ID A0A183SXY3_SCHSO Unreviewed; 1067 AA.
AC A0A183SXY3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Glutamate receptor {ECO:0000313|WBParaSite:SSLN_0000943001-mRNA-1};
GN ORFNames=SSLN_LOCUS9081 {ECO:0000313|EMBL:VDL95466.1};
OS Schistocephalus solidus (Tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0000943001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SSLN_0000943001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL95466.1, ECO:0000313|Proteomes:UP000275846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NST_G2 {ECO:0000313|EMBL:VDL95466.1,
RC ECO:0000313|Proteomes:UP000275846};
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}.
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 EMBL; UYSU01035029; VDL95466.1; -; Genomic_DNA.
DR STRING; 70667.A0A183SXY3; -.
DR WBParaSite; SSLN_0000943001-mRNA-1; SSLN_0000943001-mRNA-1; SSLN_0000943001.
DR Proteomes; UP000050788; Unplaced.
DR Proteomes; UP000275846; Unassembled WGS sequence.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.40.50.2300; -; 4.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_Glu_rcpt_met.
DR InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR InterPro; IPR001320; Iontro_rcpt_C.
DR InterPro; IPR028082; Peripla_BP_I.
DR PANTHER; PTHR18966:SF600; GLUTAMATE RECEPTOR 1-RELATED; 1.
DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000275846};
KW Signal {ECO:0000256|SAM:SignalP}; Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1067
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041079990"
FT TRANSMEM 616..635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 882..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 479..853
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 489..560
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
FT REGION 292..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1067 AA; 120150 MW; 471EA26CB47105D5 CRC64;
MSTNSAIHGL WLIGLLRLAI LVLCDMQELN VGFIIEGPAE RQTQVIQKAI TAANRKLAEL
LAGQPHQVTL VPLIKRIDTR NAFAATKAAI EKIVYFQANK VLTEYQLLLK ACDLLMNQVI
TVFGPGSTPA STPSLRITQK YSIPYVVIQW SDDDSLQNYS INLHPSYNEV GRVLRKFIEE
AEDWKQLGII YAKEEGKTMK NYGLEKFESL LSHFKGEVIM RKWHTNDMAH KYVIKYFRTT
MSHFRFLVDI PHSEIPEFLD LDTQFLDPKT FAVDKGANFS AISLTNVLSQ QFQSPPQHDI
NRQTSARSRK TGADSGPEAA SGRESLTYYL LLYDTLHVMA VGISRFISTN SLAIQPPLGL
SCSSGDTWSQ GPLLLESIKS VGPDDVNGFT GYIQFDEQGR RKGLNISVLE INRDGFQEVS
YSLDLKKPSL PAFGCTVLRC HATGQILKFG YWNEIEEFVV TKKFAETQAE IQKELTGQTL
RVTTIEDTPF IMYKGNLTAD GQKSMDPKDW HGFCIDLLNE CAAALHFNYT VHPVAHGSYG
KAEIIDGVEV WDGIIGELQF KRADLAVAML TINYEREKVI DFTTPFMNLG VSIIFKKPVG
TQVDLFSFLR PLSPPVWGYV LIAYVGVSMA LFFVARFSPY EWRNPHPCNA DSEVLENSFN
MLNSLWFTLG SLMQKGSDIL PRATSTRIVA GFWWFFTLII ISSYTANLAA FLTVERMKAP
IEDVNDLAKQ TKIKYGTREG GSSAAFFEKS NLSVYQRMWQ FMSSNKNVMM NSTTEAIARV
KRGGYAYILE SSVNEYYTQR NCELMQVGNN LDSKGYGIGF PQGSKYRDSF SEVILQLQRS
QTLEQMRRYW WGNYSIVEPC NDQPKKSADA TSLGVEQVGG CFVMVLIGLA ASFLVGLAEF
LYKAYQRSKI TKASQYTFIT SPNLGNLIDD ALRLISKMQH QTQMSSPKRS MHEEVAREFR
FSMARSSTRD VAAESALKLP QPPSKCIPTK ECRSAAMAYA PCLPATVRPA GYRSSSARFS
DRRLSVFDVT LLHRRCSSNR RSRSSTSSQM NTGLHTHLSL LYMYLRK
//
