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Database: UniProt
Entry: I1IQA7_BRADI
LinkDB: I1IQA7_BRADI
Original site: I1IQA7_BRADI 
ID   I1IQA7_BRADI            Unreviewed;       953 AA.
AC   I1IQA7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Glutamate receptor {ECO:0000256|PIRNR:PIRNR037090};
GN   ORFNames=BRADI_4g30820v3 {ECO:0000313|EMBL:KQJ90319.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ90319.1};
RN   [1] {ECO:0000313|EMBL:KQJ90319.1, ECO:0000313|EnsemblPlants:KQJ90319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ90319.1,
RC   ECO:0000313|EnsemblPlants:KQJ90319};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQJ90319.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ90319.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQJ90319}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ90319};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
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}.
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DR   EMBL; CM000883; KQJ90319.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1IQA7; -.
DR   STRING; 15368.I1IQA7; -.
DR   EnsemblPlants; KQJ90319; KQJ90319; BRADI_4g30820v3.
DR   Gramene; KQJ90319; KQJ90319; BRADI_4g30820v3.
DR   eggNOG; KOG1052; Eukaryota.
DR   HOGENOM; CLU_007358_0_2_1; -.
DR   InParanoid; I1IQA7; -.
DR   OMA; WHRTIAT; -.
DR   OrthoDB; 1011589at2759; -.
DR   Proteomes; UP000008810; Chromosome 4.
DR   ExpressionAtlas; I1IQA7; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IBA:GO_Central.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
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; -; 3.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR044440; GABAb_receptor_plant_PBP1.
DR   InterPro; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR000337; GPCR_3.
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   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR18966:SF445; GLUTAMATE RECEPTOR; 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   PIRSF; PIRSF037090; Iontro_Glu-like_rcpt_pln; 1.
DR   PRINTS; PR00248; GPCRMGR.
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   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:UP000008810};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..953
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014095452"
FT   TRANSMEM        583..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        643..667
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        823..844
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          456..803
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   REGION          854..880
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          887..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..880
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        888..906
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   953 AA;  105298 MW;  FB5D217D42B86DF2 CRC64;
     MEKAPRAILF LLLIVHFGVA TTSKGGEFHV GVILDLGSLV GKVARTSVAL AVEDFYSVHP
     NYSTKLVLHI RDSMGSDVQA ASAAIELLEN HKVQAIIGPQ KSSEAVFISN IGNITQVPTV
     SFTATSPSLT SDSMPYFVRA TLNDSAQVNS IALLIKAYGW REVVPVYDDT DYGRGILPSL
     VDALQEIDAR VPYRSVVPSS ATSEIITQEL YKLKAMQTRV FIVHMSPTMT SLLFTKAKEV
     GMMNKGFVWI TTDGISNIID SLNPSVIEAM NGVLGVRYHF PKSNELDNFS IKWNRMYQRD
     NPDESPFNKL SIVGLWGYDT IRALAQAAEK AGISSATNQQ PQSIKNSTCL ESMVISTNGP
     DILTAIVQNK FRGISGDFDL TNRQLKVSVF QIINVVGRGW REIGFWTVNG GLSRQFNQTG
     MKITEPASLI DLNPVIWPGE STETPRGWEI PTVGKKLRVG VRTSIYQELI KTFKDPVTDA
     TKASGLTVDI FEEAVKRLPF ALTYDYEAFD SADPPSTGSY DDFVNQVYLQ KYDIAVADTT
     ITYNRSLYVD FTVPYTESGV GMIVPVKESM IKNMWIFLKP LSAGMWFGGI IFFMYTGVVV
     WFLEYLNGNE HIHGPFSLKQ LGITMFFSIS EEKEKLERVL SRIVIRVWMF VLLVLTSSYT
     ASFASMLTVH QLSPTVTDVH ELQKKGEYVG FHNGSYVGGL LLDIGFDRSK IRAYDTPDDL
     YGALSKGSKN GGIAALVLEA PYIKHFLAKY NKGYTMVGPI YKSAGFAFAL PKNSPLRAEI
     SRAILSITGG DTIIQIEKKW VDHNSHQNDD TIDGSDAITF QSFGGLFLLT GIVTACSLFV
     AVLMNHYKKY QKNAASRGDN QNECGHEKRG ESGDSQGEQR DQNINDIEKQ EPLQVSHSLN
     TNGDKLPDSE NNDICCRCTQ NNKATSLTHI GSEIIHRGDK STRSLSGSKL VPS
//
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