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ACHB3_RAT
ID   ACHB3_RAT               Reviewed;         464 AA.
AC   P12391;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=Neuronal acetylcholine receptor subunit beta-3;
DE   Flags: Precursor;
GN   Name=Chrnb3; Synonyms=Acrb3;
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].
RX   PubMed=2703489; DOI=10.1016/s0021-9258(18)83343-9;
RA   Deneris E.S., Boulter J., Swanson L.W., Patrick J., Heinemann S.F.;
RT   "Beta 3: a new member of nicotinic acetylcholine receptor gene family is
RT   expressed in brain.";
RL   J. Biol. Chem. 264:6268-6272(1989).
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 types of
CC       subunits: alpha and beta.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
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; J04636; AAC28887.1; -; mRNA.
DR   PIR; A33523; A33523.
DR   RefSeq; NP_598281.1; NM_133597.1.
DR   AlphaFoldDB; P12391; -.
DR   SMR; P12391; -.
DR   ComplexPortal; CPX-203; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3.
DR   STRING; 10116.ENSRNOP00000016656; -.
DR   BindingDB; P12391; -.
DR   ChEMBL; CHEMBL3137275; -.
DR   ChEMBL; CHEMBL3883329; -.
DR   DrugCentral; P12391; -.
DR   GlyGen; P12391; 2 sites.
DR   PhosphoSitePlus; P12391; -.
DR   PaxDb; P12391; -.
DR   Ensembl; ENSRNOT00000016656; ENSRNOP00000016656; ENSRNOG00000012448.
DR   GeneID; 171131; -.
DR   KEGG; rno:171131; -.
DR   UCSC; RGD:621544; rat.
DR   CTD; 1142; -.
DR   RGD; 621544; Chrnb3.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000156892; -.
DR   HOGENOM; CLU_018074_1_2_1; -.
DR   InParanoid; P12391; -.
DR   OMA; EWMDHKL; -.
DR   OrthoDB; 381858at2759; -.
DR   PhylomeDB; P12391; -.
DR   TreeFam; TF315605; -.
DR   Reactome; R-RNO-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR   Reactome; R-RNO-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR   PRO; PR:P12391; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000012448; Expressed in testis and 3 other tissues.
DR   Genevisible; P12391; 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:0098691; C:dopaminergic 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: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: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:0051899; P:membrane depolarization; IC:ComplexPortal.
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:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
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..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..464
FT                   /note="Neuronal acetylcholine receptor subunit beta-3"
FT                   /id="PRO_0000000386"
FT   TOPO_DOM        31..238
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        327..434
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        435..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        159..173
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   464 AA;  53261 MW;  5D3B1F7DB934D1D8 CRC64;
     MTGFLRVFLV LSATLSGSWV TLTATAGLSS VAEHEDALLR HLFQGYQKWV RPVLNSSDII
     KVYFGLKISQ LVDVDEKNQL MTTNVWLKQE WTDQKLRWNP EEYGGINSIK VPSESLWLPD
     IVLFENADGR FEGSLMTKAI VKSSGTVSWT PPASYKSSCT MDVTFFPFDR QNCSMKFGSW
     TYDGTMVDLI LINENVDRKD FFDNGEWEIL NAKGMKGNRR EGFYSYPFVT YSFVLRRLPL
     FYTLFLIIPC LGLSFLTVLV FYLPSDEGEK LSLSTSVLVS LTVFLLVIEE IIPSSSKVIP
     LIGEYLLFIM IFVTLSIIVT VFVINVHHRS SSTYHPMAPW VKRLFLQRLP RWLCMKDPMD
     RFSFPDGKES DTAVRGKVSG KRKQTPASDG ERVLVAFLEK ASESIRYISR HVKKEHFISQ
     VVQDWKFVAQ VLDRIFLWLF LIASVLGSIL IFIPALKMWI HRFH
 
 
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