ACHA_TORMA
ID ACHA_TORMA Reviewed; 461 AA.
AC P02711;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Acetylcholine receptor subunit alpha;
DE Flags: Precursor;
GN Name=CHRNA1;
OS Torpedo marmorata (Marbled electric ray).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX NCBI_TaxID=7788;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-335 AND 341-411.
RX PubMed=6183641; DOI=10.1093/nar/10.19.5809;
RA Sumikawa K., Houghton M., Smith J.C., Bell L., Richards B.M., Barnard E.A.;
RT "The molecular cloning and characterisation of cDNA coding for the alpha
RT subunit of the acetylcholine receptor.";
RL Nucleic Acids Res. 10:5809-5822(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6572962; DOI=10.1073/pnas.80.7.2067;
RA Devillers-Thiery A., Giraudat J., Bentaboulet M., Changeux J.-P.;
RT "Complete mRNA coding sequence of the acetylcholine binding alpha-subunit
RT of Torpedo marmorata acetylcholine receptor: a model for the transmembrane
RT organization of the polypeptide chain.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:2067-2071(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6549423; DOI=10.1007/978-1-4684-4868-9_3;
RA Devillers-Thiery A., Giraudat J., Bentaboulet M., Klarsfeld A.,
RA Changeux J.-P.;
RT "Molecular genetics of Torpedo marmorata acetylcholine receptor.";
RL Adv. Exp. Med. Biol. 181:17-29(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-79.
RX PubMed=6327147; DOI=10.1101/sqb.1983.048.01.014;
RA Barnard E.A., Beeson D., Bilbe G., Brown D.A., Constanti A.,
RA Conti-Tronconi B.M., Dolly J.O., Dunn S.M.J., Mehraban F., Richards B.M.,
RA Smart T.G.;
RT "Acetylcholine and GABA receptors: subunits of central and peripheral
RT receptors and their encoding nucleic acids.";
RL Cold Spring Harb. Symp. Quant. Biol. 48:109-124(1983).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.0 ANGSTROMS) OF 235-461.
RX PubMed=12827192; DOI=10.1038/nature01748;
RA Miyazawa A., Fujiyoshi Y., Unwin N.;
RT "Structure and gating mechanism of the acetylcholine receptor pore.";
RL Nature 423:949-955(2003).
RN [6]
RP STRUCTURE BY NMR OF 206-228 IN COMPLEX WITH ALPHA-BUNGAROTOXIN.
RX PubMed=12160749; DOI=10.1016/s0896-6273(02)00773-0;
RA Samson A.O., Scherf T., Eisenstein M., Chill J.H., Anglister J.;
RT "The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins
RT and species-specific resistance to alpha-bungarotoxin revealed by NMR.";
RL Neuron 35:319-332(2002).
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.
CC {ECO:0000250|UniProtKB:P02708}.
CC -!- SUBUNIT: Pentamer of two alpha chains, and one each of the beta, delta,
CC and gamma chains. {ECO:0000269|PubMed:12160749}.
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; J00963; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M25893; AAA96704.1; -; mRNA.
DR EMBL; M14807; AAA49273.1; -; mRNA.
DR PIR; A93440; A93440.
DR PIR; I50548; I50548.
DR PIR; I50549; I50549.
DR PDB; 1L4W; NMR; -; B=206-226.
DR PDB; 1LJZ; NMR; -; B=206-226.
DR PDB; 1OED; EM; 4.00 A; A/D=235-461.
DR PDB; 2BG9; EM; 4.00 A; A/D=25-461.
DR PDB; 4AQ5; EM; 6.20 A; A/D=1-461.
DR PDB; 4AQ9; EM; 6.20 A; A/D=1-461.
DR PDB; 4BOG; EM; 50.00 A; 2/A/D/F/I/K/N/P/S/U/X/Z=1-461.
DR PDB; 4BOI; EM; 41.00 A; A/D=1-461.
DR PDB; 4BON; EM; 40.00 A; A/D=1-461.
DR PDB; 4BOO; EM; 42.00 A; A/D=1-461.
DR PDB; 4BOR; EM; 42.00 A; A/D=1-461.
DR PDB; 4BOT; EM; 42.00 A; A/D=1-461.
DR PDBsum; 1L4W; -.
DR PDBsum; 1LJZ; -.
DR PDBsum; 1OED; -.
DR PDBsum; 2BG9; -.
DR PDBsum; 4AQ5; -.
DR PDBsum; 4AQ9; -.
DR PDBsum; 4BOG; -.
DR PDBsum; 4BOI; -.
DR PDBsum; 4BON; -.
DR PDBsum; 4BOO; -.
DR PDBsum; 4BOR; -.
DR PDBsum; 4BOT; -.
DR AlphaFoldDB; P02711; -.
DR SMR; P02711; -.
DR ComplexPortal; CPX-2635; Acetylcholine receptor, alpha1-beta1-gamma-delta.
DR PRIDE; P02711; -.
DR EvolutionaryTrace; P02711; -.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IPI:ComplexPortal.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IDA:ComplexPortal.
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; 2.
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 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane;
KW Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..24
FT CHAIN 25..461
FT /note="Acetylcholine receptor subunit alpha"
FT /id="PRO_0000000311"
FT TOPO_DOM 25..234
FT /note="Extracellular"
FT TRANSMEM 235..259
FT /note="Helical"
FT TRANSMEM 267..285
FT /note="Helical"
FT TRANSMEM 301..320
FT /note="Helical"
FT TOPO_DOM 321..432
FT /note="Cytoplasmic"
FT TRANSMEM 433..451
FT /note="Helical"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 152..166
FT DISULFID 216..217
FT /note="Associated with receptor activation"
FT CONFLICT 347
FT /note="V -> L (in Ref. 3; AAA96704)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="S -> C (in Ref. 3; AAA96704)"
FT /evidence="ECO:0000305"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:1L4W"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1L4W"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1L4W"
SQ SEQUENCE 461 AA; 52795 MW; 5354B3F8451D4F8C CRC64;
MILCSYWHVG LVLLLFSCCG LVLGSEHETR LVANLLENYN KVIRPVEHHT HFVDITVGLQ
LIQLINVDEV NQIVETNVRL RQQWIDVRLR WNPADYGGIK KIRLPSDDVW LPDLVLYNNA
DGDFAIVHMT KLLLDYTGKI MWTPPAIFKS YCEIIVTHFP FDQQNCTMKL GIWTYDGTKV
SISPESDRPD LSTFMESGEW VMKDYRGWKH WVYYTCCPDT PYLDITYHFI MQRIPLYFVV
NVIIPCLLFS FLTVLVFYLP TDSGEKMTLS ISVLLSLTVF LLVIVELIPS TSSAVPLIGK
YMLFTMIFVI SSIIVTVVVI NTHHRSPSTH TMPQWVRKIF INTIPNVMFF STMKRASKEK
QENKIFADDI DISDISGKQV TGEVIFQTPL IKNPDVKSAI EGVKYIAEHM KSDEESSNAA
EEWKYVAMVI DHILLCVFML ICIIGTVSVF AGRLIELSQE G
