ACHB2_CHICK
ID ACHB2_CHICK Reviewed; 491 AA.
AC P09484;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 156.
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;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=White leghorn; TISSUE=Brain;
RX PubMed=3267226; DOI=10.1002/j.1460-2075.1988.tb02852.x;
RA Nef P., Oneyser C., Alliod C., Couturier S., Ballivet M.;
RT "Genes expressed in the brain define three distinct neuronal nicotinic
RT acetylcholine receptors.";
RL EMBO J. 7:595-601(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=3272170; DOI=10.1016/0896-6273(88)90145-6;
RA Schoepfer R., Whiting P., Esch F., Blacher R., Shimasaki S., Lindstrom J.;
RT "cDNA clones coding for the structural subunit of a chicken brain nicotinic
RT acetylcholine receptor.";
RL Neuron 1:241-248(1988).
RN [3]
RP MUTAGENESIS OF LYS-278, AND SUBUNIT.
RX PubMed=2005979; DOI=10.1038/350235a0;
RA Cooper E., Couturier S., Ballivet M.;
RT "Pentameric structure and subunit stoichiometry of a neuronal nicotinic
RT acetylcholine receptor.";
RL Nature 350:235-238(1991).
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 (also called beta). A functional receptor
CC seems to consist of two alpha-chains and three non-alpha chains. The
CC pentamer alpha3-beta-2 interacts with the conotoxin BuIA and the
CC conotoxin MII (By similarity). {ECO:0000250|UniProtKB:P12390,
CC ECO:0000269|PubMed:2005979}.
CC -!- INTERACTION:
CC P09484; P09482: CHRNA4; NbExp=7; IntAct=EBI-10686072, EBI-10686088;
CC P09484; P26152: CHRNA5; NbExp=8; IntAct=EBI-10686072, EBI-10686157;
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; X07353; CAA30286.1; -; Genomic_DNA.
DR EMBL; X07400; CAA30286.1; JOINED; Genomic_DNA.
DR EMBL; X07354; CAA30286.1; JOINED; Genomic_DNA.
DR EMBL; X07355; CAA30286.1; JOINED; Genomic_DNA.
DR EMBL; X07356; CAA30286.1; JOINED; Genomic_DNA.
DR EMBL; X07357; CAA30286.1; JOINED; Genomic_DNA.
DR EMBL; AJ250362; CAB59627.1; -; mRNA.
DR EMBL; X53092; CAA37258.1; -; mRNA.
DR PIR; S00380; ACCHNN.
DR RefSeq; NP_990144.1; NM_204813.1.
DR AlphaFoldDB; P09484; -.
DR SMR; P09484; -.
DR ComplexPortal; CPX-172; Neuronal nicotinic acetylcholine receptor complex, 3xalpha4-2xbeta2.
DR ComplexPortal; CPX-173; Neuronal nicotinic acetylcholine receptor complex, 2xalpha4-3xbeta2.
DR ComplexPortal; CPX-179; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2.
DR ComplexPortal; CPX-192; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2.
DR ComplexPortal; CPX-193; Neuronal nicotinic acetylcholine receptor complex, alpha3-beta2.
DR ComplexPortal; CPX-201; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3.
DR ComplexPortal; CPX-217; Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2.
DR ComplexPortal; CPX-239; Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2.
DR IntAct; P09484; 5.
DR STRING; 9031.ENSGALP00000004261; -.
DR PaxDb; P09484; -.
DR GeneID; 395605; -.
DR KEGG; gga:395605; -.
DR CTD; 1141; -.
DR VEuPathDB; HostDB:geneid_395605; -.
DR eggNOG; KOG3645; Eukaryota.
DR InParanoid; P09484; -.
DR OrthoDB; 381858at2759; -.
DR PhylomeDB; P09484; -.
DR PRO; PR:P09484; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IPI:ComplexPortal.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:AgBase.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0030425; C:dendrite; IDA:AgBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IDA:AgBase.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0042166; F:acetylcholine binding; IEA:Ensembl.
DR GO; GO:0015464; F:acetylcholine receptor activity; IEA:Ensembl.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IBA:GO_Central.
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:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0035095; P:behavioral response to nicotine; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051899; P:membrane depolarization; IDA:ComplexPortal.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
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..18
FT CHAIN 19..491
FT /note="Neuronal acetylcholine receptor subunit beta-2"
FT /id="PRO_0000000382"
FT TOPO_DOM 19..226
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 77
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 129
FT /note="Key residue for a rapid dissociation (K(off)) from
FT the conotoxin BuIA"
FT /evidence="ECO:0000250|UniProtKB:P12390"
FT SITE 137
FT /note="Key residue for a rapid dissociation (K(off)) from
FT the conotoxin BuIA"
FT /evidence="ECO:0000250|UniProtKB:P12390"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 148..162
FT /evidence="ECO:0000250"
FT MUTAGEN 278
FT /note="K->E: Increases channel conductance by almost 100%."
FT /evidence="ECO:0000269|PubMed:2005979"
SQ SEQUENCE 491 AA; 56032 MW; 984331E8A76D9750 CRC64;
MALLRVLCLL AALRRSLCTD TEERLVEYLL DPTRYNKLIR PATNGSQLVT VQLMVSLAQL
ISVHEREQIM TTNVWLTQEW EDYRLTWKPE DFDNMKKVRL PSKHIWLPDV VLYNNADGMY
EVSFYSNAVI SYDGSIFWLP PAIYKSACKI EVKHFPFDQQ NCTMKFRSWT YDRTEIDLVL
KSEVASLDDF TPSGEWDIVA LPGRRNENPD DSTYVDITYD FIIRRKPLFY TINLIIPCIL
ITSLAILVFY LPSDCGEKMT LCISVLLALT VFLLLISKIV PPTSLDVPLV GKYLMFTMVL
VTFSIVTSVC VLNVHHRSPT THTMPPWVRT LFLRKLPALL FMKQPQQNCA RQRLRQRRQT
QERAAAATLF LRAGARACAC YANPGAAKAE GLNGYRERQG QGPDPPAPCG CGLEEAVEGV
RFIADHMRSE DDDQSVSEDW KYVAMVIDRL FLWIFVFVCV FGTVGMFLQP LFQNYATNSL
LQLGQGTPTS K
