ACHA5_MOUSE
ID ACHA5_MOUSE Reviewed; 467 AA.
AC Q2MKA5; Q6PW45;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-5;
DE Flags: Precursor;
GN Name=Chrna5;
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 2).
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 [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA VanEngelenburg S., Stitzel J.A.;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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). Interacts with LYPD6.
CC {ECO:0000250|UniProtKB:P30532}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2MKA5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2MKA5-2; Sequence=VSP_028132;
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-5/CHRNA5 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; AY574264; AAS90360.1; -; mRNA.
DR EMBL; DQ318788; ABC49856.1; -; mRNA.
DR EMBL; BC106853; AAI06854.1; -; mRNA.
DR CCDS; CCDS52800.1; -. [Q2MKA5-2]
DR RefSeq; NP_789814.2; NM_176844.4. [Q2MKA5-2]
DR RefSeq; XP_006510836.1; XM_006510773.3.
DR AlphaFoldDB; Q2MKA5; -.
DR SMR; Q2MKA5; -.
DR BioGRID; 225945; 2.
DR ComplexPortal; CPX-188; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2.
DR ComplexPortal; CPX-209; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4.
DR ComplexPortal; CPX-216; Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2.
DR STRING; 10090.ENSMUSP00000091365; -.
DR ChEMBL; CHEMBL3350222; -.
DR GlyGen; Q2MKA5; 3 sites.
DR iPTMnet; Q2MKA5; -.
DR PhosphoSitePlus; Q2MKA5; -.
DR PaxDb; Q2MKA5; -.
DR PRIDE; Q2MKA5; -.
DR Antibodypedia; 15098; 336 antibodies from 36 providers.
DR DNASU; 110835; -.
DR Ensembl; ENSMUST00000093844; ENSMUSP00000091365; ENSMUSG00000035594. [Q2MKA5-2]
DR Ensembl; ENSMUST00000213960; ENSMUSP00000150942; ENSMUSG00000035594. [Q2MKA5-1]
DR GeneID; 110835; -.
DR KEGG; mmu:110835; -.
DR UCSC; uc009prv.2; mouse. [Q2MKA5-2]
DR UCSC; uc009prw.2; mouse. [Q2MKA5-1]
DR CTD; 1138; -.
DR MGI; MGI:87889; Chrna5.
DR VEuPathDB; HostDB:ENSMUSG00000035594; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000159270; -.
DR HOGENOM; CLU_018074_1_2_1; -.
DR InParanoid; Q2MKA5; -.
DR OMA; KWANIII; -.
DR OrthoDB; 381858at2759; -.
DR PhylomeDB; Q2MKA5; -.
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; 110835; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q2MKA5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q2MKA5; protein.
DR Bgee; ENSMUSG00000035594; Expressed in spermatid and 44 other tissues.
DR ExpressionAtlas; Q2MKA5; baseline and differential.
DR Genevisible; Q2MKA5; MM.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IPI:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
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:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
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; ISO:MGI.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0035095; P:behavioral response to nicotine; ISO:MGI.
DR GO; GO:0071316; P:cellular response to nicotine; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISO:MGI.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051899; P:membrane depolarization; IDA: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:0098908; P:regulation of neuronal action potential; ISO:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0035094; P:response to nicotine; IMP:MGI.
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; 2.
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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..467
FT /note="Neuronal acetylcholine receptor subunit alpha-5"
FT /id="PRO_0000304938"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..467
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 170..184
FT /evidence="ECO:0000250"
FT DISULFID 234..235
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..35
FT /note="MAARGSRRRALRLLLMVQLLAGRWRPAGAARGARG -> MQISNA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_028132"
SQ SEQUENCE 467 AA; 53448 MW; 8F5BBA03D6191BA8 CRC64;
MAARGSRRRA LRLLLMVQLL AGRWRPAGAA RGARGGLPEL SSAAKHEDSL FRDLFEDYEK
WVRPVEHLSD KIKIKFGLAI SQLVDVDEKN QLMTTNVWLK QEWIDVKLRW NPDDYGGIKI
IRVPSDSLWI PDIVLFDNAD GRFEGASTKT VVRYNGTVTW TQPANYKSSC TIDVTFFPFD
LQNCSMKFGS WTYDGSQVDI ILEDQDVDRT DFFDNGEWEI MSAMGSKGNR TDSCCWYPCI
TYSFVIKRLP LFYTLFLIIP CIGLSFLTVV VFYLPSNEGE KISLCTSVLV SLTVFLLVIE
EIIPSSSKVI PLIGEYLVFT MIFVTLSIMV TVFAINIHHR SSSTHNAMAP WVRKIFLHKL
PKLLCMRSHA DRYFTQREEA EKDGGPKSRN TLEAALDCIR YITRHVVKEN DVREVVEDWK
FIAQVLDRMF LWTFLLVSII GTLGLFVPVI YKWANIIVPV HIGNTIK
