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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//