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Database: UniProt
Entry: A0A0V0X959_9BILA
LinkDB: A0A0V0X959_9BILA
Original site: A0A0V0X959_9BILA 
ID   A0A0V0X959_9BILA        Unreviewed;       498 AA.
AC   A0A0V0X959;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   13-SEP-2023, entry version 27.
DE   SubName: Full=Ligand-gated ion channel 50 {ECO:0000313|EMBL:KRX84576.1};
GN   Name=lgc-50 {ECO:0000313|EMBL:KRX84576.1};
GN   ORFNames=T06_65 {ECO:0000313|EMBL:KRX84576.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX84576.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX84576.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX84576.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       {ECO:0000256|RuleBase:RU000687}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX84576.1}.
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DR   EMBL; JYDK01000005; KRX84576.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0X959; -.
DR   STRING; 92179.A0A0V0X959; -.
DR   Proteomes; UP000054673; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   CDD; cd18990; LGIC_ECD_GABAAR; 1.
DR   CDD; cd19049; LGIC_TM_anion; 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; 1.
DR   InterPro; IPR006028; GABAA/Glycine_rcpt.
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   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945:SF406; LIGAND-GATED ION CHANNEL 46-RELATED; 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; PR00253; GABAARECEPTR.
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   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU000687};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU000687};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU000687};
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..24
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           25..498
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022251380"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        283..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        312..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        479..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          45..249
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          257..493
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
FT   REGION          344..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   498 AA;  58339 MW;  D25398CBD43C3AA0 CRC64;
     MTNFFTYAWI YLFVVRMLPN FGVSYAYTEH HSLWKAEFPR CTKDSEIIER LLSTYNRNKV
     PGGMASVKLE VWVQEITSIS DITSDFNIDL YVSELWLDPA LSYSHMNPCK QNLSLNNEIL
     KHLWTPNSCF INSKTAEIHE SPFPNIFLLI YPNGTVWTNY RLTLTGPCTM DLTAFPFDSV
     TCQLTFESFN YNTDEVKMSW TDIGVEPMRE KMELADYMLE NIVNFRNEVS YPAGKWHELT
     MQFKFKRRPG WYILQAYLPT FLTIFISWIA FCLGTKAIPA RTMLGVNALL AMTFQFGNVI
     RNLPRVSYVK AIDVWMLSCM TFVFCSLLEL AWVGYLSRKA NGFKRPPTSA ARNQSSHKHK
     KKKTVMLKNE PKNYGTMNFD MENFHSIHHL NRNNSHTNVT TAFPFFDSDD PYEYRPPGLQ
     RQMNVNLFPK SYSYLCKCQQ RLNQSNSYNK LKETTANQTE NQFYDYDSLA LKIDHISCFV
     FPTLFVLFNI FYWCYYLT
//
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