for the interaction with
alpha-conotoxins PnIA, GID and MII,
allowing them to bind deep into the nAChR
cleft. {ECO:0000305|PubMed:15929983}.
SITE 135 135 Key residue for a rapid dissociation
(K(off)) from the conotoxin BuIA.
{ECO:0000305|PubMed:16964981}.
SITE 143 143 Key residue for a rapid dissociation
(K(off)) from the conotoxin BuIA.
{ECO:0000305|PubMed:16964981}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 167 167 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 154 168 {ECO:0000250}.
MUTAGEN 83 83 T->D: 9-fold increase in affinity to the
conotoxin BuIA (15-fold decrease in
K(off)). {ECO:0000269|PubMed:16964981}.
MUTAGEN 83 83 T->G: 12-fold increase in affinity to the
conotoxin BuIA (11-fold decrease in
K(off)). {ECO:0000269|PubMed:16964981}.
MUTAGEN 83 83 T->K: 20-fold increase in affinity to the
conotoxin BuIA (37-fold decrease in
K(off)); 2-fold decrease in affinity to
the conotoxin MII (no change in K(off),
but 2-fold decrease in K(on)).
{ECO:0000269|PubMed:16964981}.
MUTAGEN 83 83 T->S: 19-fold increase in affinity to the
conotoxin BuIA (7-fold decrease in
K(off)). {ECO:0000269|PubMed:16964981}.
MUTAGEN 83 83 T->V: 3-fold increase in affinity to the
conotoxin BuIA (2-fold decrease in
K(off)). {ECO:0000269|PubMed:16964981}.
MUTAGEN 118 118 L->Q: 40-fold, 165-fold, and 300-fold
decrease in inhibition of alpha-3-beta-
2(L118Q) nAChR by alpha-conotoxins PnIA,
GID and MII, respectively.
{ECO:0000269|PubMed:15929983}.
MUTAGEN 135 135 V->A: Very small decrease or no change in
inhibition of alpha-3-beta-2(V135A) nAChR
by alpha-conotoxins PnIA, GID and MII.
{ECO:0000269|PubMed:15929983}.
MUTAGEN 135 135 V->G: No change in inhibition of alpha-3-
beta-2(V135G) nAChR by alpha-conotoxins
GID and MII. 4.4-fold decrease in
inhibition of alpha-3-beta-2(V135G) nAChR
by alpha-conotoxins PnIA.
{ECO:0000269|PubMed:15929983}.
MUTAGEN 135 135 V->I: 8.3-fold decrease in affinity to
the conotoxin BuIA (4-fold increase in
K(off) and a 2-fold decrease in K(on)).
{ECO:0000269|PubMed:16964981}.
MUTAGEN 143 143 F->A: No change in inhibition of alpha-3-
beta-2(F143A) nAChR by alpha-conotoxins
PnIA, GID and MII. 12-fold and 6.6-fold
increase in inhibition of alpha-4-beta-
2(F143A) nAChR by alpha-conotoxins GID
and MII, respectively, but no change in
inhibition of the same receptor by alpha-
conotoxin PnIA.
{ECO:0000269|PubMed:15929983}.
MUTAGEN 143 143 F->Q: 6.6-fold increase in affinity to
the conotoxin BuIA (7-fold decrease in
K(off)). {ECO:0000269|PubMed:16964981}.
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


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