ACHA_ERICO
ID ACHA_ERICO Reviewed; 84 AA.
AC P54249;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Acetylcholine receptor subunit alpha;
DE Flags: Fragment;
GN Name=CHRNA1;
OS Erinaceus concolor (Eastern European hedgehog) (Erinaceus roumanicus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=37316;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RX PubMed=7619817; DOI=10.1021/bi00028a029;
RA Barchan D., Ovadia M., Kochva E., Fuchs S.;
RT "The binding site of the nicotinic acetylcholine receptor in animal species
RT resistant to alpha-bungarotoxin.";
RL Biochemistry 34:9172-9176(1995).
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: 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 (in immature muscle) or epsilon (in mature muscle) chains. The muscle
CC heteropentamer composed of alpha-1, beta-1, delta, epsilon subunits
CC interacts with the alpha-conotoxin ImII.
CC {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U17016; AAA61645.1; -; mRNA.
DR AlphaFoldDB; P54249; -.
DR SMR; P54249; -.
DR GO; GO:0070161; C:anchoring 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:0005230; F:extracellular ligand-gated ion 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; IPR018000; Neurotransmitter_ion_chnl_CS.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR SUPFAM; SSF63712; SSF63712; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW Synapse; Transmembrane; Transport.
FT CHAIN <1..>84
FT /note="Acetylcholine receptor subunit alpha"
FT /id="PRO_0000076971"
FT SITE 66
FT /note="Confers toxin resistance"
FT /evidence="ECO:0000255"
FT SITE 68
FT /note="Confers toxin resistance"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 7..21
FT /evidence="ECO:0000250"
FT DISULFID 71..72
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 84
SQ SEQUENCE 84 AA; 9756 MW; 439578668037047F CRC64;
AIFKSYCEII VTHFPFDEQN CSMKLGTWTY DGSVVAINPE NDQPDLSNFM ESGEWVIKEA
RGWKHRVIYA CCPSTPYLDI TYHF
