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ACHB3_PANTR
ID   ACHB3_PANTR             Reviewed;         458 AA.
AC   Q5IS75;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Neuronal acetylcholine receptor subunit beta-3;
DE   Flags: Precursor;
GN   Name=CHRNB3;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA   Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA   Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT   "Accelerated evolution of nervous system genes in the origin of Homo
RT   sapiens.";
RL   Cell 119:1027-1040(2004).
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 seems to be composed of two different type of
CC       subunits: alpha and beta. {ECO:0000250}.
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-3/CHRNB3 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY665253; AAV74291.1; -; mRNA.
DR   RefSeq; NP_001029105.1; NM_001033933.1.
DR   AlphaFoldDB; Q5IS75; -.
DR   SMR; Q5IS75; -.
DR   STRING; 9598.ENSPTRP00000054732; -.
DR   PaxDb; Q5IS75; -.
DR   Ensembl; ENSPTRT00000062178; ENSPTRP00000054732; ENSPTRG00000020209.
DR   GeneID; 464500; -.
DR   KEGG; ptr:464500; -.
DR   CTD; 1142; -.
DR   VGNC; VGNC:7590; CHRNB3.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000156892; -.
DR   InParanoid; Q5IS75; -.
DR   OMA; QHSNDTI; -.
DR   OrthoDB; 381858at2759; -.
DR   Proteomes; UP000002277; Chromosome 8.
DR   Bgee; ENSPTRG00000020209; Expressed in dorsolateral prefrontal cortex and 3 other tissues.
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:0050877; P:nervous system process; IBA:GO_Central.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   GO; GO:0035094; P:response to nicotine; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; 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; 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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..458
FT                   /note="Neuronal acetylcholine receptor subunit beta-3"
FT                   /id="PRO_0000000385"
FT   TOPO_DOM        25..232
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..428
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        429..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        51
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   458 AA;  52729 MW;  D6E919E53CBD21F8 CRC64;
     MLPDFMLVLI VLGIPSSATT GFNSIAENED ALLRHLFQGY QKWVRPVLHS NDTIKVYFGL
     KISQLVDVDE KNQLMTTNVW LKQEWTDHKL RWNPDDYGGI HSIKVPSESL WLPDIVLFEN
     ADGRFEGSLM TKVIVKSNGT VVWTPPASYK SSCTMDVTFF PFDRQNCSMK FGSWTYDGTM
     VDLILINENV DRKDFFDNGE WEILNAKGMK GNRRDGVYSY PFITYSFVLR RLPLFYTLFL
     IIPCLGLSFL TVLVFYLPSD EGEKLSLSTS VLVSLTVFLL VIEEIIPSSS KVIPLIGEYL
     LFIMIFVTLS IIVTVFVINV HHRSSSTYHP MAPWVKRLFL QKLPKLLCMK DHVDRYSSPE
     KEESQPVVKG KVLEKKKQKQ LSDGEKVLVA FLEKAADSIR YISRHVKKEH FISQVVQDWK
     FVAQVLDRIF LWLFLIVSVT GSVLIFTPAL KMWLHSYH
 
 
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