ID A0A087QNE7_APTFO Unreviewed; 435 AA.
AC A0A087QNE7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE SubName: Full=Neuronal acetylcholine receptor subunit alpha-10 {ECO:0000313|EMBL:KFM02751.1};
DE Flags: Fragment;
GN ORFNames=AS27_06648 {ECO:0000313|EMBL:KFM02751.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM02751.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM02751.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM02751.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL225752; KFM02751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QNE7; -.
DR STRING; 9233.A0A087QNE7; -.
DR Proteomes; UP000053286; 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; cd19051; LGIC_TM_cation; 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:SF889; NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-10; 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:KFM02751.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286};
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 214..237
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 277..296
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 414..432
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 7..211
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 219..429
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT REGION 333..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM02751.1"
FT NON_TER 435
FT /evidence="ECO:0000313|EMBL:KFM02751.1"
SQ SEQUENCE 435 AA; 48971 MW; 50EAC9FF6A637156 CRC64;
AQGRFAYKLL HDLFANYSSA LRPVEDTDRA LNVTLQVTLS QIIDMDERNQ VLTSYLWVRQ
AWLDAHLTWD KDAYDGIDSI RIPSSYVWRP DIILYNNADD RFGGSMETNV VLRSDGHIMW
DSPAITRSSC KVDVSYFPFD GQRCHLTFGS WTYNGNQIDL HNRLDAGDLT DFVENVEWEV
LGMPATRNVI TYGCCSEPYP DITYTLLLRR RASFYIFNLL LPCIMVSFLA PLGFYLPSDS
GEKVSLGVTV LLALTVFQLL VAESMPPSES VPLIGKYYIA TMTMITASTA LTIFIMNIHH
CGPGARPVPP WARRLILHHM ARLCCVYEVG ESCKSPQRAP GRRAGRGDAG VPGESPGEGE
VGAEVGGCPR DRCLCHHDGL LRNVSYIAGW VRRHRAAQRW TGEWKKVAKV MDRFLMWVFF
LMVFLMSVLV LAKAA
//