ACHA_NATTE
ID ACHA_NATTE Reviewed; 127 AA.
AC P14144;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Acetylcholine receptor subunit alpha;
DE Flags: Fragment;
GN Name=CHRNA1;
OS Natrix tessellata (Dice snake) (Coronella tessellata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Colubridae; Natricinae; Natrix.
OX NCBI_TaxID=8584;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=2780569; DOI=10.1073/pnas.86.18.7255;
RA Neumann D., Barchan D., Horowitz M., Kochva E., Fuchs S.;
RT "Snake acetylcholine receptor: cloning of the domain containing the four
RT extracellular cysteines of the alpha subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7255-7259(1989).
CC -!- FUNCTION: Upon acetylcholine binding, the AChR responds by an extensive
CC change in conformation that affects all subunits and leads to opening
CC of an ion-conducting channel across the plasma membrane (By
CC similarity). Does not bind alpha-bungarotoxin.
CC {ECO:0000250|UniProtKB:P02708}.
CC -!- SUBUNIT: One of the alpha chains that assemble within the acetylcholine
CC receptor, a pentamer of two alpha chains, a beta, a delta, and a gamma
CC or epsilon chains. {ECO:0000250|UniProtKB:P02708}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P02708}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P02708}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-1/CHRNA1 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; M26389; AAA49387.1; -; Genomic_DNA.
DR EMBL; M30045; AAA60451.1; -; Genomic_DNA.
DR PIR; B41384; B41384.
DR AlphaFoldDB; P14144; -.
DR SMR; P14144; -.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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; IPR018000; Neurotransmitter_ion_chnl_CS.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW Synapse; Transport.
FT CHAIN <1..>127
FT /note="Acetylcholine receptor subunit alpha"
FT /id="PRO_0000076976"
FT TOPO_DOM <1..>127
FT /note="Extracellular"
FT SITE 92
FT /note="Confers toxin resistance"
FT /evidence="ECO:0000255"
FT SITE 94
FT /note="Confers toxin resistance"
FT /evidence="ECO:0000255"
FT SITE 99
FT /note="Confers toxin resistance"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..47
FT /evidence="ECO:0000250"
FT DISULFID 97..98
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
FT CONFLICT 39
FT /note="Y -> H (in Ref. 1; AAA60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="R -> W (in Ref. 1; AAA60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="T -> N (in Ref. 1; AAA60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="A -> D (in Ref. 1; AAA60451)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="Y -> S (in Ref. 1; AAA60451)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 127
SQ SEQUENCE 127 AA; 14740 MW; 66740A006B6DB2D7 CRC64;
ADGIFAIDQF TKVLLNYTGH ITWNPPAIFK SYCEIIVTYF PFDEQNCSMK LGTRTYDGTV
VAIYPEGPRP DLSNYMQSGE WALKDYRGFW HSVNYSCCLD TPYLDITYHF ILLRLPLYFI
VNVIIPC
