ID A0A2P5CC14_TREOI Unreviewed; 886 AA.
AC A0A2P5CC14;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glutamate receptor {ECO:0000256|PIRNR:PIRNR037090};
GN ORFNames=TorRG33x02_290850 {ECO:0000313|EMBL:PON58600.1};
OS Trema orientale (Charcoal tree) (Celtis orientalis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Trema.
OX NCBI_TaxID=63057 {ECO:0000313|EMBL:PON58600.1, ECO:0000313|Proteomes:UP000237000};
RN [1] {ECO:0000313|Proteomes:UP000237000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glutamate-gated receptor that probably acts as non-selective
CC cation channel. {ECO:0000256|PIRNR:PIRNR037090}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000256|ARBA:ARBA00008685, ECO:0000256|PIRNR:PIRNR037090}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PON58600.1}.
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DR EMBL; JXTC01000384; PON58600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5CC14; -.
DR STRING; 63057.A0A2P5CC14; -.
DR InParanoid; A0A2P5CC14; -.
DR OrthoDB; 1011589at2759; -.
DR Proteomes; UP000237000; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR CDD; cd13686; GluR_Plant; 1.
DR CDD; cd19990; PBP1_GABAb_receptor_plant; 1.
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; IPR044440; GABAb_receptor_plant_PBP1.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR InterPro; IPR001320; Iontro_rcpt_C.
DR InterPro; IPR017103; Iontropic_Glu_rcpt_pln.
DR InterPro; IPR028082; Peripla_BP_I.
DR PANTHER; PTHR18966:SF508; GLUTAMATE RECEPTOR 2.9-LIKE ISOFORM X1; 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 PIRSF; PIRSF037090; Iontro_Glu-like_rcpt_pln; 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR037090-50};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|PIRNR:PIRNR037090};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|PIRNR:PIRNR037090};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286,
KW ECO:0000256|PIRNR:PIRNR037090};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037090};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR037090};
KW Reference proteome {ECO:0000313|Proteomes:UP000237000};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037090}.
FT TRANSMEM 498..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 558..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 740..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 371..720
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DISULFID 667..724
FT /evidence="ECO:0000256|PIRSR:PIRSR037090-50"
SQ SEQUENCE 886 AA; 100109 MW; 8E3E030C2F0EACFE CRC64;
MKDKDIHAII GPERSMQAKF VISLGEKSRV PIISFSATSP SVSPTHNPFF IRTTQDDSSQ
VQAIASIVQK YGWREVVLIY EDTEYGNGLI PYLTDAFQHI NTQVSYRSVI SPSTNSNYQE
QIAKELSKIM ARETRVLVVH MIASLGSELF RQAAEIGMMS EGFAWIISDG LSTLLDPVSK
DVTLSSMQGV LGVRPHVPMS KGLKDFKMRY FNTIRKNANQ INLFGLWAYD TIWALARAVE
SVGKMNISSG SRKSVWKNGS EPFGLVRVSK LGPMLLETLE RTKFKGLSGK FHLKGRQLQH
VAYEIFNVIG KREKVIGYWR ADKGTISHDL AKYSSNTTSM KDEVLKAIAW PGLTRVPPKG
WVIPLVGQKL KIGVPVTNGF KEFFQVKWDP RTDEPTFSGL SYDIFLAVLD KLPFAVPCEF
IPYANSSREM LGTYNELVYQ IKLEKYDAVV GDVTINANRT SYVDFTLPYS ESGISMVVKI
KEEEKNIWIF LKPLSWDLWL TTGGAFIFTG FVVWVFEYRT NTEFRGPLNQ QLGTVFWFSF
STLVFAHREK VKNNWSRLVL IIWIFVVLIL TQSYTASLAS MLTVQRLQPA VVDVNELKRN
GDFVGYSSNS FVRGFLIEQL NFNESKLRPY STPKEYHDAL SKGSKQGGVD AIFDEIPYIK
LFLARYCSQY TMVGPTYKSN GFGFAFPLGS PLVSYISRAI LKVTEDHIKM RELEQKYLGD
TDSCQNQDSK FSSDGSSLNL YSFGGLFIIT GLASGFSFLI FLVKFHRKHW PAVNANHSES
SIWSRVATMA KHFDNRVTPL HDSNNRTESN AGAEVLPINN SNFQNHSTRF SRDVEMGASA
NDEQEDNHNF QNHSMTSFSQ DVETTVIDEQ EENHSIDSRL FIYGGS
//
