ID   ACHB3_MOUSE             Reviewed;         464 AA.
AC   Q8BMN3; Q8R5H3; Q9CYK8;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 168.
DE   RecName: Full=Neuronal acetylcholine receptor subunit beta-3;
DE   Flags: Precursor;
GN   Name=Chrnb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Stitzel J.A., Lautner M.A., Jimenez M., Bhandarkar S.J., Curtis C.D.,
RA   Remias J.;
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RA   Groot-Kormelink P.J.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(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 types of
CC       subunits: alpha and beta. {ECO:0000250}.
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=1;
CC         IsoId=Q8BMN3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BMN3-2; Sequence=VSP_013775;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF467896; AAL75573.1; -; mRNA.
DR   EMBL; AY574268; AAS90364.1; -; mRNA.
DR   EMBL; AK017571; BAB30812.1; -; mRNA.
DR   EMBL; AK030464; BAC26973.1; -; mRNA.
DR   EMBL; BC058193; AAH58193.1; -; mRNA.
DR   CCDS; CCDS22216.1; -. [Q8BMN3-2]
DR   CCDS; CCDS22217.1; -. [Q8BMN3-1]
DR   RefSeq; NP_081730.1; NM_027454.4. [Q8BMN3-2]
DR   RefSeq; NP_775304.1; NM_173212.4. [Q8BMN3-1]
DR   AlphaFoldDB; Q8BMN3; -.
DR   SMR; Q8BMN3; -.
DR   ComplexPortal; CPX-202; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3.
DR   STRING; 10090.ENSMUSP00000052297; -.
DR   ChEMBL; CHEMBL3885610; -.
DR   GlyCosmos; Q8BMN3; 2 sites, No reported glycans.
DR   GlyGen; Q8BMN3; 2 sites.
DR   iPTMnet; Q8BMN3; -.
DR   PhosphoSitePlus; Q8BMN3; -.
DR   EPD; Q8BMN3; -.
DR   PaxDb; 10090-ENSMUSP00000052297; -.
DR   ProteomicsDB; 285922; -. [Q8BMN3-1]
DR   ProteomicsDB; 285923; -. [Q8BMN3-2]
DR   Antibodypedia; 11480; 194 antibodies from 33 providers.
DR   DNASU; 108043; -.
DR   Ensembl; ENSMUST00000060943.5; ENSMUSP00000052297.4; ENSMUSG00000031492.14. [Q8BMN3-1]
DR   Ensembl; ENSMUST00000079463.12; ENSMUSP00000078428.5; ENSMUSG00000031492.14. [Q8BMN3-2]
DR   GeneID; 108043; -.
DR   KEGG; mmu:108043; -.
DR   UCSC; uc009lit.2; mouse. [Q8BMN3-1]
DR   UCSC; uc009liu.2; mouse. [Q8BMN3-2]
DR   AGR; MGI:106212; -.
DR   CTD; 1142; -.
DR   MGI; MGI:106212; Chrnb3.
DR   VEuPathDB; HostDB:ENSMUSG00000031492; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000156892; -.
DR   HOGENOM; CLU_018074_1_0_1; -.
DR   InParanoid; Q8BMN3; -.
DR   OMA; VRHNGTI; -.
DR   OrthoDB; 5489962at2759; -.
DR   PhylomeDB; Q8BMN3; -.
DR   TreeFam; TF315605; -.
DR   Reactome; R-MMU-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR   Reactome; R-MMU-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR   BioGRID-ORCS; 108043; 1 hit in 78 CRISPR screens.
DR   PRO; PR:Q8BMN3; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8BMN3; Protein.
DR   Bgee; ENSMUSG00000031492; Expressed in retinal neural layer and 30 other cell types or tissues.
DR   ExpressionAtlas; Q8BMN3; baseline and differential.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; ISO:MGI.
DR   GO; GO:0098691; C:dopaminergic synapse; IDA:SynGO.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0042166; F:acetylcholine binding; ISO:MGI.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IBA:GO_Central.
DR   GO; GO:1901363; F:heterocyclic compound binding; IEA:Ensembl.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:0035094; P:response to nicotine; IBA:GO_Central.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
DR   CDD; cd19064; LGIC_TM_nAChR; 1.
DR   Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR   Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 2.
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   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945:SF75; NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT BETA-3; 1.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 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; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR   SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
DR   Genevisible; Q8BMN3; MM.
PE   2: Evidence at transcript 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..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..464
FT                   /note="Neuronal acetylcholine receptor subunit beta-3"
FT                   /id="PRO_0000000384"
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   REGION          368..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT   VAR_SEQ         75..89
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_013775"
FT   CONFLICT        170
FT                   /note="K -> R (in Ref. 1; AAL75573)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   464 AA;  53112 MW;  2ECEA3E0DAF2D5EB CRC64;
     MTGFLRVFLA LSATLSGSWV TLTATAGLSS VAEHEDALLR HLFQGYQKCV RPVLNSSDII
     KVYFGLKISQ LVDVDEKNQL MTTNVWLKQE WTDQKLRWNP EDYGGINSIK VPSESLWLPD
     IVLFENADGR FEGSLMTKAI VKSSGTVSWT PPASYKSSCT MDVTFFPFDK QNCSMKFGSW
     TYDGTMVDLI LINENVDRKD FFDNGEWEIL NAKGMKGNRR EGFYSYPFVT YSFVLRRLPL
     FYTLFLIIPC LGLSFLTVLV FYLPSDEGEK LSLSTSVLVS LTVFLLVIEE IIPSSSKVIP
     LIGEYLLFIM IFVTLSIIVT VFVINVHHRS SSTYHPMAPW VKRLFLEKLP RWLCMKDPRD
     RFSFPDGTES KGTVRGKFPG KKKQTPTSDG ERVLVAFLEK ASESIRYISR HVKKEHFISQ
     VVQDWKFVAQ VLDRIFLWLF LTASVLGSVL IFIPALKMWI HRFH
//