ID H3B7M9_LATCH Unreviewed; 508 AA.
AC H3B7M9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Acetylcholine receptor subunit gamma {ECO:0000256|ARBA:ARBA00039195};
GN Name=CHRNG {ECO:0000313|Ensembl:ENSLACP00000017900.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000017900.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000017900.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00003328}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034104}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034099}.
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:0000256|ARBA:ARBA00038482}.
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DR EMBL; AFYH01083700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01083701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01083702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01083703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005997427.2; XM_005997365.2.
DR AlphaFoldDB; H3B7M9; -.
DR STRING; 7897.ENSLACP00000017900; -.
DR Ensembl; ENSLACT00000018030.1; ENSLACP00000017900.1; ENSLACG00000015771.2.
DR GeneID; 102351763; -.
DR KEGG; lcm:102351763; -.
DR CTD; 1146; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000160041; -.
DR InParanoid; H3B7M9; -.
DR OMA; CVDACNL; -.
DR OrthoDB; 5489962at2759; -.
DR TreeFam; TF315605; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000015771; Expressed in mesonephros and 1 other cell type or tissue.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015464; F:acetylcholine receptor activity; IEA:Ensembl.
DR GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IEA:InterPro.
DR GO; GO:1905145; P:cellular response to acetylcholine; IEA:Ensembl.
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 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 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU000687};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU000687};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Signal {ECO:0000256|RuleBase:RU000687};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000687};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU000687};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000687}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT CHAIN 18..508
FT /note="Acetylcholine receptor subunit gamma"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5022252160"
FT TRANSMEM 237..259
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 271..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 299..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 469..491
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 22..236
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 243..486
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
SQ SEQUENCE 508 AA; 58854 MW; 0EF80FEF732B3E83 CRC64;
MGTVVVLLCL SITGVLCRNQ EELLLNKLMR DYNSNLRPAE NEGDIINVTL KLTLTNLISL
NEIEEALTTN VWIEMTWRDY RLQWNPHEHH NITCLRVPSK MVWLPDIVLE NNIDGNFEIT
LYINVLVSPN GNIYWLPPAI YRSSCSIIVN YFPFDWQNCS LVFRSQTYSA NEIDLQLTVE
ENQTIEWIVI DPEDFTENGE WAIKHKPAKR LVNDRFTKDD LEYQEVIFYL IIQRKPLFYV
INIITPCVLI SSIGLLVYFL PAKAGGQKCT LSINVLLAQT VYLFLIAKKV PETSQAVPLI
VKYLTFLMCM EIIIVMNCVI VLNVSLRTPN THTMSHKVRE LFLKWLPRYL GMHLNPSEEV
WCAPVPRRKS SLRLIFKADE YMLRKARSEL MFERQKERDG LMKAVLQKIG SRLENGTIHD
ICYSLSHTAP QIRKCVEACN YIVKSTQEQN EFDSENEEWI LVGKVIDRVC FWIIFCVFIC
GTVGVFLMAH FNQAPSDPFP GDPKKYLP
//
