ACHB4_RAT
ID ACHB4_RAT Reviewed; 495 AA.
AC P12392; Q63361;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Neuronal acetylcholine receptor subunit beta-4;
DE AltName: Full=Neuronal acetylcholine receptor non-alpha-2 chain;
DE Short=N-alpha 2;
DE Flags: Precursor;
GN Name=Chrnb4; Synonyms=Acrb4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX PubMed=2642007; DOI=10.1016/0896-6273(89)90207-9;
RA Duvoisin R.M., Deneris E.S., Patrick J., Heinemann S.F.;
RT "The functional diversity of the neuronal nicotinic acetylcholine receptors
RT is increased by a novel subunit: beta 4.";
RL Neuron 3:487-496(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT).
RX PubMed=1689727; DOI=10.1016/s0021-9258(19)39588-2;
RA Boulter J., O'Shea-Greenfield A., Duvoisin R.M., Connolly J.G., Wada E.,
RA Jensen A., Gardner P.D., Ballivet M., Deneris E.S., McKinnon D.,
RA Heinemann S.F., Patrick J.;
RT "Alpha 3, alpha 5, and beta 4: three members of the rat neuronal nicotinic
RT acetylcholine receptor-related gene family form a gene cluster.";
RL J. Biol. Chem. 265:4472-4482(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=Superior cervical ganglion;
RX PubMed=2918319; DOI=10.1111/j.1471-4159.1989.tb02553.x;
RA Isenberg K.E., Meyer G.E.;
RT "Cloning of a putative neuronal nicotinic acetylcholine receptor subunit.";
RL J. Neurochem. 52:988-991(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Groot-Kormelink P.J.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBUNIT, AND SITES LYS-81; ILE-133 AND GLN-141.
RX PubMed=16964981; DOI=10.1021/bi0611715;
RA Shiembob D.L., Roberts R.L., Luetje C.W., McIntosh J.M.;
RT "Determinants of alpha-conotoxin BuIA selectivity on the nicotinic
RT acetylcholine receptor beta subunit.";
RL Biochemistry 45:11200-11207(2006).
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 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 (By similarity).
CC Interacts with LYPD6 (By similarity). The pentamer alpha3-beta-4
CC interacts with the conotoxin BuIA (PubMed:16964981). The heteropentamer
CC composed of alpha-3 and beta-4 subunits interacts with the alpha-
CC conotoxin ImI (By similarity). {ECO:0000250|UniProtKB:P30926,
CC ECO:0000269|PubMed:16964981}.
CC -!- INTERACTION:
CC P12392; P09483: Chrna4; NbExp=4; IntAct=EBI-9008856, EBI-7842410;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Short;
CC IsoId=P12392-1; Sequence=Displayed;
CC Name=Long;
CC IsoId=P12392-2; Sequence=VSP_000076;
CC -!- TISSUE SPECIFICITY: In the brain, it is detected in the medial
CC habenula. In the peripheral nervous system, it is found at least in the
CC adrenal gland.
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; U42976; AAA85212.1; -; mRNA.
DR EMBL; M33953; AAA41668.1; -; Genomic_DNA.
DR EMBL; J05232; AAA41668.1; JOINED; Genomic_DNA.
DR EMBL; M89971; AAA41668.1; JOINED; Genomic_DNA.
DR EMBL; M33951; AAA41668.1; JOINED; Genomic_DNA.
DR EMBL; M89989; AAA41668.1; JOINED; Genomic_DNA.
DR EMBL; M33952; AAA41668.1; JOINED; Genomic_DNA.
DR EMBL; X15834; CAA33839.1; -; mRNA.
DR EMBL; AY574260; AAS90356.1; -; mRNA.
DR PIR; A30992; A30992.
DR PIR; B35721; B35721.
DR RefSeq; NP_434693.1; NM_052806.2. [P12392-1]
DR AlphaFoldDB; P12392; -.
DR SMR; P12392; -.
DR ComplexPortal; CPX-183; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta4.
DR ComplexPortal; CPX-205; Neuronal nicotinic acetylcholine receptor complex, alpha3-beta4.
DR ComplexPortal; CPX-208; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4.
DR ComplexPortal; CPX-211; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta4.
DR ComplexPortal; CPX-219; Neuronal nicotinic acetylcholine receptor complex, alpha4-beta4.
DR IntAct; P12392; 6.
DR STRING; 10116.ENSRNOP00000051052; -.
DR BindingDB; P12392; -.
DR ChEMBL; CHEMBL2658; -.
DR DrugCentral; P12392; -.
DR GlyGen; P12392; 4 sites.
DR PhosphoSitePlus; P12392; -.
DR PaxDb; P12392; -.
DR Ensembl; ENSRNOT00000019458; ENSRNOP00000019458; ENSRNOG00000014427. [P12392-1]
DR GeneID; 25103; -.
DR KEGG; rno:25103; -.
DR UCSC; RGD:2351; rat. [P12392-1]
DR CTD; 1143; -.
DR RGD; 2351; Chrnb4.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000158708; -.
DR HOGENOM; CLU_018074_1_1_1; -.
DR InParanoid; P12392; -.
DR OMA; PSKLYGN; -.
DR OrthoDB; 381858at2759; -.
DR Reactome; R-RNO-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR Reactome; R-RNO-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR Reactome; R-RNO-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P12392; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000014427; Expressed in ovary and 8 other tissues.
DR Genevisible; P12392; RN.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098981; C:cholinergic synapse; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0042166; F:acetylcholine binding; IDA:RGD.
DR GO; GO:0015464; F:acetylcholine receptor activity; ISO:RGD.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; ISO:RGD.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:1901363; F:heterocyclic compound binding; IDA:RGD.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
DR GO; GO:0001508; P:action potential; ISO:RGD.
DR GO; GO:0035095; P:behavioral response to nicotine; ISO:RGD.
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:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0051899; P:membrane depolarization; IDA:ComplexPortal.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR GO; GO:0051971; P:positive regulation of transmission of nerve impulse; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; ISO:RGD.
DR GO; GO:0035094; P:response to nicotine; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0006939; P:smooth muscle contraction; ISO:RGD.
DR GO; GO:0060084; P:synaptic transmission involved in micturition; ISO:RGD.
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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..495
FT /note="Neuronal acetylcholine receptor subunit beta-4"
FT /id="PRO_0000000391"
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:0000305|PubMed:16964981"
FT SITE 133
FT /note="Key residue for a low dissociation (K(off)) from the
FT conotoxin BuIA"
FT /evidence="ECO:0000305|PubMed:16964981"
FT SITE 141
FT /note="Key residue for a low dissociation (K(off)) from the
FT conotoxin BuIA"
FT /evidence="ECO:0000305|PubMed:16964981"
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"
FT VAR_SEQ 17
FT /note="D -> DARLFDCSGVLPDKGPAGLTVRFP (in isoform Long)"
FT /evidence="ECO:0000303|PubMed:2918319"
FT /id="VSP_000076"
FT CONFLICT 9
FT /note="V -> VV (in Ref. 3; CAA33839)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="Missing (in Ref. 2; AAA41668)"
FT /evidence="ECO:0000305"
FT CONFLICT 230..231
FT /note="KP -> NA (in Ref. 2; AAA41668 and 3; CAA33839)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..288
FT /note="Missing (in Ref. 3; CAA33839)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="D -> N (in Ref. 3; CAA33839)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 55861 MW; 688F37AB80448F7F CRC64;
MRGTPLLLVS LFSLLQDGDC 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 LEVSLVRVPH
PSQLHLATAD TAATSALGPT SPSNLYGSSM YFVNPVPAAP KSAVSSHTAG LPRDARLRSS
GRFREDLQEA LEGVSFIAQH LESDDRDQSV IEDWKFVAMV VDRLFLWVFV FVCILGTMGL
FLPPLFQIHA PSKDS
