ACHA7_BOVIN
ID ACHA7_BOVIN Reviewed; 499 AA.
AC P54131;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-7;
DE Flags: Precursor;
GN Name=CHRNA7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND SUBUNIT.
RC TISSUE=Adrenal medulla;
RX PubMed=7620615; DOI=10.1111/j.1460-9568.1995.tb00668.x;
RA Garcia-Guzman M., Sala F., Sala S., Campos-Caro A., Stuehmer W.,
RA Gutierrez L., Criado M.;
RT "Alpha-bungarotoxin-sensitive nicotinic receptors on bovine chromaffin
RT cells: molecular cloning, functional expression and alternative splicing of
RT the alpha 7 subunit.";
RL Eur. J. Neurosci. 7:647-655(1995).
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. Homooligomer of the short form gives rise to
CC unfunctional channels, as does coexpression of both long and short
CC forms of the receptor (PubMed:7620615). Interacts with RIC3; which is
CC required for proper folding and assembly. Interacts with LYPD6 (By
CC similarity). Interacts with the alpha-conotoxin RgIA (By similarity).
CC Interacts with alpha-conotoxins ImI and ImII (By similarity). Interacts
CC with CANX (By similarity). {ECO:0000250|UniProtKB:P36544,
CC ECO:0000250|UniProtKB:Q05941, ECO:0000269|PubMed:7620615}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P49582};
CC Multi-pass membrane protein {ECO:0000255}. Note=TMEM35A/NACHO and RIC3
CC promote its trafficking to the cell membrane.
CC {ECO:0000250|UniProtKB:P49582, ECO:0000250|UniProtKB:Q05941}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P54131-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P54131-2; Sequence=VSP_000075;
CC -!- TISSUE SPECIFICITY: At least in chromaffin cells.
CC -!- PTM: Glycosylations at Asn-43, Asn-87 and Asn-130 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; X93604; CAA63802.1; -; mRNA.
DR RefSeq; NP_776940.1; NM_174515.2. [P54131-1]
DR AlphaFoldDB; P54131; -.
DR SMR; P54131; -.
DR STRING; 9913.ENSBTAP00000020942; -.
DR BindingDB; P54131; -.
DR ChEMBL; CHEMBL5934; -.
DR PaxDb; P54131; -.
DR GeneID; 282178; -.
DR KEGG; bta:282178; -.
DR CTD; 1139; -.
DR eggNOG; KOG3646; Eukaryota.
DR InParanoid; P54131; -.
DR OrthoDB; 845098at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; ISS:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
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: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:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0035094; P:response to nicotine; ISS:UniProtKB.
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 1: Evidence at protein 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..19
FT /evidence="ECO:0000250"
FT CHAIN 20..499
FT /note="Neuronal acetylcholine receptor subunit alpha-7"
FT /id="PRO_0000000365"
FT TOPO_DOM 20..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 257..264
FT /note="Essential for TMEM35A/NACHO-mediated proper subunit
FT assembly and trafficking to cell membrane"
FT /evidence="ECO:0000250|UniProtKB:P49582"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 147..161
FT /evidence="ECO:0000250"
FT DISULFID 209..210
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
FT VAR_SEQ 262..290
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:7620615"
FT /id="VSP_000075"
SQ SEQUENCE 499 AA; 56003 MW; AEE5D0B3820D42D5 CRC64;
MRGSLCLALA ASILHVSLQG EFQRKLYKDL VKNYNPLERP VANDSLPLTV YFSLSLLQIM
DVDEKNQVLT TNIWLQMTWT DHYLQWNASE YPGVKTVRFP DGQIWKPDIL LYNSADERFD
ATFHTNVLVN SSGHCQYLPP GIFKSSCYID VRWFPFDVQQ CKLKFGSWSY GGWSLDLQMQ
EADISGYIPN GEWDLVGVLG KRSEKFYECC KEPYPDVTFT VSIRRRTLYY GLNLLIPCVL
ISALALLVFL LPADSGEKIS LGITVLLSLT VFMLLVAEIM PATSDSVPLI AQYFASTMII
VGLSVVVTVI VLQYHHHDPD GGKMPKWTRV VLLNWCAWFL RMKRPGEDKV RPACQHNERR
CSLASVEMSA VAGPPATNGN LLYIGFRGLD TMHCAPTPDS GVVCGRVACS PTHDEHLLHA
GQPSEGDPDL AKILEEVRYI AHRFRCQDES EAVCSEWKFA ACVVDRLCLM AFSVFTILCT
IGILMSAPNF VEAVSKDFA
