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Acetylcholine receptor subunit alpha

 ACHA_TETCF              Reviewed;         461 AA.
P02710;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
10-MAY-2017, entry version 128.
RecName: Full=Acetylcholine receptor subunit alpha;
Flags: Precursor;
Name=CHRNA1;
Tetronarce californica (Pacific electric ray) (Torpedo californica).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
NCBI_TaxID=7787;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6182472; DOI=10.1038/299793a0;
Noda M., Takahashi H., Tanabe T., Toyosato M., Furutani Y., Hirose T.,
Asai M., Inayama S., Miyata T., Numa S.;
"Primary structure of alpha-subunit precursor of Torpedo californica
acetylcholine receptor deduced from cDNA sequence.";
Nature 299:793-797(1982).
[2]
PROTEIN SEQUENCE OF 25-127; 336-421 AND 429-450, AND GLYCOSYLATION AT
ASN-165.
PubMed=6585820; DOI=10.1073/pnas.81.9.2631;
Conti-Tronconi B.M., Hunkapiller M.W., Raftery M.A.;
"Molecular weight and structural nonequivalence of the mature alpha
subunits of Torpedo californica acetylcholine receptor.";
Proc. Natl. Acad. Sci. U.S.A. 81:2631-2634(1984).
[3]
PROTEIN SEQUENCE OF 29-41; 82-88; 132-149; 338-354 AND 363-411.
PubMed=2605252; DOI=10.1021/bi00449a034;
Moore C.R., Yates J.R. III, Griffin P.R., Shabanowitz J.,
Martino P.A., Hunt D.F., Cafiso D.S.;
"Proteolytic fragments of the nicotinic acetylcholine receptor
identified by mass spectrometry: implications for receptor
topography.";
Biochemistry 28:9184-9191(1989).
[4]
PROTEIN SEQUENCE OF 104-131.
PubMed=1744130;
Cohen J.B., Sharp S.D., Liu W.S.;
"Structure of the agonist-binding site of the nicotinic acetylcholine
receptor. [3H]acetylcholine mustard identifies residues in the cation-
binding subsite.";
J. Biol. Chem. 266:23354-23364(1991).
[5]
PROTEIN SEQUENCE OF 234-266; 287-319 AND 423-453.
PubMed=8130199; DOI=10.1021/bi00176a016;
Blanton M.P., Cohen J.B.;
"Identifying the lipid-protein interface of the Torpedo nicotinic
acetylcholine receptor: secondary structure implications.";
Biochemistry 33:2859-2872(1994).
[6]
PROTEIN SEQUENCE OF 126-145 AND 192-198, GLYCOSYLATION AT ASN-165, AND
DISULFIDE BOND.
PubMed=2742850; DOI=10.1021/bi00434a048;
Kellaris K.V., Ware D.K., Smith S., Kyte J.;
"Assessment of the number of free cysteines and isolation and
identification of cystine-containing peptides from acetylcholine
receptor.";
Biochemistry 28:3469-3482(1989).
[7]
DISULFIDE BONDS.
PubMed=3722144;
Kao P.N., Karlin A.;
"Acetylcholine receptor binding site contains a disulfide cross-link
between adjacent half-cystinyl residues.";
J. Biol. Chem. 261:8085-8088(1986).
[8]
STRUCTURE BY NMR OF 209-220.
PubMed=8241115; DOI=10.1021/bi00097a004;
Basus V.J., Song G., Hawrot E.;
"NMR solution structure of an alpha-bungarotoxin/nicotinic receptor
peptide complex.";
Biochemistry 32:12290-12298(1993).
[9]
STRUCTURE BY NMR OF 91-100.
PubMed=9062066;
DOI=10.1002/(SICI)1097-0282(1996)40:5<419::AID-BIP1>3.0.CO;2-Z;
Orlewski P., Marraud M., Cung M.T., Tsikaris V.,
Sakarellos-Daitsiotis M., Sakarellos C., Vatzaki E., Tzartos S.J.;
"Compared structures of the free nicotinic acetylcholine receptor main
immunogenic region (MIR) decapeptide and the antibody-bound [A76]MIR
analogue: a molecular dynamics simulation from two-dimensional NMR
data.";
Biopolymers 40:419-432(1996).
-!- FUNCTION: After binding acetylcholine, the AChR responds by an
extensive change in conformation that affects all subunits and
leads to opening of an ion-conducting channel across the plasma
membrane.
-!- SUBUNIT: Pentamer of two alpha chains, and one each of the beta,
delta, and gamma chains.
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
membrane protein.
-!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-
1/CHRNA1 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J00963; AAA96705.1; -; mRNA.
PIR; A03170; ACRYA1.
PDB; 1ABT; NMR; -; B=209-220.
PDB; 1DXZ; NMR; -; A=260-291.
PDB; 1IDG; NMR; -; B=205-222.
PDB; 1IDH; NMR; -; B=205-222.
PDB; 1LK1; Model; -; A/E=26-235.
PDB; 1LXG; NMR; -; B=205-222.
PDB; 1LXH; NMR; -; B=205-222.
PDB; 1OLK; Model; -; A/C=27-235.
PDB; 1TOR; NMR; -; A=91-100.
PDB; 1TOS; NMR; -; A=91-99.
PDB; 3MRA; NMR; -; A=301-325.
PDBsum; 1ABT; -.
PDBsum; 1DXZ; -.
PDBsum; 1IDG; -.
PDBsum; 1IDH; -.
PDBsum; 1LK1; -.
PDBsum; 1LXG; -.
PDBsum; 1LXH; -.
PDBsum; 1OLK; -.
PDBsum; 1TOR; -.
PDBsum; 1TOS; -.
PDBsum; 3MRA; -.
ProteinModelPortal; P02710; -.
SMR; P02710; -.
IntAct; P02710; 3.
BindingDB; P02710; -.
ChEMBL; CHEMBL3097; -.
TCDB; 1.A.9.1.9; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
SwissPalm; P02710; -.
UniCarbKB; P02710; -.
HOVERGEN; HBG003756; -.
EvolutionaryTrace; P02710; -.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
Gene3D; 2.70.170.10; -; 1.
InterPro; IPR006202; Neur_chan_lig-bd.
InterPro; IPR006201; Neur_channel.
InterPro; IPR006029; Neurotrans-gated_channel_TM.
InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
PANTHER; PTHR18945; PTHR18945; 1.
Pfam; PF02931; Neur_chan_LBD; 1.
Pfam; PF02932; Neur_chan_memb; 2.
PRINTS; PR00254; NICOTINICR.
PRINTS; PR00252; NRIONCHANNEL.
SUPFAM; SSF63712; SSF63712; 1.
SUPFAM; SSF90112; SSF90112; 1.
TIGRFAMs; TIGR00860; LIC; 1.
PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Direct protein sequencing;
Disulfide bond; Glycoprotein; Ion channel; Ion transport;
Ligand-gated ion channel; Membrane; Postsynaptic cell membrane;
Receptor; Signal; Synapse; Transmembrane; Transmembrane helix;
Transport.
SIGNAL 1 24 {ECO:0000269|PubMed:6585820}.
CHAIN 25 461 Acetylcholine receptor subunit alpha.
/FTId=PRO_0000000310.
TOPO_DOM 25 234 Extracellular.
TRANSMEM 235 259 Helical.
TRANSMEM 267 285 Helical.
TRANSMEM 301 320 Helical.
TOPO_DOM 321 432 Cytoplasmic.
TRANSMEM 433 451 Helical.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2742850,
ECO:0000269|PubMed:6585820}.
DISULFID 152 166
DISULFID 216 217 Associated with receptor activation.
TURN 93 99 {ECO:0000244|PDB:1TOR}.
STRAND 214 218 {ECO:0000244|PDB:1LXG}.
STRAND 262 264 {ECO:0000244|PDB:1DXZ}.
HELIX 265 287 {ECO:0000244|PDB:1DXZ}.
TURN 288 290 {ECO:0000244|PDB:1DXZ}.
HELIX 304 306 {ECO:0000244|PDB:3MRA}.
HELIX 307 323 {ECO:0000244|PDB:3MRA}.
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


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