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Neuronal acetylcholine receptor subunit alpha-7

 ACHA7_RAT               Reviewed;         502 AA.
Q05941; Q53YK2;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 2.
28-FEB-2018, entry version 149.
RecName: Full=Neuronal acetylcholine receptor subunit alpha-7;
Flags: Precursor;
Name=Chrna7; Synonyms=Acra7;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7678857;
Seguela P., Wadiche J., Dineley-Miller K., Dani J.A., Patrick J.W.;
"Molecular cloning, functional properties, and distribution of rat
brain alpha 7: a nicotinic cation channel highly permeable to
calcium.";
J. Neurosci. 13:596-604(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
Boulter J.;
Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
[3]
SEQUENCE REVISION TO 363.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Hartley M.;
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
Groot-Kormelink P.J.;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH RIC3, AND MUTAGENESIS OF LEU-433; LYS-435; VAL-440;
ASN-445; ARG-446; PHE-447 AND ARG-448.
PubMed=15927954; DOI=10.1074/jbc.M503746200;
Castillo M., Mulet J., Gutierrez L.M., Ortiz J.A., Castelan F.,
Gerber S., Sala S., Sala F., Criado M.;
"Dual role of the RIC-3 protein in trafficking of serotonin and
nicotinic acetylcholine receptors.";
J. Biol. Chem. 280:27062-27068(2005).
[6]
INTERACTION WITH RIC3.
PubMed=16120769; DOI=10.1124/mol.105.017459;
Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R.,
Gibb A.J., Millar N.S.;
"RIC-3 enhances functional expression of multiple nicotinic
acetylcholine receptor subtypes in mammalian cells.";
Mol. Pharmacol. 68:1431-1438(2005).
[7]
MUTAGENESIS OF SER-81 AND LEU-141, AND SUBUNIT.
PubMed=25740413; DOI=10.1124/mol.114.096511;
Azam L., Papakyriakou A., Zouridakis M., Giastas P., Tzartos S.J.,
McIntosh J.M.;
"Molecular interaction of alpha-conotoxin RgIA with the rat
alpha9alpha10 nicotinic acetylcholine receptor.";
Mol. Pharmacol. 87:855-864(2015).
[8]
ERRATUM.
PubMed=27559150; DOI=10.1124/mol.114.096511err;
Azam L., Papakyriakou A., Zouridakis M., Giastas P., Tzartos S.J.,
McIntosh J.M.;
"Corrections to 'Molecular interaction of alpha-conotoxin RgIA with
the rat alpha9alpha10 nicotinic acetylcholine receptor'.";
Mol. Pharmacol. 90:415-417(2016).
-!- FUNCTION: After binding acetylcholine, the AChR responds by an
extensive change in conformation that affects all subunits and
leads to opening of an ion-conducting channel across the plasma
membrane. The channel is blocked by alpha-bungarotoxin.
-!- SUBUNIT: Homopentamer (By similarity). Interacts with RIC3; which
is required for proper folding and assembly (PubMed:15927954,
PubMed:16120769). Interacts with LYPD6 (By similarity). Interacts
with the alpha-conotoxin RgIA (PubMed:25740413). Interacts with
alpha-conotoxins ImI and ImII (By similarity).
{ECO:0000250|UniProtKB:P36544, ECO:0000250|UniProtKB:P54131,
ECO:0000269|PubMed:15927954, ECO:0000269|PubMed:16120769,
ECO:0000269|PubMed:25740413}.
-!- INTERACTION:
P60615:- (xeno); NbExp=4; IntAct=EBI-79422, EBI-7516391;
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
membrane protein.
-!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-
7/CHRNA7 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; S53987; AAB25224.2; -; mRNA.
EMBL; L31619; AAC33136.1; -; mRNA.
EMBL; AY574256; AAS90352.1; -; mRNA.
PIR; T01378; T01378.
RefSeq; NP_036964.3; NM_012832.3.
UniGene; Rn.9698; -.
ProteinModelPortal; Q05941; -.
SMR; Q05941; -.
IntAct; Q05941; 3.
STRING; 10116.ENSRNOP00000045255; -.
BindingDB; Q05941; -.
ChEMBL; CHEMBL4980; -.
GuidetoPHARMACOLOGY; 468; -.
iPTMnet; Q05941; -.
PhosphoSitePlus; Q05941; -.
SwissPalm; Q05941; -.
PaxDb; Q05941; -.
GeneID; 25302; -.
KEGG; rno:25302; -.
UCSC; RGD:2348; rat.
CTD; 1139; -.
RGD; 2348; Chrna7.
eggNOG; KOG3645; Eukaryota.
eggNOG; ENOG410XQGR; LUCA.
HOGENOM; HOG000006756; -.
HOVERGEN; HBG003756; -.
InParanoid; Q05941; -.
KO; K04809; -.
OrthoDB; EOG091G0R20; -.
PhylomeDB; Q05941; -.
PRO; PR:Q05941; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:ARUK-UCL.
GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
GO; GO:0030673; C:axolemma; ISO:RGD.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0043198; C:dendritic shaft; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
GO; GO:0030426; C:growth cone; IDA:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0044853; C:plasma membrane raft; IDA:ARUK-UCL.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
GO; GO:0042166; F:acetylcholine binding; IDA:RGD.
GO; GO:0015464; F:acetylcholine receptor activity; ISO:RGD.
GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:ARUK-UCL.
GO; GO:0008179; F:adenylate cyclase binding; IPI:RGD.
GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
GO; GO:0051117; F:ATPase binding; IDA:RGD.
GO; GO:0017081; F:chloride channel regulator activity; ISO:RGD.
GO; GO:0008144; F:drug binding; IDA:RGD.
GO; GO:0005216; F:ion channel activity; ISO:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0097110; F:scaffold protein binding; IDA:RGD.
GO; GO:0015643; F:toxic substance binding; ISO:RGD.
GO; GO:0095500; P:acetylcholine receptor signaling pathway; IDA:ARUK-UCL.
GO; GO:0000187; P:activation of MAPK activity; ISO:RGD.
GO; GO:0008306; P:associative learning; ISO:RGD.
GO; GO:0042113; P:B cell activation; ISO:RGD.
GO; GO:0048149; P:behavioral response to ethanol; ISO:RGD.
GO; GO:0035095; P:behavioral response to nicotine; ISO:RGD.
GO; GO:0006816; P:calcium ion transport; IMP:MGI.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
GO; GO:0050890; P:cognition; ISO:RGD.
GO; GO:0140059; P:dendrite arborization; ISO:RGD.
GO; GO:0097061; P:dendritic spine organization; ISO:RGD.
GO; GO:0042416; P:dopamine biosynthetic process; IEP:RGD.
GO; GO:0006897; P:endocytosis; ISO:RGD.
GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
GO; GO:0060112; P:generation of ovulation cycle rhythm; ISO:RGD.
GO; GO:0034220; P:ion transmembrane transport; ISO:RGD.
GO; GO:0006811; P:ion transport; ISO:RGD.
GO; GO:0007611; P:learning or memory; ISO:RGD.
GO; GO:0007613; P:memory; IDA:ARUK-UCL.
GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
GO; GO:0098815; P:modulation of excitatory postsynaptic potential; ISO:RGD.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISO:RGD.
GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISO:RGD.
GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:RGD.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD.
GO; GO:0019228; P:neuronal action potential; IDA:RGD.
GO; GO:0042698; P:ovulation cycle; ISO:RGD.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:RGD.
GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:RGD.
GO; GO:1905920; P:positive regulation of CoA-transferase activity; ISO:RGD.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:ARUK-UCL.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:RGD.
GO; GO:0001988; P:positive regulation of heart rate involved in baroreceptor response to decreased systemic arterial blood pressure; ISO:RGD.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:RGD.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
GO; GO:1905906; P:regulation of amyloid fibril formation; ISO:RGD.
GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; ISO:RGD.
GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
GO; GO:1901214; P:regulation of neuron death; ISO:RGD.
GO; GO:0014061; P:regulation of norepinephrine secretion; ISO:RGD.
GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; ISO:RGD.
GO; GO:1905144; P:response to acetylcholine; IDA:ARUK-UCL.
GO; GO:1904645; P:response to amyloid-beta; ISO:RGD.
GO; GO:0009409; P:response to cold; ISO:RGD.
GO; GO:0045471; P:response to ethanol; ISO:RGD.
GO; GO:0032094; P:response to food; ISO:RGD.
GO; GO:0001666; P:response to hypoxia; ISO:RGD.
GO; GO:0035094; P:response to nicotine; IGI:ARUK-UCL.
GO; GO:0050893; P:sensory processing; IDA:ARUK-UCL.
GO; GO:0007165; P:signal transduction; ISO:RGD.
GO; GO:0050808; P:synapse organization; ISO:RGD.
GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:RGD.
GO; GO:0042110; P:T cell activation; ISO:RGD.
Gene3D; 2.70.170.10; -; 1.
InterPro; IPR006202; Neur_chan_lig-bd.
InterPro; IPR036734; Neur_chan_lig-bd_sf.
InterPro; IPR006201; Neur_channel.
InterPro; IPR036719; Neuro-gated_channel_TM_sf.
InterPro; IPR006029; Neurotrans-gated_channel_TM.
InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
PANTHER; PTHR18945; PTHR18945; 1.
Pfam; PF02931; Neur_chan_LBD; 1.
Pfam; PF02932; Neur_chan_memb; 1.
PRINTS; PR00254; NICOTINICR.
PRINTS; PR00252; NRIONCHANNEL.
SUPFAM; SSF63712; SSF63712; 1.
SUPFAM; SSF90112; SSF90112; 1.
TIGRFAMs; TIGR00860; LIC; 1.
PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
Membrane; Postsynaptic cell membrane; Receptor; Reference proteome;
Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 22 {ECO:0000250}.
CHAIN 23 502 Neuronal acetylcholine receptor subunit
alpha-7.
/FTId=PRO_0000000369.
TOPO_DOM 23 230 Extracellular. {ECO:0000255}.
TRANSMEM 231 255 Helical. {ECO:0000255}.
TRANSMEM 262 280 Helical. {ECO:0000255}.
TRANSMEM 296 317 Helical. {ECO:0000255}.
TOPO_DOM 318 469 Cytoplasmic. {ECO:0000255}.
TRANSMEM 470 490 Helical. {ECO:0000255}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 150 164 {ECO:0000250}.
DISULFID 212 213 Associated with receptor activation.
{ECO:0000250}.
MUTAGEN 81 81 S->T: 10-fold more potently inhibited by
the alpha-conotoxin RgIA.
{ECO:0000269|PubMed:25740413}.
MUTAGEN 141 141 L->D: No change in inhibition by the
alpha-conotoxin RgIA.
{ECO:0000269|PubMed:25740413}.
MUTAGEN 433 433 L->A: Abolishes dependency on RIC3 for
functional expression.
{ECO:0000269|PubMed:15927954}.
MUTAGEN 435 435 K->A: No effect on dependency on RIC3 for
functional expression.
{ECO:0000269|PubMed:15927954}.
MUTAGEN 440 440 V->A: Impairs dependency on RIC3 for
functional expression.
{ECO:0000269|PubMed:15927954}.
MUTAGEN 445 445 N->A: Slightly impairs dependency on RIC3
for functional expression.
{ECO:0000269|PubMed:15927954}.
MUTAGEN 446 446 R->A: Impairs dependency on RIC3 for
functional expression.
{ECO:0000269|PubMed:15927954}.
MUTAGEN 447 447 F->A: Impairs dependency on RIC3 for
functional expression.
{ECO:0000269|PubMed:15927954}.
MUTAGEN 448 448 R->A: Impairs dependency on RIC3 for
functional expression.
{ECO:0000269|PubMed:15927954}.
CONFLICT 447 447 F -> N (in Ref. 1; AAB25224).
{ECO:0000305}.
CONFLICT 469 469 R -> P (in Ref. 1; AAB25224).
{ECO:0000305}.
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


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