(data stored in SCRATCH zone)

SWISSPROT: 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   08-MAY-2019, entry version 134.
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.,
RA   Martino P.A., Hunt D.F., Cafiso D.S.;
RT   "Proteolytic fragments of the nicotinic acetylcholine receptor
RT   identified by mass spectrometry: implications for receptor
RT   topography.";
RL   Biochemistry 28:9184-9191(1989).
RN   [4]
RP   PROTEIN SEQUENCE OF 104-131.
RX   PubMed=1744130;
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;
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
RT   peptide 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.,
RA   Sakarellos-Daitsiotis M., 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
RT   data.";
RL   Biopolymers 40:419-432(1996).
CC   -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC       extensive change in conformation that affects all subunits and
CC       leads to opening of an ion-conducting channel across the plasma
CC       membrane.
CC   -!- SUBUNIT: Pentamer of two alpha chains, and one each of the beta,
CC       delta, and gamma chains.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-
CC       1/CHRNA1 sub-subfamily. {ECO:0000305}.
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; 1LK1; Model; -; A/E=26-235.
DR   PDB; 1LXG; NMR; -; B=205-222.
DR   PDB; 1LXH; NMR; -; B=205-222.
DR   PDB; 1OLK; Model; -; A/C=27-235.
DR   PDB; 1TOR; NMR; -; A=91-100.
DR   PDB; 1TOS; NMR; -; A=91-99.
DR   PDB; 3MRA; NMR; -; A=301-325.
DR   PDBsum; 1ABT; -.
DR   PDBsum; 1DXZ; -.
DR   PDBsum; 1IDG; -.
DR   PDBsum; 1IDH; -.
DR   PDBsum; 1LK1; -.
DR   PDBsum; 1LXG; -.
DR   PDBsum; 1LXH; -.
DR   PDBsum; 1OLK; -.
DR   PDBsum; 1TOR; -.
DR   PDBsum; 1TOS; -.
DR   PDBsum; 3MRA; -.
DR   SMR; P02710; -.
DR   ComplexPortal; CPX-2187; Acetylcholine receptor, alpha1-beta1-gamma-delta.
DR   IntAct; P02710; 3.
DR   BindingDB; P02710; -.
DR   ChEMBL; CHEMBL3097; -.
DR   TCDB; 1.A.9.1.9; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR   GlyConnect; 7; -.
DR   iPTMnet; P02710; -.
DR   SwissPalm; P02710; -.
DR   UniCarbKB; P02710; -.
DR   PRIDE; P02710; -.
DR   EvolutionaryTrace; P02710; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
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   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; 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;
DR   PRODOM; P02710.
DR   SWISS-2DPAGE; P02710.
KW   3D-structure; Cell junction; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Postsynaptic cell membrane;
KW   Receptor; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:6585820}.
FT   CHAIN        25    461       Acetylcholine receptor subunit alpha.
FT                                /FTId=PRO_0000000310.
FT   TOPO_DOM     25    234       Extracellular.
FT   TRANSMEM    235    259       Helical.
FT   TRANSMEM    267    285       Helical.
FT   TRANSMEM    301    320       Helical.
FT   TOPO_DOM    321    432       Cytoplasmic.
FT   TRANSMEM    433    451       Helical.
FT   CARBOHYD    165    165       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:2742850,
FT                                ECO:0000269|PubMed:6585820}.
FT   DISULFID    152    166
FT   DISULFID    216    217       Associated with receptor activation.
FT   TURN         93     99       {ECO:0000244|PDB:1TOR}.
FT   STRAND      214    218       {ECO:0000244|PDB:1LXG}.
FT   STRAND      262    264       {ECO:0000244|PDB:1DXZ}.
FT   HELIX       265    287       {ECO:0000244|PDB:1DXZ}.
FT   TURN        288    290       {ECO:0000244|PDB:1DXZ}.
FT   HELIX       304    306       {ECO:0000244|PDB:3MRA}.
FT   HELIX       307    323       {ECO:0000244|PDB:3MRA}.
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
//

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