ACHA7_MACMU
ID ACHA7_MACMU Reviewed; 502 AA.
AC Q866A2;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-7;
DE Flags: Precursor;
GN Name=CHRNA7;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14764638; DOI=10.1210/en.2003-1728;
RA Proskocil B.J., Sekhon H.S., Jia Y., Savchenko V., Blakely R.D.,
RA Lindstrom J., Spindel E.R.;
RT "Acetylcholine is an autocrine or paracrine hormone synthesized and
RT secreted by airway bronchial epithelial cells.";
RL Endocrinology 145:2498-2506(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. The
CC channel is blocked by alpha-bungarotoxin (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homopentamer. Interacts with RIC3; which is required for
CC proper folding and assembly. Interacts with LYPD6. Interacts with the
CC alpha-conotoxin RgIA. Interacts with alpha-conotoxins ImI and ImII (By
CC similarity). Interacts with CANX (By similarity).
CC {ECO:0000250|UniProtKB:P36544, ECO:0000250|UniProtKB:P54131,
CC ECO:0000250|UniProtKB:Q05941}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:P49582}; Multi-pass membrane protein
CC {ECO:0000255}. Note=TMEM35A/NACHO and RIC3 promote its trafficking to
CC the cell membrane. {ECO:0000250|UniProtKB:P49582,
CC ECO:0000250|UniProtKB:Q05941}.
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; AF486623; AAO84497.1; -; mRNA.
DR RefSeq; NP_001028055.1; NM_001032883.1.
DR AlphaFoldDB; Q866A2; -.
DR SMR; Q866A2; -.
DR STRING; 9544.ENSMMUP00000029721; -.
DR BindingDB; Q866A2; -.
DR ChEMBL; CHEMBL2150833; -.
DR Ensembl; ENSMMUT00000031766; ENSMMUP00000029721; ENSMMUG00000022577.
DR GeneID; 574230; -.
DR KEGG; mcc:574230; -.
DR CTD; 1139; -.
DR VEuPathDB; HostDB:ENSMMUG00000022577; -.
DR VGNC; VGNC:109119; CHRNA7.
DR eggNOG; KOG3646; Eukaryota.
DR GeneTree; ENSGT00940000154617; -.
DR HOGENOM; CLU_018074_0_3_1; -.
DR InParanoid; Q866A2; -.
DR OMA; WDLMGIP; -.
DR OrthoDB; 845098at2759; -.
DR TreeFam; TF315605; -.
DR PRO; PR:Q866A2; -.
DR Proteomes; UP000006718; Chromosome 7.
DR Bgee; ENSMMUG00000022577; Expressed in dorsolateral prefrontal cortex and 17 other tissues.
DR ExpressionAtlas; Q866A2; baseline.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; ISS:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0042166; F:acetylcholine binding; ISS:UniProtKB.
DR GO; GO:0015464; F:acetylcholine receptor activity; ISS:UniProtKB.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; ISS:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; ISS:UniProtKB.
DR GO; GO:0017081; F:chloride channel regulator activity; ISS:UniProtKB.
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:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0015643; F:toxic substance binding; ISS:UniProtKB.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050890; P:cognition; ISS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IEA:Ensembl.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:1905144; P:response to acetylcholine; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0035094; P:response to nicotine; ISS:UniProtKB.
DR GO; GO:0007614; P:short-term memory; IDA:ARUK-UCL.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
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; 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 2: Evidence at transcript 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_0000000367"
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"
SQ SEQUENCE 502 AA; 56429 MW; 213C8A282242AC4A CRC64;
MRCSQGGVWL ALAASLLHVS LQGEFQRKLY KELVKNYNPL ERPVANDSQP LTVYFSLSLL
QIMDVDEKNQ VLTTNIWLQM SWTDHYLQWN VSEYPGVKTV RFPDGQIWKP DILLYNSADE
RFDATFHTNV LVNSSGHCQY LPPGIFKSSC YIDVRWFPFD VQHCKLKFGS WSYGGWSLDL
QMQEADISGY IPSGEWDLVG IPGKRSEKFY ECCKEPYPDV TFTVTMRRRT LYYGLNLLIP
CVLISALALL VFLLPADSGE KISLGITVLL SLTVFMLLVA EIMPATSDSV PLIAQYFAST
MIIVGLSVVV TVIVLQYHHH DPDGGKMPKW TRVILLNWCA WFLRMKRPGE DKVRPACQHK
QRRCSLASVE MSAVAPPPAS NGNLLYIGFR GLDGMHCAPT PDSGVVCGRM ACSPTHDEHL
LHGGQPPEGD PDLAKILEEV RYIANRFRCQ DESEAVCSEW KFAACVVDRL CLMAFSVFTI
ICTIGILMSA PNFVEAVSKD FA
