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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
 
 
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