ACHB2_CARAU
ID ACHB2_CARAU Reviewed; 459 AA.
AC P19370;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Neuronal acetylcholine receptor subunit beta-2;
DE AltName: Full=GF-beta-2;
DE Flags: Fragment;
GN Name=chrnb2;
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=2402468; DOI=10.1093/nar/18.17.5307;
RA Hieber V.C., Bouchey J.E., Agranoff B.W., Goldman D.;
RT "Nucleotide and deduced amino acid sequence of the goldfish neural
RT nicotinic acetylcholine receptor beta-2 subunit.";
RL Nucleic Acids Res. 18:5307-5307(1990).
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: Neuronal AChR seems to be composed of two different type of
CC subunits: alpha and non-alpha (beta). The pentamer alpha3-beta-2
CC interacts with the conotoxin BuIA and the conotoxin MII (By
CC similarity). {ECO:0000250|UniProtKB:P12390}.
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; X54052; CAA37986.1; -; mRNA.
DR PIR; S14703; S14703.
DR AlphaFoldDB; P19370; -.
DR SMR; P19370; -.
DR Proteomes; UP000515129; Genome assembly.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; ISS:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042166; F:acetylcholine binding; ISS:UniProtKB.
DR GO; GO:0015464; F:acetylcholine receptor activity; ISS:UniProtKB.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; ISS:UniProtKB.
DR GO; GO:0035095; P:behavioral response to nicotine; ISS:UniProtKB.
DR GO; GO:0050890; P:cognition; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0050877; P:nervous system process; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR GO; GO:0008542; P:visual learning; ISS:UniProtKB.
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; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN <1..459
FT /note="Neuronal acetylcholine receptor subunit beta-2"
FT /id="PRO_0000076980"
FT TOPO_DOM <1..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 54
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 106
FT /note="Key residue for a rapid dissociation (K(off)) from
FT the conotoxin BuIA"
FT /evidence="ECO:0000250|UniProtKB:P12390"
FT SITE 114
FT /note="Key residue for a rapid dissociation (K(off)) from
FT the conotoxin BuIA"
FT /evidence="ECO:0000250|UniProtKB:P12390"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 125..139
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 459 AA; 53040 MW; 860B1A011AA47CF6 CRC64;
LRSDFLLGPE RYNKLIRPAV NKSQQVTIGI KVSLAQLISV NEREQIMTTN VWLTQEWTDY
RLVWDPNEYE GIKKLRIPSQ HIWLPDIVLY NNADGVYEVS FYCNAVVSNT GDIFWLPPAI
YKSACAIEVR NFPFDQQNCT LKFRSWTYDR TELDLVLTSD FASRDDYTPS GEWDIVSLPG
RKNEDPNDLT YLDITYDFVI KRKPLFYTIN LIIPCVLITS LAILVFYLPS DCGEKVTLCM
SVLLALTVFL LLISKIVPPT SLAVPLIGKY LMFTMVLVTF SIVTSVCVLN VHHRSPSTHY
MPEWVKCVFL HKLPAFLLMR RPGRSNVRER FRRKHQRKSF SSHQDGDSFF LTDDPGRVCG
AWRVGDLPEG SEFRQRVKVR HDQDVDEAID GVRFIAEHMK IEDDDEGIIE DWKYVAMVID
RLFLWIFILV CVVGTLGLFV QPLFQSYNTP VAEEVYGDF
