ACHB4_BOVIN
ID ACHB4_BOVIN Reviewed; 496 AA.
AC Q8SPU6;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Neuronal acetylcholine receptor subunit beta-4;
DE Flags: Precursor;
GN Name=CHRNB4; Synonyms=ACRB4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal medulla;
RX PubMed=9003033; DOI=10.1046/j.1471-4159.1997.68020488.x;
RA Campos-Caro A., Smillie F.I., Dominguez del Toro E., Rovira J.C.,
RA Vicente-Agullo F., Chapuli J., Juiz J.M., Sala S., Sala F., Ballesta J.J.,
RA Criado M.;
RT "Neuronal nicotinic acetylcholine receptors on bovine chromaffin cells:
RT cloning, expression, and genomic organization of receptor subunits.";
RL J. Neurochem. 68:488-497(1997).
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 -!- 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; AF487465; AAL88712.1; -; mRNA.
DR RefSeq; NP_776942.1; NM_174517.1.
DR AlphaFoldDB; Q8SPU6; -.
DR SMR; Q8SPU6; -.
DR STRING; 9913.ENSBTAP00000048228; -.
DR ChEMBL; CHEMBL3350221; -.
DR PaxDb; Q8SPU6; -.
DR PRIDE; Q8SPU6; -.
DR GeneID; 282181; -.
DR KEGG; bta:282181; -.
DR CTD; 1143; -.
DR eggNOG; KOG3645; Eukaryota.
DR InParanoid; Q8SPU6; -.
DR OrthoDB; 381858at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..496
FT /note="Neuronal acetylcholine receptor subunit beta-4"
FT /id="PRO_0000000388"
FT TOPO_DOM 20..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..496
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT SITE 82
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 CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 153..167
FT /evidence="ECO:0000250"
SQ SEQUENCE 496 AA; 55946 MW; 3A2412BE46AAA349 CRC64;
MRSALPLVLF SLVALCGRGD CRVANAEEKL MDDLLNKTRY NNLIRPATSS SQLISIQLQL
SLAQLISVNE REQIMTTNIW LKQEWTDYRL AWNSSRYEGV NILRIPANRV WLPDIVLYNN
ADGSYEVSLY TNVVVRSNGS VMWLPPAICK SACKIEVKHF PFDQQNCTLK FRSWTYDHTE
IDMVLKMPTA SMDDFTPSGE WDIVALPGRR TVNPQDPSYV DVTYDFIIKR KPLFYTINLI
IPCVLITSLA ILVFYLPSDC GEKMTLCISV LLALTVFLLL ISKIVPPTSL NVPLIGKYLM
FTMVLVTFSI VTSVCVLNVH HRSPSTHTMA PWVKRCFLHK LPTFLFIKRP RQQPSRAPQS
SLARLTKSEA TTTTTLAMGP TSSSNLYGNS MYFVNPGLAA PKSPVASDSA GIPRDFRLRS
SGRFRQDVQE ALEGVSFIAQ HMKSDDLDQS VIEDWKYVAM VVDRLFLWVF VVVCVLGTVG
LFLPPLFQTH TPSEEP
