ID ACHA_CHICK Reviewed; 456 AA.
AC P09479;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 27-MAR-2024, entry version 163.
DE RecName: Full=Acetylcholine receptor subunit alpha;
DE Flags: Precursor;
GN Name=CHRNA1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=White leghorn; TISSUE=Brain;
RX PubMed=3267226; DOI=10.1002/j.1460-2075.1988.tb02852.x;
RA Nef P., Oneyser C., Alliod C., Couturier S., Ballivet M.;
RT "Genes expressed in the brain define three distinct neuronal nicotinic
RT acetylcholine receptors.";
RL EMBO J. 7:595-601(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 1-12.
RX PubMed=3821734; DOI=10.1128/mcb.7.2.951-955.1987;
RA Klarsfeld A., Daubas P., Bourachot B., Changeux J.-P.;
RT "A 5'-flanking region of the chicken acetylcholine receptor alpha-subunit
RT gene confers tissue specificity and developmental control of expression in
RT transfected cells.";
RL Mol. Cell. Biol. 7:951-955(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-227 AND 260-333.
RX PubMed=6327170; DOI=10.1101/sqb.1983.048.01.011;
RA Ballivet M., Nef P., Stalder R., Fulpius B.;
RT "Genomic sequences encoding the alpha-subunit of acetylcholine receptor are
RT conserved in evolution.";
RL Cold Spring Harb. Symp. Quant. Biol. 48:83-87(1983).
RN [4]
RP PROTEIN SEQUENCE OF 21-44.
RX PubMed=3860855; DOI=10.1073/pnas.82.15.5208;
RA Conti-Tronconi B.M., Dunn S.M.J., Barnard E.A., Dolly J.O., Lai F.A.,
RA Ray N., Raftery M.A.;
RT "Brain and muscle nicotinic acetylcholine receptors are different but
RT homologous proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5208-5212(1985).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:P02709};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P02709};
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; X07330; CAA30282.1; -; Genomic_DNA.
DR EMBL; X07331; CAA30282.1; JOINED; Genomic_DNA.
DR EMBL; X12434; CAA30282.1; JOINED; Genomic_DNA.
DR EMBL; X12435; CAA30282.1; JOINED; Genomic_DNA.
DR EMBL; X12436; CAA30282.1; JOINED; Genomic_DNA.
DR EMBL; X07335; CAA30282.1; JOINED; Genomic_DNA.
DR EMBL; AJ250359; CAB59624.1; -; mRNA.
DR EMBL; AF051909; AAC06012.1; -; Genomic_DNA.
DR EMBL; M14808; AAA48565.1; -; Genomic_DNA.
DR EMBL; M14809; AAA48564.1; -; Genomic_DNA.
DR PIR; I50149; I50149.
DR PIR; I50150; I50150.
DR PIR; S00376; ACCHAN.
DR RefSeq; NP_990147.1; NM_204816.1.
DR AlphaFoldDB; P09479; -.
DR SMR; P09479; -.
DR ComplexPortal; CPX-254; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma.
DR STRING; 9031.ENSGALP00000046874; -.
DR GlyCosmos; P09479; 1 site, No reported glycans.
DR PaxDb; 9031-ENSGALP00000015122; -.
DR GeneID; 395608; -.
DR KEGG; gga:395608; -.
DR CTD; 1134; -.
DR VEuPathDB; HostDB:geneid_395608; -.
DR eggNOG; KOG3645; Eukaryota.
DR HOGENOM; CLU_018074_2_1_1; -.
DR InParanoid; P09479; -.
DR PhylomeDB; P09479; -.
DR PRO; PR:P09479; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0035094; P:response to nicotine; IBA:GO_Central.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
DR CDD; cd19014; LGIC_ECD_nAChR_A1; 1.
DR CDD; cd19064; LGIC_TM_nAChR; 1.
DR Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 2.
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 NCBIfam; TIGR00860; LIC; 1.
DR PANTHER; PTHR18945:SF74; ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA; 1.
DR PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00254; NICOTINICR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:3860855"
FT CHAIN 21..456
FT /note="Acetylcholine receptor subunit alpha"
FT /id="PRO_0000000308"
FT TOPO_DOM 21..229
FT /note="Extracellular"
FT TRANSMEM 230..254
FT /note="Helical"
FT TRANSMEM 262..280
FT /note="Helical"
FT TRANSMEM 296..315
FT /note="Helical"
FT TOPO_DOM 316..427
FT /note="Cytoplasmic"
FT TRANSMEM 428..446
FT /note="Helical"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 147..161
FT DISULFID 211..212
FT /note="Associated with receptor activation"
FT CONFLICT 33
FT /note="E -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 52183 MW; 0B31B6EABD7B4D42 CRC64;
MELCRVLLLI FSAAGPALCY EHETRLVDDL FREYSKVVRP VENHRDAVVV TVGLQLIQLI
NVDEVNQIVT TNVRLKQQWT DINLKWNPDD YGGVKQIRIP SDDIWRPDLV LYNNADGDFA
IVKYTKVLLE HTGKITWTPP AIFKSYCEII VTYFPFDQQN CSMKLGTWTY DGTMVVINPE
SDRPDLSNFM ESGEWVMKDY RGWKHWVYYA CCPDTPYLDI TYHFLMQRLP LYFIVNVIIP
CLLFSFLTGF VFYLPTDSGE KMTLSISVLL SLTVFLLVIV ELIPSTSSAV PLIGKYMLFT
MVFVIASIII TVIVINTHHR SPSTHTMPPW VRKIFIDTIP NIMFFSTMKR PSRDKPDKKI
FAEDIDISEI SGKQGPVPVN FYSPLTKNPD VKNAIEGIKY IAETMKSDQE SSNAADEWKF
VAMVLDHLLL VIFMLVCIIG TLAVFAGRLI ELNQQG
//
