ID A0A090LAE9_STRRB Unreviewed; 628 AA.
AC A0A090LAE9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CEF65118.1, ECO:0000313|WBParaSite:SRAE_1000337100.1};
GN ORFNames=SRAE_1000337100 {ECO:0000313|EMBL:CEF65118.1,
GN ECO:0000313|WBParaSite:SRAE_1000337100.1,
GN ECO:0000313|WormBase:SRAE_1000337100};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF65118.1};
RN [1] {ECO:0000313|EMBL:CEF65118.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_1000337100.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF65118.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_1000337100.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) 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}.
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DR EMBL; LN609528; CEF65118.1; -; Genomic_DNA.
DR STRING; 34506.A0A090LAE9; -.
DR EnsemblMetazoa; SRAE_1000337100.1; SRAE_1000337100.1; WBGene00259988.
DR WBParaSite; SRAE_1000337100.1; SRAE_1000337100.1; WBGene00259988.
DR WormBase; SRAE_1000337100; SRP04847; WBGene00259988; -.
DR eggNOG; KOG3645; Eukaryota.
DR OMA; VEIRESH; -.
DR OrthoDB; 2872899at2759; -.
DR Proteomes; UP000035682; Chromosome X.
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; cd19031; LGIC_ECD_nAChR_proto_alpha-like; 1.
DR CDD; cd19064; LGIC_TM_nAChR; 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; 2.
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 PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR PANTHER; PTHR18945:SF895; NICOTINIC ACETYLCHOLINE RECEPTOR ALPHA3, ISOFORM B; 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:UP000035682};
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 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 268..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 298..321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 333..355
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 36..267
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 274..613
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT REGION 531..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 71911 MW; 11C0B71F146F469A CRC64;
MNWISNINTI KSFQIIIYLY ILIIPLPFIE GTKDASRLFE DLLSDYNKLV RPVDNTNDTV
VVNFKLKLSQ LLDVHEKNQI MTTNVWLQHS WIDSKLKWDP AEYGGVDVLY VPSDLIWLPD
VVLYNNADGN YQVSIMTKAK LSPNGTVEWA PPAIYKSMCQ IDIEWFPFDL QTCHLIFGSW
TYGGLEVNLK HKDWHLQREE QELVIGYDRE YNETVWIVDN GIDLSDYYPS VEWDILNVPG
KRHEKRYPCC ESPFIDLTYE IHLRRKTLFY TVNLIFPSVG ISFLTALVFY LPSDGGEKIS
LCILILISLT VFFLLLVEII PSTSLVIPLI GKYLLFTMVM VTLSVIVTVI TLNIHFRSPS
THTMPKWVRK VFIQVLPYYL LMRRPKKVVK EEESEVKNCK GILRNAMLIK KDEPEVKIKK
NSYSRRKSSF VNDRKFSMRS GHTSALFEQM DYLSPHYITN AMNSSSSSSS VINATGSCHD
TSINNNKSQP FGSTFGILTD PTNIGTSSNI TQETQQPLST SIKEHLKVGG QQNITSGSSN
NNNNSNNNNN NNNTKLYTPI QSAVDSVTYI AGHLRNEEEN QQVIEDWKYV SVVMDRIFLM
LFTFFCITGI IVIILRAPTI YDRTEALA
//
