ACHA7_RAT
ID ACHA7_RAT Reviewed; 502 AA.
AC Q05941; Q53YK2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-7;
DE Flags: Precursor;
GN Name=Chrna7; Synonyms=Acra7;
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].
RC TISSUE=Brain;
RX PubMed=7678857; DOI=10.1523/jneurosci.13-02-00596.1993;
RA Seguela P., Wadiche J., Dineley-Miller K., Dani J.A., Patrick J.W.;
RT "Molecular cloning, functional properties, and distribution of rat brain
RT alpha 7: a nicotinic cation channel highly permeable to calcium.";
RL J. Neurosci. 13:596-604(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Boulter J.;
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE REVISION TO 363.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Hartley M.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Groot-Kormelink P.J.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH RIC3, MUTAGENESIS OF LEU-433; LYS-435; VAL-440; ASN-445;
RP ARG-446; PHE-447 AND ARG-448, AND SUBCELLULAR LOCATION.
RX PubMed=15927954; DOI=10.1074/jbc.m503746200;
RA Castillo M., Mulet J., Gutierrez L.M., Ortiz J.A., Castelan F., Gerber S.,
RA Sala S., Sala F., Criado M.;
RT "Dual role of the RIC-3 protein in trafficking of serotonin and nicotinic
RT acetylcholine receptors.";
RL J. Biol. Chem. 280:27062-27068(2005).
RN [6]
RP INTERACTION WITH RIC3.
RX PubMed=16120769; DOI=10.1124/mol.105.017459;
RA Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R., Gibb A.J.,
RA Millar N.S.;
RT "RIC-3 enhances functional expression of multiple nicotinic acetylcholine
RT receptor subtypes in mammalian cells.";
RL Mol. Pharmacol. 68:1431-1438(2005).
RN [7]
RP MUTAGENESIS OF SER-81 AND LEU-141, AND SUBUNIT.
RX PubMed=25740413; DOI=10.1124/mol.114.096511;
RA Azam L., Papakyriakou A., Zouridakis M., Giastas P., Tzartos S.J.,
RA McIntosh J.M.;
RT "Molecular interaction of alpha-conotoxin RgIA with the rat alpha9alpha10
RT nicotinic acetylcholine receptor.";
RL Mol. Pharmacol. 87:855-864(2015).
RN [8]
RP ERRATUM OF PUBMED:25740413.
RX PubMed=27559150; DOI=10.1124/mol.114.096511err;
RA Azam L., Papakyriakou A., Zouridakis M., Giastas P., Tzartos S.J.,
RA McIntosh J.M.;
RT "Corrections to 'Molecular interaction of alpha-conotoxin RgIA with the rat
RT alpha9alpha10 nicotinic acetylcholine receptor'.";
RL Mol. Pharmacol. 90:415-417(2016).
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 (By similarity). Interacts with RIC3; which is
CC required for proper folding and assembly (PubMed:15927954,
CC PubMed:16120769). Interacts with LYPD6 (By similarity). Interacts with
CC the alpha-conotoxin RgIA (PubMed:25740413). Interacts with alpha-
CC conotoxins ImI and ImII (By similarity). Interacts with CANX (By
CC similarity). {ECO:0000250|UniProtKB:P36544,
CC ECO:0000250|UniProtKB:P54131, ECO:0000269|PubMed:15927954,
CC ECO:0000269|PubMed:16120769, ECO:0000269|PubMed:25740413}.
CC -!- INTERACTION:
CC Q05941; PRO_0000000092 [P05067]: APP; Xeno; NbExp=3; IntAct=EBI-79422, EBI-821758;
CC Q05941; Q7Z2K8: GPRIN1; Xeno; NbExp=6; IntAct=EBI-79422, EBI-11152848;
CC Q05941; P60615; Xeno; NbExp=4; IntAct=EBI-79422, EBI-7516391;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:15927954};
CC Multi-pass membrane protein {ECO:0000255}. Note=RIC3 promotes its
CC trafficking to the cell membrane (PubMed:15927954). TMEM35A/NACHO
CC promotes its trafficking to the cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:P49582, ECO:0000269|PubMed:15927954}.
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:0000250|UniProtKB:P49582}.
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; S53987; AAB25224.2; -; mRNA.
DR EMBL; L31619; AAC33136.1; -; mRNA.
DR EMBL; AY574256; AAS90352.1; -; mRNA.
DR PIR; T01378; T01378.
DR RefSeq; NP_036964.3; NM_012832.3.
DR AlphaFoldDB; Q05941; -.
DR SMR; Q05941; -.
DR ComplexPortal; CPX-233; Neuronal nicotinic acetylcholine receptor complex, alpha7.
DR ComplexPortal; CPX-237; Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2.
DR IntAct; Q05941; 5.
DR MINT; Q05941; -.
DR STRING; 10116.ENSRNOP00000045255; -.
DR BindingDB; Q05941; -.
DR ChEMBL; CHEMBL4980; -.
DR DrugCentral; Q05941; -.
DR GuidetoPHARMACOLOGY; 468; -.
DR GlyGen; Q05941; 3 sites.
DR iPTMnet; Q05941; -.
DR PhosphoSitePlus; Q05941; -.
DR SwissPalm; Q05941; -.
DR PaxDb; Q05941; -.
DR Ensembl; ENSRNOT00000082487; ENSRNOP00000073551; ENSRNOG00000010853.
DR GeneID; 25302; -.
DR KEGG; rno:25302; -.
DR UCSC; RGD:2348; rat.
DR CTD; 1139; -.
DR RGD; 2348; Chrna7.
DR eggNOG; KOG3646; Eukaryota.
DR GeneTree; ENSGT00940000154617; -.
DR InParanoid; Q05941; -.
DR PhylomeDB; Q05941; -.
DR Reactome; R-RNO-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR PRO; PR:Q05941; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:ARUK-UCL.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
DR GO; GO:0030673; C:axolemma; ISO:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0098690; C:glycinergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
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; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; 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:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0044853; C:plasma membrane raft; IDA:ARUK-UCL.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0042734; C:presynaptic membrane; 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; ISO:RGD.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:ARUK-UCL.
DR GO; GO:0008179; F:adenylate cyclase binding; IPI:RGD.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; IDA:RGD.
DR GO; GO:0017081; F:chloride channel regulator activity; ISO:RGD.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0005216; F:ion channel activity; ISO:RGD.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0097110; F:scaffold protein binding; IDA:RGD.
DR GO; GO:0015643; F:toxic substance binding; ISO:RGD.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IDA:ARUK-UCL.
DR GO; GO:0008306; P:associative learning; ISO:RGD.
DR GO; GO:0042113; P:B cell activation; ISO:RGD.
DR GO; GO:0048149; P:behavioral response to ethanol; ISO:RGD.
DR GO; GO:0035095; P:behavioral response to nicotine; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050890; P:cognition; ISO:RGD.
DR GO; GO:0140059; P:dendrite arborization; ISO:RGD.
DR GO; GO:0097061; P:dendritic spine organization; ISO:RGD.
DR GO; GO:0042416; P:dopamine biosynthetic process; IEP:RGD.
DR GO; GO:0006897; P:endocytosis; ISO:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
DR GO; GO:0060112; P:generation of ovulation cycle rhythm; ISO:RGD.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:RGD.
DR GO; GO:0006811; P:ion transport; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0051899; P:membrane depolarization; IDA:ComplexPortal.
DR GO; GO:0007613; P:memory; IDA:ARUK-UCL.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISO:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISO:RGD.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; IMP:RGD.
DR GO; GO:0042698; P:ovulation cycle; ISO:RGD.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0001988; P:positive regulation of heart rate involved in baroreceptor response to decreased systemic arterial blood pressure; ISO:RGD.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:1905906; P:regulation of amyloid fibril formation; ISO:RGD.
DR GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; ISO:RGD.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR GO; GO:1901214; P:regulation of neuron death; ISO:RGD.
DR GO; GO:0014061; P:regulation of norepinephrine secretion; ISO:RGD.
DR GO; GO:2001023; P:regulation of response to drug; IDA:RGD.
DR GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:1905144; P:response to acetylcholine; IDA:ARUK-UCL.
DR GO; GO:1904645; P:response to amyloid-beta; ISO:RGD.
DR GO; GO:0009409; P:response to cold; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; ISO:RGD.
DR GO; GO:0032094; P:response to food; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0035094; P:response to nicotine; IDA:RGD.
DR GO; GO:0050893; P:sensory processing; IDA:ARUK-UCL.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:RGD.
DR GO; GO:0042110; P:T cell activation; 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; 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_0000000369"
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:0000250|UniProtKB:P49582"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 150..164
FT /evidence="ECO:0000250"
FT DISULFID 212..213
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
FT MUTAGEN 81
FT /note="S->T: 10-fold more potently inhibited by the alpha-
FT conotoxin RgIA."
FT /evidence="ECO:0000269|PubMed:25740413"
FT MUTAGEN 141
FT /note="L->D: No change in inhibition by the alpha-conotoxin
FT RgIA."
FT /evidence="ECO:0000269|PubMed:25740413"
FT MUTAGEN 433
FT /note="L->A: Abolishes dependency on RIC3 for functional
FT expression."
FT /evidence="ECO:0000269|PubMed:15927954"
FT MUTAGEN 435
FT /note="K->A: No effect on dependency on RIC3 for functional
FT expression."
FT /evidence="ECO:0000269|PubMed:15927954"
FT MUTAGEN 440
FT /note="V->A: Impairs dependency on RIC3 for functional
FT expression."
FT /evidence="ECO:0000269|PubMed:15927954"
FT MUTAGEN 445
FT /note="N->A: Slightly impairs dependency on RIC3 for
FT functional expression."
FT /evidence="ECO:0000269|PubMed:15927954"
FT MUTAGEN 446
FT /note="R->A: Impairs dependency on RIC3 for functional
FT expression."
FT /evidence="ECO:0000269|PubMed:15927954"
FT MUTAGEN 447
FT /note="F->A: Impairs dependency on RIC3 for functional
FT expression."
FT /evidence="ECO:0000269|PubMed:15927954"
FT MUTAGEN 448
FT /note="R->A: Impairs dependency on RIC3 for functional
FT expression."
FT /evidence="ECO:0000269|PubMed:15927954"
FT CONFLICT 447
FT /note="F -> N (in Ref. 1; AAB25224)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="R -> P (in Ref. 1; AAB25224)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 56503 MW; 289A30498C7B9A58 CRC64;
MCGGRGGIWL 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
MHGAHPSDGD PDLAKILEEV RYIANRFRCQ DESEVICSEW KFAACVVDRL CLMAFSVFTI
ICTIGILMSA PNFVEAVSKD FA
