ID   ACHB_XENLA              Reviewed;         489 AA.
AC   P49579;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Acetylcholine receptor subunit beta;
DE   Flags: Precursor; Fragment;
GN   Name=chrnb1;
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].
RX   PubMed=8081730;
RA   Kullberg R.W., Zheng Y.C., Todt W., Owens J.L., Fraser S.E., Mandel G.;
RT   "Structure and expression of the nicotinic acetylcholine receptor beta
RT   subunit of Xenopus laevis.";
RL   Recept. Channels 2:23-31(1994).
CC   -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC       extensive change in conformation that affects all subunits and leads to
CC       opening of an ion-conducting channel across the plasma membrane.
CC   -!- SUBUNIT: Pentamer of two alpha chains, and one each of the beta, delta,
CC       and gamma (in immature muscle) or epsilon (in mature muscle) chains.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. Beta-1/CHRNB1 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U04618; AAC59659.1; -; mRNA.
DR   AlphaFoldDB; P49579; -.
DR   SMR; P49579; -.
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; 1.
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                   /evidence="ECO:0000255"
FT   CHAIN           21..489
FT                   /note="Acetylcholine receptor subunit beta"
FT                   /id="PRO_0000000320"
FT   TOPO_DOM        21..235
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        324..457
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        458..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        148..162
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   489 AA;  56347 MW;  4ED50C5A26B7BA6E CRC64;
     NSGALLWPLI WGLLLIGTQA LDKEAQLRDK VFENYNINVR PARTPDQRVV VQVGMTLAHV
     ISVSEKDEEL KTKVYLEMAW NDQRLSWDPK QYGGIESLRI SSSQVWTPDI VLMNNNDGNF
     NFALQVDVLV SPNGNVTWHP PGLYVSSCSI EVQYYPFDWQ NCSMVFRSYT YGADEVTLVH
     PKDANGKEVT QAVIFPNTFE ENGQWVIRHR SSRKNSSPND PLYEDITFYL VIQRKPLFYI
     VNVIVPCILI TILAIFVFYL PPDAGEKMTL SIFALLTLTV FLLLLADKVP ETSLGVPIIV
     NYLIFTMTLV TFSVIFSVVV LNLHHRSPNT HHMPQWVKQI FIHYLPKYLC IRRPKPETPL
     PVAPPPRQVT STRHADEYFI RRPENDFFLP KQERYHADPF SRDMKWFLEG PSLGLVLPRD
     LQSAVTAIRY LAQQLQEQED YDTLKEDWQY VAMVVDRLFL WTFIAFTSLG TLSIFLDANF
     NLPPDTPFP