ACHA3_MOUSE
ID ACHA3_MOUSE Reviewed; 499 AA.
AC Q8R4G9; Q8BV44;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-3;
DE Flags: Precursor;
GN Name=Chrna3;
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].
RC STRAIN=DBA/2Ibg; TISSUE=Adrenal gland;
RA Lautner M.A., Stitzel J.A.;
RT "Cloning of mouse nicotinic acetylcholine receptor alpha 3 subunit cDNA.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Eye, and Spinal ganglion;
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).
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 is composed of two different types of subunits:
CC alpha and beta. Alpha-3 subunit can be combined to beta-2 or beta-4 to
CC give rise to functional receptors. Interacts with RIC3; which is
CC required for proper folding and assembly. Interacts with LYPD6. The
CC heteropentamer alpha-3-beta-2 interacts with alpha-conotoxins ImI,
CC ImII, PnIA, GID and MII. The heteropentamer alpha-3-beta-4 interacts
CC with the alpha-conotoxin ImI. {ECO:0000250|UniProtKB:P04757,
CC ECO:0000250|UniProtKB:P32297}.
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. Alpha-3/CHRNA3 sub-
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37909.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF472588; AAL84757.1; -; mRNA.
DR EMBL; AY574262; AAS90358.1; -; mRNA.
DR EMBL; AK051730; BAC34740.1; -; mRNA.
DR EMBL; AK053497; BAC35404.1; -; mRNA.
DR EMBL; AK080415; BAC37909.1; ALT_INIT; mRNA.
DR CCDS; CCDS23199.2; -.
DR RefSeq; NP_660111.2; NM_145129.2.
DR AlphaFoldDB; Q8R4G9; -.
DR SMR; Q8R4G9; -.
DR BioGRID; 225944; 2.
DR ComplexPortal; CPX-188; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2.
DR ComplexPortal; CPX-189; Neuronal nicotinic acetylcholine receptor complex, alpha3-beta2.
DR ComplexPortal; CPX-202; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3.
DR ComplexPortal; CPX-204; Neuronal nicotinic acetylcholine receptor complex, alpha3-beta4.
DR ComplexPortal; CPX-209; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4.
DR ComplexPortal; CPX-212; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta4.
DR STRING; 10090.ENSMUSP00000034851; -.
DR ChEMBL; CHEMBL3885609; -.
DR GlyGen; Q8R4G9; 2 sites.
DR PhosphoSitePlus; Q8R4G9; -.
DR MaxQB; Q8R4G9; -.
DR PaxDb; Q8R4G9; -.
DR PRIDE; Q8R4G9; -.
DR ProteomicsDB; 285582; -.
DR Antibodypedia; 15113; 304 antibodies from 33 providers.
DR DNASU; 110834; -.
DR Ensembl; ENSMUST00000034851; ENSMUSP00000034851; ENSMUSG00000032303.
DR GeneID; 110834; -.
DR KEGG; mmu:110834; -.
DR UCSC; uc009pry.1; mouse.
DR CTD; 1136; -.
DR MGI; MGI:87887; Chrna3.
DR VEuPathDB; HostDB:ENSMUSG00000032303; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000158487; -.
DR InParanoid; Q8R4G9; -.
DR OMA; AEHRLYA; -.
DR OrthoDB; 381858at2759; -.
DR PhylomeDB; Q8R4G9; -.
DR Reactome; R-MMU-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
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; 110834; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Chrna3; mouse.
DR PRO; PR:Q8R4G9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R4G9; protein.
DR Bgee; ENSMUSG00000032303; Expressed in lumbar dorsal root ganglion and 76 other tissues.
DR ExpressionAtlas; Q8R4G9; baseline and differential.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IPI:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0098691; C:dopaminergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IC:MGI.
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:0015464; F:acetylcholine receptor activity; ISO:MGI.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IMP:MGI.
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:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISO:MGI.
DR GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; IMP:MGI.
DR GO; GO:0035095; P:behavioral response to nicotine; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0051899; P:membrane depolarization; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0014056; P:regulation of acetylcholine secretion, neurotransmission; IMP:MGI.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR GO; GO:0006937; P:regulation of muscle contraction; IMP:MGI.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; IMP:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:1905144; P:response to acetylcholine; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0060084; P:synaptic transmission involved in micturition; IMP:MGI.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:MGI.
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 Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..499
FT /note="Neuronal acetylcholine receptor subunit alpha-3"
FT /id="PRO_0000000347"
FT TOPO_DOM 26..234
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04757"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04757"
FT CARBOHYD 49
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"
FT DISULFID 217..218
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 499 AA; 57110 MW; 721650E3F38D00FD CRC64;
MGVVLPPPPL SMLMLVLMLL PVASASEAEH RLFQYLFEDY NEIIRPVANV SHPVIIQFEV
SMSQLVKVDE VNQIMETNLW LKQIWNDYKL KWKPSDYQGV EFMRVPAEKI WKPDIVLYNN
ADGDFQVDDK TKALLKYTGE VTWIPPAIFK SSCKIDVTYF PFDYQNCTMK FGSWSYDKAK
IDLVLIGSSM NLKDYWESGE WAIIKAPGYK HEIKYNCCEE IYQDITYSLY IRRLPLFYTI
NLIIPCLLIS FLTVLVFYLP SDCGEKVTLC ISVLLSLTVF LLVITETIPS TSLVIPLIGE
YLLFTMIFVT LSIVITVFVL NVHYRTPTTH TMPTWVKAVF LNLLPRVMFM TRPTSTEEDA
PKTRNFYGAE LSNLNCFSRA DSKSCKEGYP CQDGTCGYCH HRRVKISNFS ANLTRSSSSE
SVDAVLSLSA LSPEIKEAIQ SVKYIAENMK AQNVAKEIQD DWKYVAMVID RIFLWVFILV
CILGTAGLFL QPLMARDDT
