ACHA3_RAT
ID ACHA3_RAT Reviewed; 499 AA.
AC P04757;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-3;
DE Flags: Precursor;
GN Name=Chrna3; Synonyms=Acra3;
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=3753746; DOI=10.1038/319368a0;
RA Boulter J., Evans K., Goldman D.J., Martin G., Treco D., Heinemann S.F.,
RA Patrick J.;
RT "Isolation of a cDNA clone coding for a possible neural nicotinic
RT acetylcholine receptor alpha-subunit.";
RL Nature 319:368-374(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2444984; DOI=10.1073/pnas.84.21.7763;
RA Boulter J., Connolly J.G., Deneris E.S., Goldman D.J., Heinemann S.F.,
RA Patrick J.;
RT "Functional expression of two neuronal nicotinic acetylcholine receptors
RT from cDNA clones identifies a gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7763-7767(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC TISSUE=Liver;
RX PubMed=8144606; DOI=10.1016/s0021-9258(17)34055-3;
RA Yang X., McDonough J., Fyodorov D., Morris M., Wang F., Deneris E.S.;
RT "Characterization of an acetylcholine receptor alpha 3 gene promoter and
RT its activation by the POU domain factor SCIP/Tst-1.";
RL J. Biol. Chem. 269:10252-10264(1994).
RN [4]
RP SUBUNIT.
RX PubMed=15609996; DOI=10.1021/bi048918g;
RA Ellison M., Gao F., Wang H.L., Sine S.M., McIntosh J.M., Olivera B.M.;
RT "Alpha-conotoxins ImI and ImII target distinct regions of the human alpha7
RT nicotinic acetylcholine receptor and distinguish human nicotinic receptor
RT subtypes.";
RL Biochemistry 43:16019-16026(2004).
RN [5]
RP SUBUNIT.
RX PubMed=15929983; DOI=10.1074/jbc.m504229200;
RA Dutertre S., Nicke A., Lewis R.J.;
RT "Beta2 subunit contribution to 4/7 alpha-conotoxin binding to the nicotinic
RT acetylcholine receptor.";
RL J. Biol. Chem. 280:30460-30468(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-410, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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 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 (PubMed:15609996, PubMed:15929983).
CC {ECO:0000250|UniProtKB:P32297, ECO:0000269|PubMed:15609996,
CC ECO:0000269|PubMed:15929983}.
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. Alpha-3/CHRNA3 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X03440; CAA27170.1; -; mRNA.
DR EMBL; L31621; AAA41673.1; -; mRNA.
DR EMBL; U04961; AAA18001.1; -; Unassigned_DNA.
DR PIR; A24572; A24572.
DR PIR; A53733; A53733.
DR AlphaFoldDB; P04757; -.
DR SMR; P04757; -.
DR ComplexPortal; CPX-190; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2.
DR ComplexPortal; CPX-191; Neuronal nicotinic acetylcholine receptor complex, alpha3-beta2.
DR ComplexPortal; CPX-203; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3.
DR ComplexPortal; CPX-205; Neuronal nicotinic acetylcholine receptor complex, alpha3-beta4.
DR ComplexPortal; CPX-208; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4.
DR ComplexPortal; CPX-211; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta4.
DR IntAct; P04757; 3.
DR STRING; 10116.ENSRNOP00000019307; -.
DR BindingDB; P04757; -.
DR ChEMBL; CHEMBL1907587; -.
DR ChEMBL; CHEMBL1907593; -.
DR ChEMBL; CHEMBL3137275; -.
DR ChEMBL; CHEMBL3137276; -.
DR ChEMBL; CHEMBL4106146; -.
DR DrugCentral; P04757; -.
DR GuidetoPHARMACOLOGY; 464; -.
DR GlyGen; P04757; 2 sites.
DR iPTMnet; P04757; -.
DR PhosphoSitePlus; P04757; -.
DR PaxDb; P04757; -.
DR PRIDE; P04757; -.
DR UCSC; RGD:2345; rat.
DR RGD; 2345; Chrna3.
DR eggNOG; KOG3645; Eukaryota.
DR InParanoid; P04757; -.
DR PhylomeDB; P04757; -.
DR Reactome; R-RNO-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
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:P04757; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:RGD.
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; IDA:RGD.
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:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0044853; C:plasma membrane raft; IGI:ARUK-UCL.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
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:0015464; F:acetylcholine receptor activity; IDA:RGD.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IMP:RGD.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:1901363; F:heterocyclic compound binding; IDA:RGD.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IGI:ARUK-UCL.
DR GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0035095; P:behavioral response to nicotine; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0007507; P:heart development; IEP:RGD.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0051899; P:membrane depolarization; IDA:ComplexPortal.
DR GO; GO:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0014056; P:regulation of acetylcholine secretion, neurotransmission; ISO:RGD.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0006937; P:regulation of muscle contraction; ISO:RGD.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:1905144; P:response to acetylcholine; IGI:ARUK-UCL.
DR GO; GO:0034465; P:response to carbon monoxide; IEP:RGD.
DR GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0060084; P:synaptic transmission involved in micturition; ISO:RGD.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; ISO:RGD.
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 1: Evidence at protein 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_0000000348"
FT TOPO_DOM 26..234
FT /note="Extracellular"
FT TRANSMEM 235..259
FT /note="Helical"
FT TRANSMEM 267..285
FT /note="Helical"
FT TRANSMEM 301..322
FT /note="Helical"
FT TOPO_DOM 323..471
FT /note="Cytoplasmic"
FT TRANSMEM 472..491
FT /note="Helical"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
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; 56998 MW; D66C491E832B9C34 CRC64;
MGVVLLPPPL SMLMLVLMLL PAASASEAEH 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 TRPTSGEGDT
PKTRTFYGAE LSNLNCFSRA DSKSCKEGYP CQDGTCGYCH HRRVKISNFS ANLTRSSSSE
SVNAVLSLSA LSPEIKEAIQ SVKYIAENMK AQNVAKEIQD DWKYVAMVID RIFLWVFILV
CILGTAGLFL QPLMARDDT
