ID   ACHAB_XENLA             Reviewed;         457 AA.
AC   P05377;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Acetylcholine receptor subunit alpha-1-B;
DE   Flags: Precursor;
GN   Name=chrna1-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   PubMed=3339098; DOI=10.1083/jcb.106.2.469;
RA   Baldwin T.J., Yoshihara C.M., Blackmer K., Kintner C.R., Burden S.J.;
RT   "Regulation of acetylcholine receptor transcript expression during
RT   development in Xenopus laevis.";
RL   J. Cell Biol. 106:469-478(1988).
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       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; X07067; CAA30103.1; -; mRNA.
DR   PIR; A28529; A28529.
DR   RefSeq; NP_001192088.1; NM_001205159.1.
DR   AlphaFoldDB; P05377; -.
DR   SMR; P05377; -.
DR   PRIDE; P05377; -.
DR   GeneID; 445823; -.
DR   CTD; 445823; -.
DR   Xenbase; XB-GENE-6252266; chrna1.S.
DR   Proteomes; UP000186698; Genome assembly.
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:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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   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   Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..20
FT   CHAIN           21..457
FT                   /note="Acetylcholine receptor subunit alpha-1-B"
FT                   /id="PRO_0000000313"
FT   TOPO_DOM        21..230
FT                   /note="Extracellular"
FT   TRANSMEM        231..255
FT                   /note="Helical"
FT   TRANSMEM        263..281
FT                   /note="Helical"
FT   TRANSMEM        297..316
FT                   /note="Helical"
FT   TOPO_DOM        317..428
FT                   /note="Cytoplasmic"
FT   TRANSMEM        429..447
FT                   /note="Helical"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        148..162
FT                   /evidence="ECO:0000250"
FT   DISULFID        212..213
FT                   /note="Associated with receptor activation"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   457 AA;  52107 MW;  202A84A150C4DB11 CRC64;
     MDYTASCLIF LFIAAGTVFG TDHETRLIGD LFANYNKVVR PVETYKDQVV VTVGLQLIQL
     INVDEVNQIV STNIRLKQQW RDVNLKWDPA KYGGVKKIRI PSSDVWSPDL VLYNNADGDF
     AISKDTKILL EYTGKITWTP PAIFKSYCEI IVTYFPFDQQ NCSMKFGTWT YDGSLLVINP
     ERDRPDLSNF MASGEWMMKD YRCWKHWVYY TCCPDKPYLD ITYHFVLQRL PLYFIVNVII
     PCLLFSFLTG LVFYLPTDSG EKMTLSISVL LSLTVFLLVI VELIPSTSSA VPLIGKYMLF
     TMVFVIASII ITVIVINTHH RSPSTHTMPP WVRKIFIETI PNIMFFSTMK RPSQEKQPQK
     TFAEEMDISH ISGKLGPAAV TYQSPALKNP DVKSAIEGIK YIAETMKSDQ ESNKASEEWK
     FVAMVLDHIL LAVFMTVCVI GTLAVFAGRI IEMNMQE