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Database: UniProt
Entry: R0LT19_ANAPL
LinkDB: R0LT19_ANAPL
Original site: R0LT19_ANAPL 
ID   R0LT19_ANAPL            Unreviewed;       604 AA.
AC   R0LT19;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-4 {ECO:0000256|ARBA:ARBA00039991};
DE   Flags: Fragment;
GN   ORFNames=Anapl_13777 {ECO:0000313|EMBL:EOB08909.1};
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839 {ECO:0000313|EMBL:EOB08909.1, ECO:0000313|Proteomes:UP000296049};
RN   [1] {ECO:0000313|Proteomes:UP000296049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23749191; DOI=10.1038/ng.2657;
RA   Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA   Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA   Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA   Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA   Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA   Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA   Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA   Rao M., Pitel F., Wang J., Li N.;
RT   "The duck genome and transcriptome provide insight into an avian influenza
RT   virus reservoir species.";
RL   Nat. Genet. 45:776-783(2013).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC       Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004635}. 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. Alpha-4/CHRNA4 sub-
CC       subfamily. {ECO:0000256|ARBA:ARBA00038480}.
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DR   EMBL; KB742407; EOB08909.1; -; Genomic_DNA.
DR   AlphaFoldDB; R0LT19; -.
DR   Proteomes; UP000296049; 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; 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:SF401; NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-4; 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   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:EOB08909.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000296049};
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        219..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        250..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        284..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        578..600
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          12..217
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          225..595
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
FT   REGION          362..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EOB08909.1"
FT   NON_TER         604
FT                   /evidence="ECO:0000313|EMBL:EOB08909.1"
SQ   SEQUENCE   604 AA;  68867 MW;  8582F5DA6AA015D6 CRC64;
     AFGHVETRAH AEERLLKKLF SGYNKWSRPV ANISDVVLVR FGLSIAQLID VDEKNQMMTT
     NVWVKQEWHD YKLRWDPQEY ENVTSIRIPS ELIWRPDIVL YNNADGDFAV THLTKAHLFY
     DGRIKWMPPA IYKSSCSIDV TFFPFDQQNC TMKFGSWTYD KAKIDLVSMH SHVDQLDYWE
     SGEWVIINAV GNYNSKKYEC CTEIYPDITY SFIIRRLPLF YTINLIIPCL LISCLTVLVF
     YLPSECGEKI TLCISVLLSL TVFLLLITEI IPSTSLVIPL IGEYLLFTMI FVTLSIIITV
     FVLNVHHRSP RTHTMPDWVR RIFLDIVPRL LFMKRPSTVK DNCKKLIESM HKITNSPRLW
     SETDLEPNFT TSSSPSPQSN EPSPTSSFCA HLEEPAKPQP VCKSPSGQYS VLHPEPVQVT
     CSSPQPSRHL LSDTQTTSIS KGRSLSVQQM YSPNKAEEGS IRCRSRSIQY CYLQEDSSQT
     NGQSSASPAS QRCHLNEEQP QHKPHQCKCK CKKSEAAGTP AQGSKTHSNK GEHLVLMSPA
     LKLAVEGVHY IADHLRAEDA DFSVKEDWKY VAMVIDRIFL WMFIIVCLLG TVGLFLPPWL
     AGMI
//
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