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Database: UniProt
Entry: A0A1I8GCT6_9PLAT
LinkDB: A0A1I8GCT6_9PLAT
Original site: A0A1I8GCT6_9PLAT 
ID   A0A1I8GCT6_9PLAT        Unreviewed;       506 AA.
AC   A0A1I8GCT6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   31-JUL-2019, entry version 13.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:maker-uti_cns_0001463-snap-gene-1.2-mRNA-1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Platyhelminthes; Rhabditophora; Macrostomorpha;
OC   Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0001463-snap-gene-1.2-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0001463-snap-gene-1.2-mRNA-1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26392545; DOI=10.1073/pnas.1516718112;
RA   Wasik K., Gurtowski J., Zhou X., Ramos O.M., Delas M.J.,
RA   Battistoni G., El Demerdash O., Falciatori I., Vizoso D.B.,
RA   Smith A.D., Ladurner P., Scharer L., McCombie W.R., Hannon G.J.,
RA   Schatz M.;
RT   "Genome and transcriptome of the regeneration-competent flatworm,
RT   Macrostomum lignano.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:12462-12467(2015).
RN   [2] {ECO:0000313|WBParaSite:maker-uti_cns_0001463-snap-gene-1.2-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane {ECO:0000256|SAAS:SAAS00569352}; Multi-pass membrane
CC       protein {ECO:0000256|SAAS:SAAS00569352}. Cell membrane
CC       {ECO:0000256|SAAS:SAAS00569391}; Multi-pass membrane protein
CC       {ECO:0000256|SAAS:SAAS00569391}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. {ECO:0000256|RuleBase:RU000687,
CC       ECO:0000256|SAAS:SAAS00978283}.
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DR   WBParaSite; maker-uti_cns_0001463-snap-gene-1.2-mRNA-1; maker-uti_cns_0001463-snap-gene-1.2-mRNA-1; maker-uti_cns_0001463-snap-gene-1.2.
DR   Proteomes; UP000095280; Genome assembly.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   Gene3D; 2.70.170.10; -; 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; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   PANTHER; PTHR18945; PTHR18945; 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; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|SAAS:SAAS00458005};
KW   Cell membrane {ECO:0000256|SAAS:SAAS00458000};
KW   Complete proteome {ECO:0000313|Proteomes:UP000095280};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00081591};
KW   Ion channel {ECO:0000256|RuleBase:RU000687,
KW   ECO:0000256|SAAS:SAAS00458066};
KW   Ion transport {ECO:0000256|RuleBase:RU000687,
KW   ECO:0000256|SAAS:SAAS00457919};
KW   Ligand-gated ion channel {ECO:0000256|SAAS:SAAS00172123};
KW   Membrane {ECO:0000256|SAAS:SAAS00978300, ECO:0000256|SAM:Phobius};
KW   Postsynaptic cell membrane {ECO:0000256|SAAS:SAAS00081626};
KW   Receptor {ECO:0000256|SAAS:SAAS00172128};
KW   Synapse {ECO:0000256|SAAS:SAAS00103537};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00978734,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00978768,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU000687,
KW   ECO:0000256|SAAS:SAAS00081549}.
FT   TRANSMEM    216    239       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    251    269       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    281    304       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    468    490       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        8    215       Neur_chan_LBD. {ECO:0000259|Pfam:
FT                                PF02931}.
FT   DOMAIN      222    482       Neur_chan_memb. {ECO:0000259|Pfam:
FT                                PF02932}.
FT   REGION      341    384       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      397    421       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   506 AA;  58174 MW;  645F4A02332139F5 CRC64;
     IGSDDEIKLV NLLFKHKGYN RLIRPVSNLN QTVQVGFGLA MIQLINVEEK SQVMKSNVWL
     RMTWSDYQLR WDPSDFGGIQ VIRVNPNKIW KPDIVLYNNA DGRYEVSWQP NILIFSSGTI
     LWVPPAIYKS SCTIHVQYFP FDQQECEMKF GSWTFDATQV VLDWYEGARV ADLNDYWKSG
     SWDIIDCPGN ITLVEKLGQP PQTMMIFTIT IRRKTLFYTV NLIIPCVLIS FLSVCVFYLP
     ADAGEKMTLC ISILLALVVF LLLVSKILPP TSISIPLISK FLLFTFIMNI ITIVFTVIII
     NWNFRTPRTH KMPNWVRLLF LKYLPRVLFM KRPEHIDREE MAKHRMSRMA EKCNGGGGNS
     SKPQFGRSAR GRRAGGGDTA MSDEQFEMRD INSIDEPSDF EQQQQQQHQQ HPEQPQASGF
     SNLEVTPDLR RAIAAINFIS THLRIEDEYK RVLQDWKYVA SVIDRIQLVI FSSVTIVGTV
     AILMNAPFIL DFVDQDAIIK RLTDKS
//
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