ID   ACHG_XENLA              Reviewed;         510 AA.
AC   P05376;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Acetylcholine receptor subunit gamma;
DE   Flags: Precursor;
GN   Name=chrng;
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: 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000250|UniProtKB:P13536};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC         ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P13536};
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. Gamma/CHRNG sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X07068; CAA30104.1; -; mRNA.
DR   PIR; B28529; B28529.
DR   AlphaFoldDB; P05376; -.
DR   SMR; P05376; -.
DR   GlyCosmos; P05376; 1 site, No reported glycans.
DR   AGR; Xenbase:XB-GENE-990014; -.
DR   Xenbase; XB-GENE-990014; chrng.L.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   CDD; cd19029; LGIC_ECD_nAChR_G; 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:SF60; ACETYLCHOLINE RECEPTOR SUBUNIT GAMMA; 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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..17
FT   CHAIN           18..510
FT                   /note="Acetylcholine receptor subunit gamma"
FT                   /id="PRO_0000000339"
FT   TOPO_DOM        18..234
FT                   /note="Extracellular"
FT   TRANSMEM        235..259
FT                   /note="Helical"
FT   TRANSMEM        268..286
FT                   /note="Helical"
FT   TRANSMEM        302..323
FT                   /note="Helical"
FT   TOPO_DOM        324..468
FT                   /note="Cytoplasmic"
FT   TRANSMEM        469..488
FT                   /note="Helical"
FT   MOD_RES         381
FT                   /note="Phosphotyrosine; by Tyr-kinases"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        145..159
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   510 AA;  58078 MW;  D13562CAD5CF3F73 CRC64;
     MDTVLLLVSL CISAAFCNNE EERLLNDLMK NYNKNLRPVE KDGDIISVSI KLTLTNLISL
     NEKEEALTTN VWVEMQWKDY RLSWDPNDYH GISMMRIPST SVWLPDVGLE NNVDGTFDIA
     LYTNTLVSSD GSMYWLPPAI YRSSCPVVVT YFPFDWQNCS IVFQSQTYSA NEIELLLTVD
     EQTIEWIEID PEAFTENGEW AIKHMPAKRI INHRLPRDDV NYQQIVFYLI IQRKPLFYII
     NIIVPCVLIS FVSILVYFLP AKAGGQKCTV SINILLAQTV FLFLVAQKIP ETSTSVPLIV
     KYLTFLMVVT ITIVANAVIV LNISLRTPNT HSMSSTVREL CLRTVPRLLR MHLRPTDAAP
     PLAPLMRRSS SLGLMMKADE YMLRKPRSQL MFEKQKERDG LMKVVLDKIG RGMENNTSDD
     LVHSLNHAAP EIRTCVEACC HIASATREKN DFKSENEEWI LMGRVIDRVC FLVMCFVFFL
     GTIGTFLAGH FNQAPAHPFP GDSKLYQPST
//