ACHA2_MOUSE
ID ACHA2_MOUSE Reviewed; 512 AA.
AC Q91X60;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-2;
DE Flags: Precursor;
GN Name=Chrna2;
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=BALB/cJ; TISSUE=Brain;
RA Groot-Kormelink P.J.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 non-alpha (beta). Alpha-2 subunit can be combined
CC to beta-2 or beta-4 to give rise to functional receptors. The alpha-
CC 2:beta-2 nAChR complex is proposed to be a heteropentamer with two
CC subtypes: LS (low agonist sensitivity) with a (alpha-2)3:(beta-2)2 and
CC HS (high agonist sensitivity) with a (alpha-2)2:(beta-2)3
CC stoichiometry; the subtypes differ in their subunit binding interfaces
CC which are involved in ligand binding (By similarity).
CC {ECO:0000250|UniProtKB:Q15822}.
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-2/CHRNA2 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; AY574261; AAS90357.1; -; mRNA.
DR EMBL; BC011490; AAH11490.1; -; mRNA.
DR CCDS; CCDS27219.1; -.
DR RefSeq; NP_659052.1; NM_144803.2.
DR RefSeq; XP_006518497.1; XM_006518434.3.
DR RefSeq; XP_006518498.1; XM_006518435.3.
DR RefSeq; XP_006518499.1; XM_006518436.3.
DR AlphaFoldDB; Q91X60; -.
DR SMR; Q91X60; -.
DR ComplexPortal; CPX-174; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2.
DR ComplexPortal; CPX-182; Neuronal nicotinic acetylcholine receptor complex, alpha2-beta4.
DR STRING; 10090.ENSMUSP00000022620; -.
DR ChEMBL; CHEMBL3350222; -.
DR GlyGen; Q91X60; 3 sites.
DR iPTMnet; Q91X60; -.
DR PhosphoSitePlus; Q91X60; -.
DR PaxDb; Q91X60; -.
DR PRIDE; Q91X60; -.
DR ProteomicsDB; 286066; -.
DR Antibodypedia; 10197; 174 antibodies from 24 providers.
DR DNASU; 110902; -.
DR Ensembl; ENSMUST00000022620; ENSMUSP00000022620; ENSMUSG00000022041.
DR Ensembl; ENSMUST00000206455; ENSMUSP00000145896; ENSMUSG00000022041.
DR GeneID; 110902; -.
DR KEGG; mmu:110902; -.
DR UCSC; uc007ujx.1; mouse.
DR CTD; 1135; -.
DR MGI; MGI:87886; Chrna2.
DR VEuPathDB; HostDB:ENSMUSG00000022041; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000158299; -.
DR HOGENOM; CLU_018074_1_0_1; -.
DR InParanoid; Q91X60; -.
DR OMA; QHAKNKD; -.
DR OrthoDB; 381858at2759; -.
DR PhylomeDB; Q91X60; -.
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; 110902; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q91X60; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q91X60; protein.
DR Bgee; ENSMUSG00000022041; Expressed in retinal neural layer and 32 other tissues.
DR Genevisible; Q91X60; 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:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; 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:0015464; F:acetylcholine receptor activity; ISO:MGI.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; ISO: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:0050997; F:quaternary ammonium group binding; ISO:MGI.
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; ISO:MGI.
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:1905144; P:response to acetylcholine; ISO:MGI.
DR GO; GO:0035094; P:response to nicotine; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
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 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..512
FT /note="Neuronal acetylcholine receptor subunit alpha-2"
FT /id="PRO_0000000341"
FT TOPO_DOM 28..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..174
FT /evidence="ECO:0000250"
FT DISULFID 224..225
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 512 AA; 58735 MW; AC0C6CC398B69C6C CRC64;
MAPSHPAFQF WIHLYLWCLL LMPAVLAQQG SHTHAEDRLF KHLFGGYNRW ARPVPNTSDV
VIVRFGLSIA QLIDVDEKNQ MMTTNVWLKQ EWNDYKLRWD PAEFGNITSL RVPSEMIWIP
DIVLYNNADG EFAVTHMTKA HLFFTGTVHW VPPAIYKSSC SIDVTFFPFD QQNCKMKFGS
WTYDKAKIDL EQMERTVDLK DYWESGEWAI INATGTYNSK KYDCCAEIYP DVTYYFVIRR
LPLFYTINLI IPCLLISCLT VLVFYLPSEC GEKITLCISV LLSLTVFLLL ITEIIPSTSL
VIPLIGEYLL FTMIFVTLSI VITVFVLNVH HRSPSTHNMP NWVRVALLGR VPRWLMMNRP
LPPMELHGSP GLKLSPTYHW LETNMDAEER EETEEEEEEE EDENICMCAG LPDSSMGVLY
GHGSLHLRAM GPEAKTPSQA SEILLSPQIQ KALEGVHYIA DHLRSEDADS SVKEDWKYVA
MVVDRIFLWL FIIVCFLGTI GLFLPPFLAG MI
