ACHB3_MOUSE
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 03-AUG-2022, entry version 160.
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}.
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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 GlyGen; Q8BMN3; 2 sites.
DR iPTMnet; Q8BMN3; -.
DR PhosphoSitePlus; Q8BMN3; -.
DR EPD; Q8BMN3; -.
DR PaxDb; Q8BMN3; -.
DR PRIDE; Q8BMN3; -.
DR ProteomicsDB; 285922; -. [Q8BMN3-1]
DR ProteomicsDB; 285923; -. [Q8BMN3-2]
DR Antibodypedia; 11480; 185 antibodies from 33 providers.
DR DNASU; 108043; -.
DR Ensembl; ENSMUST00000060943; ENSMUSP00000052297; ENSMUSG00000031492. [Q8BMN3-1]
DR Ensembl; ENSMUST00000079463; ENSMUSP00000078428; ENSMUSG00000031492. [Q8BMN3-2]
DR GeneID; 108043; -.
DR KEGG; mmu:108043; -.
DR UCSC; uc009lit.2; mouse. [Q8BMN3-1]
DR UCSC; uc009liu.2; mouse. [Q8BMN3-2]
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; EWMDHKL; -.
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 73 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 tissues.
DR ExpressionAtlas; Q8BMN3; baseline and differential.
DR Genevisible; Q8BMN3; MM.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; ISO:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098691; C:dopaminergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
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 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:1901363; F:heterocyclic compound binding; ISO:MGI.
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; IDA:SynGO.
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; 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 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
