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Database: UniProt
Entry: A0A0R3PCH6_ANGCS
LinkDB: A0A0R3PCH6_ANGCS
Original site: A0A0R3PCH6_ANGCS 
ID   A0A0R3PCH6_ANGCS        Unreviewed;       479 AA.
AC   A0A0R3PCH6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 2.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Cation transporter family protein {ECO:0000313|WBParaSite:ACOC_0000151501-mRNA-1};
GN   ORFNames=ACOC_LOCUS1516 {ECO:0000313|EMBL:VDM53101.1};
OS   Angiostrongylus costaricensis (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC   Angiostrongylus.
OX   NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000151501-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ACOC_0000151501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM53101.1, ECO:0000313|Proteomes:UP000267027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Costa Rica {ECO:0000313|EMBL:VDM53101.1,
RC   ECO:0000313|Proteomes:UP000267027};
RG   Pathogen Informatics;
RL   Submitted (NOV-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}.
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DR   EMBL; UYYA01000229; VDM53101.1; -; Genomic_DNA.
DR   STRING; 334426.A0A0R3PCH6; -.
DR   WBParaSite; ACOC_0000151501-mRNA-1; ACOC_0000151501-mRNA-1; ACOC_0000151501.
DR   OMA; YAFNLIM; -.
DR   Proteomes; UP000050601; Unplaced.
DR   Proteomes; UP000267027; 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; cd18997; LGIC_ECD_nAChR; 1.
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   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945:SF524; ACETYLCHOLINE RECEPTOR; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267027};
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        223..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        254..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        284..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        454..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          18..222
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          229..470
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
SQ   SEQUENCE   479 AA;  56219 MW;  8FE00591138B3621 CRC64;
     MLPLFSLLLP SVRSSPSEQR LMNDLLAGYV REERPVLDSS KPVVVSLGVS MQQIINLNEK
     EEQLEVSAWL KFQWRDENLR WQPAAYDNVT DLRHPAGTIW QPDILLYNSV DPAFDSMYKV
     NLLNYHDGVV NWVPPGIFKI SCKLDIYWFP FDEQVCFFKF GSWSFSRDKI ELAVGDFDFS
     EYLPNGEWII FNSMVNISVK YYECCVEAFE DIKFTLHLRR RTLYYAFNLI MPCFLTMVLM
     VLGFTLSPET CEKVGLQISV SLAICIFLTI MNEMTPHTSE AVPLLGVFFQ SCMVISVLAT
     SFTVFVQSYH FRSHHNTHQM TFLMRFILLE WAAWLLRMKF PERENTIDTI KESWRNRKRL
     RRDTITAVNF LHEFPFPYLQ PRQFRLRTFR LFIYSPNLQI VSKVKDDQRT SERLRVLQKI
     YDHVKMIRER SDDGVKESLV ALEWRFAAMV VDRLGFLAFF GLLATTTFVI SVRAPYLVA
//
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