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Database: UniProt
Entry: A0A498SUU3_ACAVI
LinkDB: A0A498SUU3_ACAVI
Original site: A0A498SUU3_ACAVI 
ID   A0A498SUU3_ACAVI        Unreviewed;       296 AA.
AC   A0A498SUU3;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Neurotransmitter-gated ion-channel ligand-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=NAV_LOCUS8766 {ECO:0000313|EMBL:VBB33975.1};
OS   Acanthocheilonema viteae (Filarial nematode worm) (Dipetalonema viteae).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Acanthocheilonema.
OX   NCBI_TaxID=6277 {ECO:0000313|EMBL:VBB33975.1, ECO:0000313|Proteomes:UP000276991};
RN   [1] {ECO:0000313|EMBL:VBB33975.1, ECO:0000313|Proteomes:UP000276991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL   Submitted (AUG-2018) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU000687}.
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DR   EMBL; UPTC01002893; VBB33975.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498SUU3; -.
DR   STRING; 6277.A0A498SUU3; -.
DR   Proteomes; UP000276991; 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   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; 1.
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; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR   PANTHER; PTHR18945:SF895; NICOTINIC ACETYLCHOLINE RECEPTOR ALPHA3, ISOFORM B; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276991};
KW   Signal {ECO:0000256|RuleBase:RU000687};
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   SIGNAL          1..17
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           18..296
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022267878"
FT   TRANSMEM        239..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          22..60
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          58..238
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          245..287
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
SQ   SEQUENCE   296 AA;  34210 MW;  757A98DB7130A0AF CRC64;
     MVTFGLLYIF LLPIIYCNED VSRLFEDLLV DYNKLVRPVD NKTNALVVRF KLKLSQLLDV
     TWTDIKLRWN PDEYGGVNML YVPSDMIWIP DIVLYNNADG NYQVSLSTKA KLSFNGTVEW
     TPPAIYKSMC QINVEWFPFD EQTCEMKFGS WTYGGLEVDL KHKDSDIERK VKEISVGVDG
     EHIETVWIVD KGIDLSDYYP SVEWDILGVS GKRHEIRYPC CESPFIDLTY EIHLRRKTLF
     YTVNLIFPIV GISFLAALVF YLPSDGGEKI SFCISILISL TIFFLLLGMF HSEKLQ
//
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