ID A0A091NNE2_APAVI Unreviewed; 488 AA.
AC A0A091NNE2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Acetylcholine receptor subunit gamma {ECO:0000256|ARBA:ARBA00039195};
DE Flags: Fragment;
GN ORFNames=N311_12471 {ECO:0000313|EMBL:KFP90612.1};
OS Apaloderma vittatum (Bar-tailed trogon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP90612.1, ECO:0000313|Proteomes:UP000054244};
RN [1] {ECO:0000313|EMBL:KFP90612.1, ECO:0000313|Proteomes:UP000054244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP90612.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-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; KL388050; KFP90612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091NNE2; -.
DR Proteomes; UP000054244; 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:KFP90612.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054244};
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..313
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:KFP90612.1"
FT NON_TER 488
FT /evidence="ECO:0000313|EMBL:KFP90612.1"
SQ SEQUENCE 488 AA; 55730 MW; A04BB8A5CC347ACC CRC64;
PGVSCRNQEE KLLQDLMSNY NRDLRPALRG DQILDVTLKL TLTNLISLNE REETLTTNVW
IEMQWSDYRL RWDPEKYDNI QQLRVPSTMV WLPDIVLENN IDGTFEITLY TNVLVSPDGS
VYWLPPAIYR SACVIHVTYF PFDWQNCTMV FQSQTYSANE INLLLTVEEG QTVEWIFIDP
EAFTENGEWA IKHRPARKII NSEQFTPDDI QYQQVIFYLI IQRKPLFYVI NIIVPCVLIS
AMAVLVYFLP AKAGGQKCTV SINVLLAQTV FLFLIAQKVP ETSQAVPLIG KYLTFLMVVT
VVIVVNAVVV LNISLRTPNT HSMPERVRQV CLHLLPRYLG MHMPKETPGP PRAARRRSSL
GLIVKADEYM LWKARTELLF EKQKERDGLM KTVLEKIGRG LESGSAQDFC QSLEEAGPEI
RACVDACNHI ANATREQNDF SSESEEWILV GRVIDRVCFF IMASLFVCGT VGIFLMAHFN
QAPALPFP
//
