ID T1KDA9_TETUR Unreviewed; 925 AA.
AC T1KDA9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Ionotropic glutamate receptor C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=107363262 {ECO:0000313|EnsemblMetazoa:tetur09g02270.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur09g02270.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur09g02270.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000256|ARBA:ARBA00008685}.
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DR EMBL; CAEY01002011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015785947.1; XM_015930461.1.
DR AlphaFoldDB; T1KDA9; -.
DR EnsemblMetazoa; tetur09g02270.1; tetur09g02270.1; tetur09g02270.
DR GeneID; 107363262; -.
DR KEGG; tut:107363262; -.
DR eggNOG; KOG1052; Eukaryota.
DR HOGENOM; CLU_007257_1_1_1; -.
DR OrthoDB; 1011589at2759; -.
DR Proteomes; UP000015104; 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 GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProt.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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 InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR18966:SF349; FI04462P-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 Pfam; PF00497; SBP_bac_3; 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.
PE 3: Inferred from homology;
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:UP000015104};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW 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 TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 650..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 840..863
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 443..818
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 453..518
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
SQ SEQUENCE 925 AA; 105225 MW; 89495FCDB1CE4AF3 CRC64;
MFNLYCNKDS TIKEMNFQII GKFLLLLTVI QSGFGLPETL NIGGLFTVNS LDQDLAFQVA
IQKVLNDFNR FSSATVQGIK YNVSYFDSYQ AQSNVCKLLQ EQVAAIIDTT SSPCSHHIEA
ICDNYEIPHI RTRYDWRQSM GTFSINLYPH PLRIAHATID LIIELGWKEF AVLFEDDEDT
AFVNELFKET QKEYEQMIGF PVNRLDWTIG VYQFSSVDSY RDTFGLVRRS QYKNIILHVK
SDNLYDALKQ GQQIGLMTDE YSFILTSLDL HAIDLKDFKY SGAKIHSYRI VDTNSEESRQ
FIHDWENLAQ EMGIEPSETS NNFKTETGLV YDAVLLVSNA IKEAEKTMQV EPTSLSCEEP
LTWSQGTSIL NFLTANPMDG VTGRLFFDEE GYRSNVVLHL YELSNEGFNR LGFWSDINKK
GLEIENKQPK YYNPSENAIK DRMLKVVTVE EKGYTMIKND RRPLEGNEKY EGYVIDLVEE
LSKFAGFNYE ISLFDSKAYG DCNKTSMTCT GMLGEITSDR AHLALVDLTI TAGRSEVVDF
THPFINTGIS VLFKKITKSE TQLFGFLSPF TYLVWCMITF TIIAVSISFH VIGRLSPYEW
VNPYPCRQDE PILENDLTQA NASWFIVAAL MQQGSEIAPR TLSTRWLAGV WYFFTLILVS
CYTANLAASL TIEDFNYPFS SAKDLITLDT PEVQAIKFGC KKSGSTLNFF KDSNDPIYRE
IYNRMMEHPE WLASTNDEGE ERVRESDFDY AFFMESATID YKLERNCSIV KIGGLLDHKG
YGIAVKRNSP LLRILNQGLL ALQESGQLRV LYDRWWKQRN GGGVCAAKAD TSAAVTSFKL
INVGGAFIVL LIGCGVALLI AFCELFTKLW NTSNDPVSFW EGVKNELRFA FNFQLATKQV
TKNENLIQRS ISEDKSSKIS NFSAK
//
