ACHA_TETCF
ID ACHA_TETCF Reviewed; 461 AA.
AC P02710;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Acetylcholine receptor subunit alpha;
DE Flags: Precursor;
GN Name=CHRNA1;
OS Tetronarce californica (Pacific electric ray) (Torpedo californica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
OX NCBI_TaxID=7787;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6182472; DOI=10.1038/299793a0;
RA Noda M., Takahashi H., Tanabe T., Toyosato M., Furutani Y., Hirose T.,
RA Asai M., Inayama S., Miyata T., Numa S.;
RT "Primary structure of alpha-subunit precursor of Torpedo californica
RT acetylcholine receptor deduced from cDNA sequence.";
RL Nature 299:793-797(1982).
RN [2]
RP PROTEIN SEQUENCE OF 25-127; 336-421 AND 429-450, AND GLYCOSYLATION AT
RP ASN-165.
RX PubMed=6585820; DOI=10.1073/pnas.81.9.2631;
RA Conti-Tronconi B.M., Hunkapiller M.W., Raftery M.A.;
RT "Molecular weight and structural nonequivalence of the mature alpha
RT subunits of Torpedo californica acetylcholine receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2631-2634(1984).
RN [3]
RP PROTEIN SEQUENCE OF 29-41; 82-88; 132-149; 338-354 AND 363-411.
RX PubMed=2605252; DOI=10.1021/bi00449a034;
RA Moore C.R., Yates J.R. III, Griffin P.R., Shabanowitz J., Martino P.A.,
RA Hunt D.F., Cafiso D.S.;
RT "Proteolytic fragments of the nicotinic acetylcholine receptor identified
RT by mass spectrometry: implications for receptor topography.";
RL Biochemistry 28:9184-9191(1989).
RN [4]
RP PROTEIN SEQUENCE OF 104-131.
RX PubMed=1744130; DOI=10.1016/s0021-9258(18)54504-x;
RA Cohen J.B., Sharp S.D., Liu W.S.;
RT "Structure of the agonist-binding site of the nicotinic acetylcholine
RT receptor. [3H]acetylcholine mustard identifies residues in the cation-
RT binding subsite.";
RL J. Biol. Chem. 266:23354-23364(1991).
RN [5]
RP PROTEIN SEQUENCE OF 234-266; 287-319 AND 423-453.
RX PubMed=8130199; DOI=10.1021/bi00176a016;
RA Blanton M.P., Cohen J.B.;
RT "Identifying the lipid-protein interface of the Torpedo nicotinic
RT acetylcholine receptor: secondary structure implications.";
RL Biochemistry 33:2859-2872(1994).
RN [6]
RP PROTEIN SEQUENCE OF 126-145 AND 192-198, GLYCOSYLATION AT ASN-165, AND
RP DISULFIDE BOND.
RX PubMed=2742850; DOI=10.1021/bi00434a048;
RA Kellaris K.V., Ware D.K., Smith S., Kyte J.;
RT "Assessment of the number of free cysteines and isolation and
RT identification of cystine-containing peptides from acetylcholine
RT receptor.";
RL Biochemistry 28:3469-3482(1989).
RN [7]
RP DISULFIDE BONDS.
RX PubMed=3722144; DOI=10.1016/s0021-9258(19)83877-2;
RA Kao P.N., Karlin A.;
RT "Acetylcholine receptor binding site contains a disulfide cross-link
RT between adjacent half-cystinyl residues.";
RL J. Biol. Chem. 261:8085-8088(1986).
RN [8]
RP STRUCTURE BY NMR OF 209-220.
RX PubMed=8241115; DOI=10.1021/bi00097a004;
RA Basus V.J., Song G., Hawrot E.;
RT "NMR solution structure of an alpha-bungarotoxin/nicotinic receptor peptide
RT complex.";
RL Biochemistry 32:12290-12298(1993).
RN [9]
RP STRUCTURE BY NMR OF 91-100.
RX PubMed=9062066;
RX DOI=10.1002/(sici)1097-0282(1996)40:5<419::aid-bip1>3.0.co;2-z;
RA Orlewski P., Marraud M., Cung M.T., Tsikaris V., Sakarellos-Daitsiotis M.,
RA Sakarellos C., Vatzaki E., Tzartos S.J.;
RT "Compared structures of the free nicotinic acetylcholine receptor main
RT immunogenic region (MIR) decapeptide and the antibody-bound [A76]MIR
RT analogue: a molecular dynamics simulation from two-dimensional NMR data.";
RL Biopolymers 40:419-432(1996).
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:0000250|UniProtKB:P02711}.
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; AAA96705.1; -; mRNA.
DR PIR; A03170; ACRYA1.
DR PDB; 1ABT; NMR; -; B=209-220.
DR PDB; 1DXZ; NMR; -; A=260-291.
DR PDB; 1IDG; NMR; -; B=205-222.
DR PDB; 1IDH; NMR; -; B=205-222.
DR PDB; 1LXG; NMR; -; B=205-222.
DR PDB; 1LXH; NMR; -; B=205-222.
DR PDB; 1TOR; NMR; -; A=91-100.
DR PDB; 1TOS; NMR; -; A=91-99.
DR PDB; 3MRA; NMR; -; A=301-325.
DR PDB; 6UWZ; EM; 2.69 A; A/D=25-461.
DR PDB; 7QKO; EM; 2.90 A; A/D=25-461.
DR PDB; 7QL5; EM; 2.50 A; A/D=25-461.
DR PDB; 7QL6; EM; 3.23 A; A/D=25-461.
DR PDB; 7SMM; EM; 2.50 A; A/D=25-461.
DR PDB; 7SMQ; EM; 2.70 A; A/D=25-461.
DR PDB; 7SMR; EM; 2.77 A; A/D=25-461.
DR PDB; 7SMS; EM; 3.18 A; A/D=25-461.
DR PDB; 7SMT; EM; 2.56 A; A/D=25-461.
DR PDBsum; 1ABT; -.
DR PDBsum; 1DXZ; -.
DR PDBsum; 1IDG; -.
DR PDBsum; 1IDH; -.
DR PDBsum; 1LXG; -.
DR PDBsum; 1LXH; -.
DR PDBsum; 1TOR; -.
DR PDBsum; 1TOS; -.
DR PDBsum; 3MRA; -.
DR PDBsum; 6UWZ; -.
DR PDBsum; 7QKO; -.
DR PDBsum; 7QL5; -.
DR PDBsum; 7QL6; -.
DR PDBsum; 7SMM; -.
DR PDBsum; 7SMQ; -.
DR PDBsum; 7SMR; -.
DR PDBsum; 7SMS; -.
DR PDBsum; 7SMT; -.
DR AlphaFoldDB; P02710; -.
DR SMR; P02710; -.
DR ComplexPortal; CPX-2187; Acetylcholine receptor, alpha1-beta1-gamma-delta.
DR IntAct; P02710; 3.
DR BindingDB; P02710; -.
DR ChEMBL; CHEMBL3097; -.
DR DrugCentral; P02710; -.
DR TCDB; 1.A.9.1.9; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR GlyConnect; 7; 35 N-Linked glycans.
DR iPTMnet; P02710; -.
DR SwissPalm; P02710; -.
DR EvolutionaryTrace; P02710; -.
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; IMP: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; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Postsynaptic cell membrane; Receptor; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:6585820"
FT CHAIN 25..461
FT /note="Acetylcholine receptor subunit alpha"
FT /id="PRO_0000000310"
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:0000269|PubMed:2742850,
FT ECO:0000269|PubMed:6585820"
FT DISULFID 152..166
FT DISULFID 216..217
FT /note="Associated with receptor activation"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 53..68
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 73..85
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 163..174
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 198..216
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 222..233
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1DXZ"
FT HELIX 266..287
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:1DXZ"
FT HELIX 297..323
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 340..343
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 395..448
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 452..456
FT /evidence="ECO:0007829|PDB:6UWZ"
SQ SEQUENCE 461 AA; 52741 MW; 398C86C9309AF0D8 CRC64;
MILCSYWHVG LVLLLFSCCG LVLGSEHETR LVANLLENYN KVIRPVEHHT HFVDITVGLQ
LIQLISVDEV NQIVETNVRL RQQWIDVRLR WNPADYGGIK KIRLPSDDVW LPDLVLYNNA
DGDFAIVHMT KLLLDYTGKI MWTPPAIFKS YCEIIVTHFP FDQQNCTMKL GIWTYDGTKV
SISPESDRPD LSTFMESGEW VMKDYRGWKH WVYYTCCPDT PYLDITYHFI MQRIPLYFVV
NVIIPCLLFS FLTGLVFYLP TDSGEKMTLS ISVLLSLTVF LLVIVELIPS TSSAVPLIGK
YMLFTMIFVI SSIIITVVVI NTHHRSPSTH TMPQWVRKIF IDTIPNVMFF STMKRASKEK
QENKIFADDI DISDISGKQV TGEVIFQTPL IKNPDVKSAI EGVKYIAEHM KSDEESSNAA
EEWKYVAMVI DHILLCVFML ICIIGTVSVF AGRLIELSQE G
