Chrnb2
entrez
54239
canonical
uniprot
P12390
canonical
ensembl
ENSRNOG00000020778
resolver
ensembl
ENSRNOG00055021542
resolver
ensembl
ENSRNOG00060026560
resolver
ensembl
ENSRNOG00065027552
resolver
ensp
ENSRNOP00000028200
resolver
ensp
ENSRNOP00055029894
resolver
ensp
ENSRNOP00060038185
resolver
ensp
ENSRNOP00065038972
resolver
enst
ENSRNOT00055036806
resolver
enst
ENSRNOT00060045994
resolver
enst
ENSRNOT00065047496
resolver
genesymbol
Chrnb2
resolver
genesymbol_syn
Acrb2
resolver
uniprot
Q53YK1
resolver
uniprot_entry
ACHB2_RAT
resolver
uniprot_sec
Q53YK1
resolver
activity_regulation
ACTIVITY REGULATION: Activated by a myriad of ligands such as acetylcholine, cytisine, nicotine, choline and epibatidine (PubMed:10465681, PubMed:9882698). Channel potentiation by calcium is stoichiometry-selective, CHRNA4:CHRNB2 nACh receptor is achieved by calcium association with topographically distinct sites framed by anionic residues within the CHRNA4 subunit and between the CHRNA4 and CHRNB2 subunits. Oligomeric amyloid-beta protein 42 activates specifially CHRNA7:CHRNB2 nAchRs (By similarity). nAChR activity is inhibited by the antagonist alpha-conotoxins BuIA, PnIA, PnIC, GID and MII, small disulfide-constrained peptides from cone snails (PubMed:10465681, PubMed:15609996, PubMed:15929983, PubMed:16964981). {ECO:0000250|UniProtKB:P17787, ECO:0000269|PubMed:10465681, ECO:0000269|PubMed:15609996, ECO:0000269|PubMed:15929983, ECO:0000269|PubMed:16964981, ECO:0000269|PubMed:9882698}.
uniprot
proteins
amino_acid_sequence
MAGHSNSMALFSFSLLWLCSGVLGTDTEERLVEHLLDPSRYNKLIRPATNGSELVTVQLMVSLAQLISVHEREQIMTTNVWLTQEWEDYRLTWKPEDFDNMKKVRLPSKHIWLPDVVLYNNADGMYEVSFYSNAVVSYDGSIFWLPPAIYKSACKIEVKHFPFDQQNCTMKFRSWTYDRTEIDLVLKSDVASLDDFTPSGEWDIIALPGRRNENPDDSTYVDITYDFIIRRKPLFYTINLIIPCVLITSLAILVFYLPSDCGEKMTLCISVLLALTVFLLLISKIVPPTSLDVPLVGKYLMFTMVLVTFSIVTSVCVLNVHHRSPTTHTMAPWVKVVFLEKLPTLLFLQQPRHRCARQRLRLRRRQREREGAGALFFREGPAADPCTCFVNPASVQGLAGAFRAEPTAAGPGRSVGPCSCGLREAVDGVRFIADHMRSEDDDQSVREDWKYVAMVIDRLFLWIFVFVCVFGTVGMFLQPLFQNYTATTFLHPDHSAPSSK
uniprot
proteins
function
FUNCTION: Component of neuronal acetylcholine receptors (nAChRs) that function as pentameric, ligand-gated cation channels with high calcium permeability among other activities. nAChRs are excitatory neurotrasnmitter receptors formed by a collection of nAChR subunits known to mediate synaptic transmission in the nervous system and the neuromuscular junction. Each nAchR subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, cation permeability, and binding to allosteric modulators (PubMed:10465681). CHRNB2 forms heteropentameric neuronal acetylcholine receptors with CHRNA2, CHRNA3, CHRNA4 and CHRNA6, as well as CHRNA5 and CHRNB3 as accesory subunits (PubMed:10465681). Found in two major stoichiometric forms,(CHRNA4)3:(CHRNB2)2 and (CHRNA4)2:(CHRNB2)3, the two stoichiometric forms differ in their unitary conductance, calcium permeability, ACh sensitivity and potentiation by divalent cation (By similarity). Heteropentameric channels with CHRNA6 and CHRNA4 exhibit high sensitivity to ACh and nicotine and are predominantly expressed in only a few brain areas, including dopaminergic neurons, norepirephrine neurons and cells of the visual system. nAChrs containing CHRNA6 subunits mediate endogenous cholinergic modulation of dopamine and gamma-aminobutyric acid (GABA) release in response to nicotine at nerve terminals (PubMed:21325521). Also forms functional nAChRs with other subunits such as CHRNA7:CHRNB2, mainly expressed in basal forebrain cholinergic neurons (By similarity). {ECO:0000250|UniProtKB:P17787, ECO:0000269|PubMed:10465681, ECO:0000269|PubMed:21325521}.
uniprot
proteins
mass_dalton
56909
uniprot
proteins
mutagenesis
MUTAGEN 83; /note="T->D: 9-fold increase in affinity to the conotoxin BuIA (15-fold decrease in K(off))."; /evidence="ECO:0000269|PubMed:16964981"; MUTAGEN 83; /note="T->G: 12-fold increase in affinity to the conotoxin BuIA (11-fold decrease in K(off))."; /evidence="ECO:0000269|PubMed:16964981"; MUTAGEN 83; /note="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))."; /evidence="ECO:0000269|PubMed:16964981"; MUTAGEN 83; /note="T->S: 19-fold increase in affinity to the conotoxin BuIA (7-fold decrease in K(off))."; /evidence="ECO:0000269|PubMed:16964981"; MUTAGEN 83; /note="T->V: 3-fold increase in affinity to the conotoxin BuIA (2-fold decrease in K(off))."; /evidence="ECO:0000269|PubMed:16964981"; MUTAGEN 118; /note="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."; /evidence="ECO:0000269|PubMed:15929983"; MUTAGEN 135; /note="V->A: Very small decrease or no change in inhibition of alpha-3-beta-2(V135A) nAChR by alpha-conotoxins PnIA, GID and MII."; /evidence="ECO:0000269|PubMed:15929983"; MUTAGEN 135; /note="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."; /evidence="ECO:0000269|PubMed:15929983"; MUTAGEN 135; /note="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))."; /evidence="ECO:0000269|PubMed:16964981"; MUTAGEN 143; /note="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."; /evidence="ECO:0000269|PubMed:15929983"; MUTAGEN 143; /note="F->Q: 6.6-fold increase in affinity to the conotoxin BuIA (7-fold decrease in K(off))."; /evidence="ECO:0000269|PubMed:16964981
uniprot
proteins
protein_family
Acetylcholine receptor (TC 1.A.9.1) subfamily
uniprot
proteins
protein_family
Beta-2/CHRNB2 sub-subfamily
uniprot
proteins
protein_family
Ligand-gated ion channel (TC 1.A.9) family
uniprot
proteins
pubmed
10465681
uniprot
proteins
pubmed
15609996
uniprot
proteins
pubmed
15929983
uniprot
proteins
pubmed
16964981
uniprot
proteins
pubmed
21325521
uniprot
proteins
pubmed
2444984
uniprot
proteins
pubmed
3272154
uniprot
proteins
pubmed
9882698
uniprot
proteins
sequence_length
500
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Synaptic cell membrane {ECO:0000269|PubMed:21325521}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P17787}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 238..258; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 267..287; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 300..320; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 459..479; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins