ID   ACHB3_CHICK             Reviewed;         455 AA.
AC   P43679;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Neuronal acetylcholine receptor subunit beta-3;
DE   Flags: Precursor;
GN   Name=CHRNB3;
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;
RX   PubMed=7852408; DOI=10.1074/jbc.270.7.3224;
RA   Hernandez M.C., Erkman L., Matter-Sadzinski L., Roztocil T., Ballivet M.,
RA   Matter J.-M.;
RT   "Characterization of the nicotinic acetylcholine receptor beta 3 gene. Its
RT   regulation within the avian nervous system is effected by a promoter 143
RT   base pairs in length.";
RL   J. Biol. Chem. 270:3224-3233(1995).
RN   [2]
RP   SEQUENCE REVISION TO 331.
RA   Ballivet M.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
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 beta.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Relatively abundant in the developing retina and in
CC       the trigeminal ganglion.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. Beta-3/CHRNB3 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X83739; CAB59814.1; -; mRNA.
DR   PIR; A55972; A55972.
DR   AlphaFoldDB; P43679; -.
DR   SMR; P43679; -.
DR   ComplexPortal; CPX-201; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3.
DR   STRING; 9031.ENSGALP00000024774; -.
DR   PaxDb; P43679; -.
DR   VEuPathDB; HostDB:geneid_395604; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   InParanoid; P43679; -.
DR   OrthoDB; 381858at2759; -.
DR   PhylomeDB; P43679; -.
DR   Proteomes; UP000000539; 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   GO; GO:0051899; P:membrane depolarization; IC:ComplexPortal.
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; 2.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..455
FT                   /note="Neuronal acetylcholine receptor subunit beta-3"
FT                   /id="PRO_0000000387"
FT   TOPO_DOM        21..229
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        318..425
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        426..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        150..164
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   455 AA;  52276 MW;  3D7A7AFA77D8511A CRC64;
     MLCLMLCVLC WSRSDVAALG SVVENEDALL RHLFQGYQKW VRPVENSNDT IKVLFGLKIS
     QLVDVDEKNQ LMTTNVWLKQ EWMDHKLSWN PEEYGGITAI RVPSESLWLP DIVLFENADG
     RFEGSLMTKA IVKYNGVVQW MPPASYKSSC TMELTFFPFD RQNCSMKFGS WTYDGSMVDL
     ILVDENVDTK DFFDNGEWEI LNAKGMKGNR KDGLYSYPFV TYSFVLRRLP LFYTLFLIIP
     CLGLSFLTVL VFYLPSDEGE KLSLSTSVLV SLTVFLLVIE EIIPSSSKVI PLIGEYLLFI
     MIFVTLSIIV TVFVINVHHR SSATYHPMAP WVKRLFLQKL PRLLCMKGHV DRYSFSDTEE
     KETTLKSKLP GKQKHKQAKD GEKVVIAFLE KAADSIRYIS RHVKKDAFIR QVVQDWKFVA
     QVLDRIFLWL FLVVSVTGSV LIFTPALQMW LNSTL