ID A0A183K5B7_9TREM Unreviewed; 562 AA.
AC A0A183K5B7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Neur_chan_LBD domain-containing protein {ECO:0000313|WBParaSite:SCUD_0001019001-mRNA-1};
GN ORFNames=SCUD_LOCUS10188 {ECO:0000313|EMBL:VDP38785.1};
OS Schistosoma curassoni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6186 {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0001019001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SCUD_0001019001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP38785.1, ECO:0000313|Proteomes:UP000279833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dakar {ECO:0000313|EMBL:VDP38785.1}, and Dakar, Senegal
RC {ECO:0000313|Proteomes:UP000279833};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UZAK01033635; VDP38785.1; -; Genomic_DNA.
DR STRING; 6186.A0A183K5B7; -.
DR WBParaSite; SCUD_0001019001-mRNA-1; SCUD_0001019001-mRNA-1; SCUD_0001019001.
DR Proteomes; UP000050789; Unplaced.
DR Proteomes; UP000279833; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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; 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 PANTHER; PTHR18945:SF865; ACETYLCHOLINE RECEPTOR SUBUNIT BETA-LIKE 2; 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; 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 Ion channel {ECO:0000256|RuleBase:RU000687};
KW Ion transport {ECO:0000256|RuleBase:RU000687};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW Reference proteome {ECO:0000313|Proteomes:UP000279833};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000687};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU000687}; Transport {ECO:0000256|RuleBase:RU000687}.
FT TRANSMEM 298..322
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 328..345
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 357..382
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 397..414
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 75..295
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 303..522
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
SQ SEQUENCE 562 AA; 65322 MW; 6E30CCB7D945DFD9 CRC64;
MQFDDLRNVC PIRFHRLLLI SSSAGSWNAV LAFPIVDFTS ASDPPRSLMI LPSIQLIFLL
YNYDCQCYEL SEQLFIKQLL SNYEIASRPI QYGNETLNIF LCIILKQIID LDEKNQILHT
SLLIQLKWID ETIQLRMLQL YDLYHRNNTT NKLKTYFPSL VLPSSRIWTP DLYVYNNADD
GKNGLLDVSH SRVRISQKGE VTWNLPVSIR SSCNVDVLYF PFDHQLCNIQ LASWIYDQSQ
LQLNIISMNT TIMLNKLIEN VELAVPELKL FKDYRITVGG QNITQINLRI HIYRRAIFYT
YTVIAPSILL CILTVFSFWL PSGNVKKIDM GLTVFLFLYF LQVMIAENTP ESNSTPLIGT
FLTMVMTLNS ISLIFATIVL HIHRRSKNDP CPTPHPLLWR LIIGIFGYLA MIPYKKMNQY
SIHLNCNHNN YIDNDHISYK SYKGDYRKSI IDERDLNEHE RLHNSNDPIT DSNNNNNNTD
LYNPTIVTNE EYSKEVNIRR WLYIARVVDR LLFQVYLITT IISIFVFLIY LPNSYDIKLN
AVVALPILVF TSASEPRCSS MM
//