ID ACHB4_MOUSE Reviewed; 495 AA.
AC Q8R493; Q8VI06;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=Neuronal acetylcholine receptor subunit beta-4;
DE Flags: Precursor;
GN Name=Chrnb4; Synonyms=Acrb4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/HeJ;
RA Lautner M.A., Remias J., Curtis C., Bhandarkar S., Stitzel J.A.;
RT "Cloning of a mouse nicotinic acetylcholine receptor beta 4 subunit cDNA.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Groot Kormelink P.J.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 120-395, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=12225896; DOI=10.1016/s0165-5728(02)00220-5;
RA Kuo Y.-P., Lucero L., Michaels J., DeLuca D., Lukas R.L.;
RT "Differential expression of nicotinic acetylcholine receptor subunits in
RT fetal and neonatal mouse thymus.";
RL J. Neuroimmunol. 130:140-154(2002).
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 {ECO:0000250}.
CC -!- SUBUNIT: Neuronal AChR is composed of two different types of subunits:
CC alpha and beta. Beta-4 subunit can be combined to alpha-2, alpha-3 or
CC alpha-4 to give rise to functional receptors. Interacts with RIC3;
CC which is required for proper folding and assembly. Interacts with
CC LYPD6. The pentamer alpha3-beta-4 interacts with the conotoxin BuIA.
CC The heteropentamer composed of alpha-3 and beta-4 subunits interacts
CC with the alpha-conotoxin ImI (By similarity).
CC {ECO:0000250|UniProtKB:P12392, ECO:0000250|UniProtKB:P30926}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed by immature T-cells in the
CC thymus. {ECO:0000269|PubMed:12225896}.
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; AF492840; AAM11659.1; -; mRNA.
DR EMBL; AY574269; AAS90365.1; -; mRNA.
DR EMBL; AF325351; AAL37367.1; -; mRNA.
DR CCDS; CCDS23200.1; -.
DR RefSeq; NP_683746.1; NM_148944.4.
DR AlphaFoldDB; Q8R493; -.
DR SMR; Q8R493; -.
DR ComplexPortal; CPX-182; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta4.
DR ComplexPortal; CPX-204; Neuronal nicotinic acetylcholine receptor complex, alpha3-beta4.
DR ComplexPortal; CPX-209; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4.
DR ComplexPortal; CPX-212; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta4.
DR ComplexPortal; CPX-220; Neuronal nicotinic acetylcholine receptor complex, alpha4-beta4.
DR IntAct; Q8R493; 2.
DR STRING; 10090.ENSMUSP00000034854; -.
DR BindingDB; Q8R493; -.
DR ChEMBL; CHEMBL3301382; -.
DR ChEMBL; CHEMBL3885609; -.
DR GlyConnect; 2548; 1 N-Linked glycan (1 site).
DR GlyCosmos; Q8R493; 4 sites, 1 glycan.
DR GlyGen; Q8R493; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8R493; -.
DR PhosphoSitePlus; Q8R493; -.
DR PaxDb; 10090-ENSMUSP00000034854; -.
DR Antibodypedia; 15128; 186 antibodies from 29 providers.
DR DNASU; 108015; -.
DR Ensembl; ENSMUST00000034854.8; ENSMUSP00000034854.7; ENSMUSG00000035200.8.
DR GeneID; 108015; -.
DR KEGG; mmu:108015; -.
DR UCSC; uc009prz.1; mouse.
DR AGR; MGI:87892; -.
DR CTD; 1143; -.
DR MGI; MGI:87892; Chrnb4.
DR VEuPathDB; HostDB:ENSMUSG00000035200; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000158708; -.
DR HOGENOM; CLU_018074_1_0_1; -.
DR InParanoid; Q8R493; -.
DR OMA; PRQKPCN; -.
DR OrthoDB; 5489962at2759; -.
DR PhylomeDB; Q8R493; -.
DR TreeFam; TF315605; -.
DR Reactome; R-MMU-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR Reactome; R-MMU-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR Reactome; R-MMU-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 108015; 3 hits in 80 CRISPR screens.
DR PRO; PR:Q8R493; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R493; Protein.
DR Bgee; ENSMUSG00000035200; Expressed in habenula and 59 other cell types or tissues.
DR ExpressionAtlas; Q8R493; baseline and differential.
DR Genevisible; Q8R493; MM.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; ISO:MGI.
DR GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0042166; F:acetylcholine binding; ISO:MGI.
DR GO; GO:0015464; F:acetylcholine receptor activity; ISO:MGI.
DR GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; ISO:MGI.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0035095; P:behavioral response to nicotine; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0019228; P:neuronal action potential; IGI:MGI.
DR GO; GO:0051971; P:positive regulation of transmission of nerve impulse; IMP:CACAO.
DR GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; IMP:MGI.
DR GO; GO:0035094; P:response to nicotine; IGI:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0006939; P:smooth muscle contraction; IGI:MGI.
DR GO; GO:0060084; P:synaptic transmission involved in micturition; IMP:MGI.
DR CDD; cd19064; LGIC_TM_nAChR; 1.
DR Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 2.
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 NCBIfam; TIGR00860; LIC; 1.
DR PANTHER; PTHR18945:SF385; NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT BETA-4; 1.
DR PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 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; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 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; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..495
FT /note="Neuronal acetylcholine receptor subunit beta-4"
FT /id="PRO_0000000390"
FT TOPO_DOM 21..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..297
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..495
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT SITE 81
FT /note="Key residue that facilitates effective access of the
FT conotoxin BuIA to the channel binding site"
FT /evidence="ECO:0000250|UniProtKB:P12392"
FT SITE 133
FT /note="Key residue for a low dissociation (K(off)) from the
FT conotoxin BuIA"
FT /evidence="ECO:0000250|UniProtKB:P12392"
FT SITE 141
FT /note="Key residue for a low dissociation (K(off)) from the
FT conotoxin BuIA"
FT /evidence="ECO:0000250|UniProtKB:P12392"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 152..166
FT /evidence="ECO:0000250"
SQ SEQUENCE 495 AA; 55809 MW; 025AF3585C17A6A8 CRC64;
MRGTPLLLVS LFALLQPGDC RLANAEEKLM DDLLNKTRYN NLIRPATSSS QLISIRLELS
LSQLISVNER EQIMTTSIWL KQEWTDYRLA WNSSCYEGVN ILRIPAKRVW LPDIVLYNNA
DGTYEVSVYT NVIVRSNGSI QWLPPAIYKS ACKIEVKHFP FDQQNCTLKF RSWTYDHTEI
DMVLKSPTAI MDDFTPSGEW DIVALPGRRT VNPQDPSYVD VTYDFIIKRK PLFYTINLII
PCVLITSLAI LVFYLPSDCG EKMTLCISVL LALTFFLLLI SKIVPPTSLD IPLIGKYLLF
TMVLVTFSIV TTVCVLNVHH RSPSTHTMAS WVKECFLHKL PTFLFMKRPG LEVSPARVPH
SSQLHLTTAE ATSTSALGPS SPSNLYGNSM YFVNPVPATP KSAVSSHTAG LPRDARLRSS
GRFRQDLQEA LEGVSFIAQH LESDDRDQSV IEDWKFVAMV VDRLFLWVFV IVCILGTMGL
FLPPLFQIHA PSKGL
//
