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   24-JAN-2024, entry version 132.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyCosmos; Q2MKA5; 3 sites, No reported glycans.
DR   GlyGen; Q2MKA5; 3 sites.
DR   iPTMnet; Q2MKA5; -.
DR   PhosphoSitePlus; Q2MKA5; -.
DR   PaxDb; 10090-ENSMUSP00000091365; -.
DR   Antibodypedia; 15098; 366 antibodies from 36 providers.
DR   DNASU; 110835; -.
DR   Ensembl; ENSMUST00000093844.5; ENSMUSP00000091365.4; ENSMUSG00000035594.11. [Q2MKA5-2]
DR   Ensembl; ENSMUST00000213960.2; ENSMUSP00000150942.2; ENSMUSG00000035594.11. [Q2MKA5-1]
DR   GeneID; 110835; -.
DR   KEGG; mmu:110835; -.
DR   UCSC; uc009prv.2; mouse. [Q2MKA5-2]
DR   UCSC; uc009prw.2; mouse. [Q2MKA5-1]
DR   AGR; MGI:87889; -.
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; SCCWYPH; -.
DR   OrthoDB; 5489962at2759; -.
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 78 CRISPR screens.
DR   PRO; PR:Q2MKA5; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q2MKA5; Protein.
DR   Bgee; ENSMUSG00000035594; Expressed in spermatid and 46 other cell types or tissues.
DR   ExpressionAtlas; Q2MKA5; baseline and differential.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; IPI:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0098691; C:dopaminergic synapse; IDA:SynGO.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
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 monoatomic cation-selective channel activity; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISO:MGI.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:0098908; P:regulation of neuronal action potential; ISO:MGI.
DR   GO; GO:0035094; P:response to nicotine; IMP:MGI.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
DR   CDD; cd19064; LGIC_TM_nAChR; 1.
DR   Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR   Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 2.
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   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945:SF76; NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-5; 1.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 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; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR   SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
DR   Genevisible; Q2MKA5; MM.
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
//