ACHA7_MOUSE
ID ACHA7_MOUSE Reviewed; 502 AA.
AC P49582;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-7;
DE Flags: Precursor;
GN Name=Chrna7; Synonyms=Acra7;
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;
RX PubMed=7601470; DOI=10.1016/0888-7543(95)80228-e;
RA Orr-Urtreger A., Seldin M.F., Baldini A., Beaudet A.L.;
RT "Cloning and mapping of the mouse alpha 7-neuronal nicotinic acetylcholine
RT receptor.";
RL Genomics 26:399-402(1995).
RN [2]
RP SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-46; ASN-90 AND ASN-133,
RP MUTAGENESIS OF ASN-46; ASN-90 AND ASN-133, AND REGION.
RX PubMed=32783947; DOI=10.1016/j.celrep.2020.108025;
RA Kweon H.J., Gu S., Witham E., Dhara M., Yu H., Mandon E.D., Jawhari A.,
RA Bredt D.S.;
RT "NACHO Engages N-Glycosylation ER Chaperone Pathways for alpha7 Nicotinic
RT Receptor Assembly.";
RL Cell Rep. 32:108025-108025(2020).
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. The
CC channel is blocked by alpha-bungarotoxin.
CC -!- SUBUNIT: Homopentamer (PubMed:32783947). Interacts with RIC3; which is
CC required for proper folding and assembly. Interacts with LYPD6.
CC Interacts with the alpha-conotoxin RgIA (By similarity). Interacts with
CC alpha-conotoxins ImI and ImII (By similarity). Interacts with CANX (By
CC similarity). {ECO:0000250|UniProtKB:P36544,
CC ECO:0000250|UniProtKB:P54131, ECO:0000250|UniProtKB:Q05941,
CC ECO:0000269|PubMed:32783947}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:32783947};
CC Multi-pass membrane protein {ECO:0000255}. Note=TMEM35A/NACHO promotes
CC its trafficking to the cell membrane (PubMed:32783947). RIC3 promotes
CC its trafficking to the cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q05941, ECO:0000269|PubMed:32783947}.
CC -!- PTM: Glycosylations at Asn-46, Asn-90 and Asn-133 are essential for
CC TMEM35A/NACHO-mediated proper subunit assembly and trafficking to the
CC cell membrane. {ECO:0000269|PubMed:32783947}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-7/CHRNA7 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; L37663; AAC42053.1; -; mRNA.
DR CCDS; CCDS21329.1; -.
DR PIR; A57175; A57175.
DR RefSeq; NP_031416.3; NM_007390.3.
DR AlphaFoldDB; P49582; -.
DR SMR; P49582; -.
DR BioGRID; 197934; 2.
DR ComplexPortal; CPX-234; Neuronal nicotinic acetylcholine receptor complex, alpha7.
DR ComplexPortal; CPX-238; Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2.
DR DIP; DIP-48732N; -.
DR IntAct; P49582; 4.
DR STRING; 10090.ENSMUSP00000032738; -.
DR BindingDB; P49582; -.
DR ChEMBL; CHEMBL3365; -.
DR DrugCentral; P49582; -.
DR GlyGen; P49582; 3 sites.
DR iPTMnet; P49582; -.
DR PhosphoSitePlus; P49582; -.
DR PaxDb; P49582; -.
DR PRIDE; P49582; -.
DR ProteomicsDB; 286067; -.
DR DNASU; 11441; -.
DR Ensembl; ENSMUST00000032738; ENSMUSP00000032738; ENSMUSG00000030525.
DR GeneID; 11441; -.
DR KEGG; mmu:11441; -.
DR UCSC; uc009vel.1; mouse.
DR CTD; 1139; -.
DR MGI; MGI:99779; Chrna7.
DR VEuPathDB; HostDB:ENSMUSG00000030525; -.
DR eggNOG; KOG3646; Eukaryota.
DR GeneTree; ENSGT00940000154617; -.
DR HOGENOM; CLU_018074_0_3_1; -.
DR InParanoid; P49582; -.
DR OMA; WDLMGIP; -.
DR OrthoDB; 845098at2759; -.
DR PhylomeDB; P49582; -.
DR TreeFam; TF315605; -.
DR Reactome; R-MMU-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR BioGRID-ORCS; 11441; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Chrna7; mouse.
DR PRO; PR:P49582; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P49582; protein.
DR Bgee; ENSMUSG00000030525; Expressed in cerebral cortex marginal layer and 57 other tissues.
DR ExpressionAtlas; P49582; baseline and differential.
DR Genevisible; P49582; MM.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IPI:ComplexPortal.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0032279; C:asymmetric synapse; ISO:MGI.
DR GO; GO:0030673; C:axolemma; IDA:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0098690; C:glycinergic synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0099065; C:integral component of spine apparatus membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; 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: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:0098793; C:presynapse; TAS:ARUK-UCL.
DR GO; GO:0042734; C:presynaptic membrane; 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; IDA:MGI.
DR GO; GO:0008179; F:adenylate cyclase binding; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0017081; F:chloride channel regulator activity; ISO:MGI.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0005216; F:ion channel activity; ISO:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0015643; F:toxic substance binding; ISO:MGI.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; ISO:MGI.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISO:MGI.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0042113; P:B cell activation; IMP:MGI.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:MGI.
DR GO; GO:0035095; P:behavioral response to nicotine; IGI:MGI.
DR GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0140059; P:dendrite arborization; IMP:ARUK-UCL.
DR GO; GO:0097061; P:dendritic spine organization; IMP:ARUK-UCL.
DR GO; GO:0006897; P:endocytosis; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0060112; P:generation of ovulation cycle rhythm; IMP:MGI.
DR GO; GO:0034220; P:ion transmembrane transport; ISO:MGI.
DR GO; GO:0006811; P:ion transport; IMP:MGI.
DR GO; GO:0007611; P:learning or memory; IGI:ARUK-UCL.
DR GO; GO:0051899; P:membrane depolarization; IDA:ComplexPortal.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IGI:ARUK-UCL.
DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IDA:ARUK-UCL.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IMP:MGI.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:ARUK-UCL.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:MGI.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; ISO:MGI.
DR GO; GO:0042698; P:ovulation cycle; IMP:MGI.
DR GO; GO:1905923; P:positive regulation of acetylcholine biosynthetic process; IC:ARUK-UCL.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IGI:ARUK-UCL.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IGI:ARUK-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:ARUK-UCL.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IGI:ARUK-UCL.
DR GO; GO:0001988; P:positive regulation of heart rate involved in baroreceptor response to decreased systemic arterial blood pressure; IMP:MGI.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IDA:ARUK-UCL.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IGI:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:ARUK-UCL.
DR GO; GO:1905906; P:regulation of amyloid fibril formation; IGI:ARUK-UCL.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR GO; GO:1901214; P:regulation of neuron death; IGI:ARUK-UCL.
DR GO; GO:0014061; P:regulation of norepinephrine secretion; IMP:MGI.
DR GO; GO:2001023; P:regulation of response to drug; ISO:MGI.
DR GO; GO:0051823; P:regulation of synapse structural plasticity; IC:ARUK-UCL.
DR GO; GO:0032222; P:regulation of synaptic transmission, cholinergic; IC:ARUK-UCL.
DR GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; 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:1904645; P:response to amyloid-beta; IMP:ARUK-UCL.
DR GO; GO:0009409; P:response to cold; IDA:ARUK-UCL.
DR GO; GO:0045471; P:response to ethanol; IMP:MGI.
DR GO; GO:0032094; P:response to food; IMP:MGI.
DR GO; GO:0035094; P:response to nicotine; IMP:MGI.
DR GO; GO:0050893; P:sensory processing; IDA:ARUK-UCL.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0050808; P:synapse organization; IGI:ARUK-UCL.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:MGI.
DR GO; GO:0042110; P:T cell activation; 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 1: Evidence at protein 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..22
FT /evidence="ECO:0000250"
FT CHAIN 23..502
FT /note="Neuronal acetylcholine receptor subunit alpha-7"
FT /id="PRO_0000000368"
FT TOPO_DOM 23..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 260..267
FT /note="Essential for TMEM35A/NACHO-mediated proper subunit
FT assembly and trafficking to cell membrane"
FT /evidence="ECO:0000269|PubMed:32783947"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:32783947"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:32783947"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:32783947"
FT DISULFID 150..164
FT /evidence="ECO:0000250"
FT DISULFID 212..213
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
FT MUTAGEN 46
FT /note="N->A: Impairs TMEM35A/NACHO-mediated proper subunit
FT assembly and trafficking to cell membrane."
FT /evidence="ECO:0000269|PubMed:32783947"
FT MUTAGEN 90
FT /note="N->A: Impairs TMEM35A/NACHO-mediated proper subunit
FT assembly and trafficking to cell membrane."
FT /evidence="ECO:0000269|PubMed:32783947"
FT MUTAGEN 133
FT /note="N->A: Impairs TMEM35A/NACHO-mediated proper subunit
FT assembly and trafficking to cell membrane."
FT /evidence="ECO:0000269|PubMed:32783947"
SQ SEQUENCE 502 AA; 56632 MW; C9312E5226D120E3 CRC64;
MCGRRGGIWL ALAAALLHVS LQGEFQRRLY KELVKNYNPL ERPVANDSQP LTVYFSLSLL
QIMDVDEKNQ VLTTNIWLQM SWTDHYLQWN MSEYPGVKNV RFPDGQIWKP DILLYNSADE
RFDATFHTNV LVNASGHCQY LPPGIFKSSC YIDVRWFPFD VQQCKLKFGS WSYGGWSLDL
QMQEADISSY IPNGEWDLMG IPGKRNEKFY ECCKEPYPDV TYTVTMRRRT LYYGLNLLIP
CVLISALALL VFLLPADSGE KISLGITVLL SLTVFMLLVA EIMPATSDSV PLIAQYFAST
MIIVGLSVVV TVIVLRYHHH DPDGGKMPKW TRIILLNWCA WFLRMKRPGE DKVRPACQHK
PRRCSLASVE LSAGAGPPTS NGNLLYIGFR GLEGMHCAPT PDSGVVCGRL ACSPTHDEHL
MHGTHPSDGD PDLAKILEEV RYIANRFRCQ DESEVICSEW KFAACVVDRL CLMAFSVFTI
ICTIGILMSA PNFVEAVSKD FA
