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Database: UniProt
Entry: A0A1I8HXF5_9PLAT
LinkDB: A0A1I8HXF5_9PLAT
Original site: A0A1I8HXF5_9PLAT 
ID   A0A1I8HXF5_9PLAT        Unreviewed;      2119 AA.
AC   A0A1I8HXF5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Neur_chan_LBD domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0008525-snap-gene-0.3-mRNA-1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0008525-snap-gene-0.3-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0008525-snap-gene-0.3-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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   WBParaSite; maker-uti_cns_0008525-snap-gene-0.3-mRNA-1; maker-uti_cns_0008525-snap-gene-0.3-mRNA-1; maker-uti_cns_0008525-snap-gene-0.3.
DR   Proteomes; UP000095280; Unplaced.
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; cd19032; LGIC_ECD_nAChR_proto_beta-like; 1.
DR   CDD; cd19064; LGIC_TM_nAChR; 2.
DR   Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 2.
DR   Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 4.
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; 2.
DR   PANTHER; PTHR18945:SF784; ACETYLCHOLINE RECEPTOR SUBUNIT BETA-LIKE 1; 1.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 2.
DR   Pfam; PF02932; Neur_chan_memb; 2.
DR   PRINTS; PR00254; NICOTINICR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 2.
DR   SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 2.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 2.
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   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        914..938
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        950..968
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        980..999
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        1175..1197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        1407..1430
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        1442..1460
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        1472..1495
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        1669..1691
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          707..914
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          921..1189
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
FT   DOMAIN          1202..1406
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          1413..1631
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1101..1124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1580..1603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1753..1832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1580..1597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1756..1773
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2119 AA;  234710 MW;  58C7C767CF409A22 CRC64;
     GSDAPPSAHL SKQRRRREHQ SLIKSPGSEI LPDNLQSDVG QIPIPGPPAP VRTELVRPGR
     QADTCSSCSA SDILASIKGA AVPALLPVRG QIGALDQPGA VHDALAGPRT EFGGFGEAVQ
     VATARQAALQ PALGWHCQSR AAGCSRTARS PPTRCGAPNR RRSRHRRWSR RPLRQDTAVA
     AAFAIVVDVL AGGEAHDVDL GPRPYRGADR PAGSTKKIDF NARLNAGSRN DKEAAHADVA
     GGSVQAAEHR LPVIEGVHSA EVERQPVAQA AQEAAVRHVL EVGLPLVEPQ QRGGQAGPAG
     LRQAEGGGPQ SGAEVVRRLH QAAAPQLLGA VSERVADAEG QGGELLQVAV DFLLLHDGLA
     EQVALHQKHH LGEGEQEAAQ HEGGPEEPQR QRGGEDCPLQ AANAGVGNEL AQLGEPRVHR
     LLLLLLLLLL LLLLEGAFNW AVLENSVFKQ VRCQFTKAAS DGALQSLGAN KSRTAGRVRG
     AGVSQQTVDV APSPRLSPPT VGLGADDVAC QLESPTAQQI ARTGQAGAMI ERRVGDSLVA
     DLEGGAQQAS VRRVDLSLER VSALYNRTVS ITAWNSAALW RSGRASDCRT DLIERKAAQA
     SPRRRRRSSR TSEPDRRDEL KAACGVCEAA RLPSLLFGPE GLTRYASSSL LPPPALTVCR
     KLPNSLAMRW APLPTPRLAS CLIAACFCVR LSLQVRESGL GSDDEVKLVN LLFKHKGYNR
     LIRPVADLNQ TVKVAFGLAM VQLINVEEKS QIMKSNVWLR MTWDDYQLRW DPTDFGGIKV
     IRVNPNKIWK PDIVLYNNAD GKYEVSWQPN ILIFNTGNIL WIPPAIYKSS CTIHVRYFPF
     DQQECEMKFG SWTFDATQVG LDWYEGVKFM DLNDYWQSGS WDIIDCPGNI TQIEKVGQAP
     QTMMIYTITI RRKTLFYTVN LIIPCVLISL LSVCVFYLPA DAGEKMTLCI SILLALVVFL
     LLVSKILPPT SISIPLISKY LLFTFIMNII TIVFTVIIIN WNFRTPRTHK MPNWVRLVFL
     KYLPKLLWMK RPEHIKREEN DNWRMDRMTD RCNGGETGGG VSRRRRRDLH SFEDVTGGGL
     DFGVNDDDDV EPSPELLELR DFRRSGRSSM PPEETAEAAE AAGPQRFAGV EVTPELRKAI
     AAINFISTHL RIEDEYKRVL QDWKYVASVI DRVQLLIFGV VTLVGTGAIL LNAPFILDFE
     VRLAHLLFQH KGYNRLIRPV TSLNATVKVE FTLSIIQIIN VEEKAQIMKS NVWLKLSWYD
     YQLRWDPKDF GGVSIIRVHP DRAWNPDIVL FNNADGKYET SWLPNILIYS SGYIMWMPPA
     IYQSTCTIHV RYFPFDQQEC EMKFGSWTFD ATQVMLDGPG VADMNSYWKS GSWDIIDCPG
     NVTKIEKVGQ APQTMMIYTI TIRRKTLFYT VNLIIPCVLI SLLSVCVFYL PADAGEKMTL
     CISILLALVV FLLLVSKILP PTSISIPLIS KFLLFTFIMN TITIVFTVII INWNFRTPRT
     HKMPNWVRLV FLKYLPQVLL MKRPEHIDQE EADKWRMDRM TDADKCNGGG GDTADLGADR
     QRQAQHIGAV PSSSFDAGFD SSGGLYDQQQ PQQQPEQPPR GLRGLRVTPE LQKSVAAINL
     IATHLRIEDE NRCHIDPPPP TRSPRMPADE SPVLQDWKYV ASVIDRIQLV IFSTVTVIGT
     IAILMNAPFI LDFVQQEAVV TELKNRFEKF SRHSTHIESG CWQGPQLKDE GQSAALRNSL
     HEDPTLWLER GKSESASLGH SPQKVTTPSL VRGASIGQKP VGVSRRSPLA SPARSLQLEQ
     QRLRAASPRP DDMASQSKSP PTQSRRPHQA PCPRVERGIG LAAWTAAHSE RRTQHGRIRS
     VQLPLQSSSS SHQVVGNVRH EAAEVQEPLA TGRHDCRVQH EADSRCCCRQ AIQQPLSAFS
     RRRRRRQQPT IIQLHRRKAL QMLFMIDNIL HVVFGAHEHW RSLVNIGWHN LQDAATTGGG
     LTARLLHDEG HGDALVQQAQ FALRRVLSGR IHEDAAVADG PVHVRHHAAD VAGSVQLLAR
     LRVLLAVHSI SGTNHLVARL QGVFGANRAI AKSAEHTEDA ADGHQAVNHV DEEIIGQHIQ
     LLDIFTLDIL TTSHAKPMQ
//
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