ID A0A093Q4T6_9PASS Unreviewed; 496 AA.
AC A0A093Q4T6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Acetylcholine receptor subunit gamma {ECO:0000256|ARBA:ARBA00039195};
DE Flags: Fragment;
GN ORFNames=N305_01871 {ECO:0000313|EMBL:KFW81455.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW81455.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW81455.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW81455.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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; KL671175; KFW81455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093Q4T6; -.
DR STRING; 328815.ENSMVIP00005003463; -.
DR Proteomes; UP000053258; Unassembled WGS sequence.
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 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, ECO:0000313|EMBL:KFW81455.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053258};
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 TRANSMEM 226..248
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 292..315
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 457..479
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 9..225
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 232..474
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW81455.1"
FT NON_TER 496
FT /evidence="ECO:0000313|EMBL:KFW81455.1"
SQ SEQUENCE 496 AA; 56341 MW; 53F90270DAD4D6BC CRC64;
PGVGCRNQEE KLLQDLMSNY NRQLRPALRG DEIIDVSLKL TLTNLISLNE REETLTTNVW
IEMQWSDYRL QWDPEKYDNI QQLRVPSTMV WLPDIVLENN IDGTFEITLY ANVLVSPDGS
IYWLPPAIYR SVCVIHVTYF PFDWQNCTMV FQSQTYSANE INLLLTVEEG QTVEWIVIDP
EAFTENGEWA IKHRPARKII NSEHFTPDDT QYQQVVFYLI IQRKPLFYII NIIVPCVLIS
AMGVLVYFLP AKAGGQKCTV SINVLLAQTV FLFLIAQKVP ETSQAVPLIG KYLTFLMVVT
VVIVVNAVIV LNVSLRTPNT HSMSPRVRQV FLHLLPRYLG MPVSEETPGP PQAVRRCSSL
GLMVKADEYM LWKARTELLF EKQKERDGLM KTVLEKIGRG LESGSPQDFC QSLEEAGPEI
RACVDACNHI ANATREQNDF GSESEEWIMV GQVIDRVCFF IMASLFVCGT VGIFLVAHFN
QAPALPFPGD PKPYQP
//
