ID A0A0A0AG02_CHAVO Unreviewed; 503 AA.
AC A0A0A0AG02;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Acetylcholine receptor subunit delta {ECO:0000256|ARBA:ARBA00039504};
DE Flags: Fragment;
GN ORFNames=N301_05134 {ECO:0000313|EMBL:KGL91935.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL91935.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL91935.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL91935.1};
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 {ECO:0000256|RuleBase:RU000687}.
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DR EMBL; KL871360; KGL91935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AG02; -.
DR STRING; 50402.A0A0A0AG02; -.
DR Proteomes; UP000053858; 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; cd19028; LGIC_ECD_nAChR_D; 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:SF61; ACETYLCHOLINE RECEPTOR SUBUNIT DELTA; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KGL91935.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
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 234..255
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 299..320
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 466..488
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 10..233
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 240..483
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT REGION 389..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL91935.1"
FT NON_TER 503
FT /evidence="ECO:0000313|EMBL:KGL91935.1"
SQ SEQUENCE 503 AA; 57765 MW; 53911EF995CDA847 CRC64;
LPGGLCMNQE ERLIHHLFEE RGYNKEVRPV VSNDQVVDVY LALTLSNLIS LKEVDETLTT
NVWLEHGWTD YRLQWNKSEF GDISVLRLPP DMLWLPEIVL ENNNDGLFEI AYYCNVLIYD
TGDVYWLPPA IFRSACPINV DFFPFDWQNC TLRFSSLAYS ALEINMHLKT DNDPKTGKNY
PVEWIIIDPE GFTENGEWEI IHRPARKNIH PEIPPDSSEH QDITFYLIIK RKPLFYVINI
VTPCILIAFM AILVFYLPAD SGEKMTLVVS VLLAQSVFLL LISQRLPATS HAIPLIGKYL
LFIMLLVTAV VMICIVVLNF HFRTPSTHIM SDWVKEVFLE SLPRLLGMTQ PAESPVGAPC
IRRCSSAGYI AKAEEYFSVK SRSELMFEKQ SERHGLTSRV TPAREPQPLR GDKGKGSTDT
GEEQLYEHIK PIVDGANFIV KYMREKNNYN EEKDNWNRVA RTLDRLCLFL ITPTLVVGTL
WIFLMGIYNH PPPLPFAGDP YDY
//
