ACHB4_CHICK
ID ACHB4_CHICK Reviewed; 470 AA.
AC P26153;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Neuronal acetylcholine receptor subunit beta-4;
DE AltName: Full=Neuronal acetylcholine receptor non-alpha-3 chain;
DE Short=N-alpha 3;
DE Flags: Precursor; Fragment;
GN Name=CHRNB4;
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 [MRNA].
RC STRAIN=White leghorn; TISSUE=Brain;
RX PubMed=1698777; DOI=10.1016/s0021-9258(18)38201-2;
RA Couturier S., Erkman L., Valera S., Rungger D., Bertrand S., Boulter J.,
RA Ballivet M., Bertrand D.;
RT "Alpha 5, alpha 3, and non-alpha 3. Three clustered avian genes encoding
RT neuronal nicotinic acetylcholine receptor-related subunits.";
RL J. Biol. Chem. 265:17560-17567(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 (also called beta). A functional receptor
CC seems to consist of two alpha-chains and three non-alpha chains. The
CC pentamer alpha3-beta-4 interacts with the conotoxin BuIA.
CC {ECO:0000250|UniProtKB:P12392}.
CC -!- INTERACTION:
CC P26153; P09481: CHRNA3; NbExp=3; IntAct=EBI-10686176, EBI-10686191;
CC P26153; P26152: CHRNA5; NbExp=4; IntAct=EBI-10686176, EBI-10686157;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: High levels in the developing ciliary and superior
CC cervical ganglia.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. Beta-4/CHRNB4 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; J05643; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A39218; A39218.
DR AlphaFoldDB; P26153; -.
DR SMR; P26153; -.
DR ComplexPortal; CPX-184; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta4.
DR ComplexPortal; CPX-206; Neuronal nicotinic acetylcholine receptor complex, alpha3-beta4.
DR ComplexPortal; CPX-207; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4.
DR ComplexPortal; CPX-214; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta4.
DR ComplexPortal; CPX-221; Neuronal nicotinic acetylcholine receptor complex, alpha4-beta4.
DR IntAct; P26153; 3.
DR STRING; 9031.ENSGALP00000039014; -.
DR PaxDb; P26153; -.
DR VEuPathDB; HostDB:geneid_395613; -.
DR eggNOG; KOG3645; Eukaryota.
DR InParanoid; P26153; -.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
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:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
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; IC:ComplexPortal.
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:0007165; P:signal transduction; IBA:GO_Central.
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 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..3
FT /evidence="ECO:0000255"
FT CHAIN 4..470
FT /note="Neuronal acetylcholine receptor subunit beta-4"
FT /id="PRO_0000000392"
FT TOPO_DOM 4..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..278
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..438
FT /note="Cytoplasmic"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..470
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT SITE 114
FT /note="Key residue for a low dissociation (K(off)) from the
FT conotoxin BuIA"
FT /evidence="ECO:0000250|UniProtKB:P12392"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 133..147
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 470 AA; 53785 MW; 3117314772886B2D CRC64;
STAADAEEKL MNHLLSPDRY NKLIRPAVNS SQLVSIELQV SLAQLISVNE REQIMTTNVW
LNQEWIDYRL AWKPSDYEGI NMLRIPAKHI WLPDIVLYNN ADGTYEVSLY TNAIVQNNGS
IRWLPPAIYK SACKIEVKHF PFDQQNCTLK FRSWTYDHTE IDMVLKTSMA SMDDFTPSGE
WDIVALPGRR TENPLDPNYV DVTYDFIIKR KPLFYTINLI IPCVLITSLA ILVFYLPSDC
GEKMTLCISV LLALTVFLLL ISKIVPPTSL DVPLIGKYLM FTMVLVTFSI VTSVCVLNVH
HRSPSTHTMP PWVKLVFLER LPAYLFMKRP ENNSPRQKPA NCKKTRAENL CMDPADFYKN
STYFVNTASA KKYDMKITDT LDNVSSHQDF RLRTGTKFSP EVQEAIDGVS FIAEHMKSDD
NDQSVIEDWK YVAMVVDRLF LWIFVLVCVL GTVGLFLQPL FQNHIAATNP
