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Database: UniProt
Entry: I1IQB0_BRADI
LinkDB: I1IQB0_BRADI
Original site: I1IQB0_BRADI 
ID   I1IQB0_BRADI            Unreviewed;       978 AA.
AC   I1IQB0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Glutamate receptor {ECO:0000256|PIRNR:PIRNR037090};
GN   Name=100836491 {ECO:0000313|EnsemblPlants:KQJ90322};
GN   ORFNames=BRADI_4g30850v3 {ECO:0000313|EMBL:KQJ90322.1};
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:KQJ90322.1};
RN   [1] {ECO:0000313|EMBL:KQJ90322.1, ECO:0000313|EnsemblPlants:KQJ90322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ90322.1,
RC   ECO:0000313|EnsemblPlants:KQJ90322};
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:KQJ90322.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ90322.1};
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:KQJ90322}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ90322};
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; KQJ90322.1; -; Genomic_DNA.
DR   RefSeq; XP_003576552.1; XM_003576504.3.
DR   AlphaFoldDB; I1IQB0; -.
DR   STRING; 15368.I1IQB0; -.
DR   EnsemblPlants; KQJ90322; KQJ90322; BRADI_4g30850v3.
DR   GeneID; 100836491; -.
DR   Gramene; KQJ90322; KQJ90322; BRADI_4g30850v3.
DR   KEGG; bdi:100836491; -.
DR   eggNOG; KOG1052; Eukaryota.
DR   HOGENOM; CLU_007358_0_2_1; -.
DR   InParanoid; I1IQB0; -.
DR   OMA; WTFMELA; -.
DR   OrthoDB; 1011589at2759; -.
DR   Proteomes; UP000008810; Chromosome 4.
DR   ExpressionAtlas; I1IQB0; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
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:SF566; 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   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:UP000008810};
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        595..613
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        655..671
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        833..855
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          472..811
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   REGION          931..978
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        759..814
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037090-50"
SQ   SEQUENCE   978 AA;  109120 MW;  FF92691BDBC19982 CRC64;
     MGAVSTLLQA EMRAVLSALL RVLRRHDFLR LVLVLLVFGS SGVTAQGGAR RQRQVVDVGV
     ILDMKTWLGN TSWACMEMAL EDFYANATQA RYRTRLKLHL RDTGPDAVDA ASAGVDLLKN
     VHVQAIVGPQ TSTQAKFLAE LGNKSSVPII SFSADCPSRS GQTPYFIRTA WNDSSQAEAI
     ASLVKKYNWR EVVPVFEDDD SNTRFIPDLV DALRQVDARV SYRCKIHPSA KEDDIRRAIS
     GLKYNWTSVF VVRMSHLLAF KFFQLAKDEG MMGQDFVWIT AYGLTDIFDV VGSPALDVMQ
     GVLGVKPHVQ DTVELQNFTR RWRKKHRLEN PGTSLSEPTV SGLYAYDTIW ALALAAEETR
     YNDSNFVSVT NNGSTDFERI GTSKAAEKLR GTLLKTNFQG MSGKFQIQDM QLLSSKYEII
     NIVGQEKRVA GFWTPEFSIS GNSSSMAELG TIIWPGGNKT PPRGWMLPMN KTLKIGVPVK
     PGFAEFVKFE NGIAKGFCID VFEAVVRELP YNVSCNYSEF GDGKVSKGTY DDLVYRVYLK
     EYDAVVGDIT ILANRSKYVD FTLPYTESGV RMLVPVRDQR QKTAWTFLKP LTTDLWLGTG
     AFFIFTGFVV WFIEHRTNKD FRGPPASQIG SVFYFSFSTL VFAHKERIVN NLSRIVLVVW
     LFVVLIVQQS YTASLSSILT VEQLQPTVTN LEEVIRKGSY VGYLNDSFLP GLLKRLKIDE
     SKMIAFDSPA EYNEALSTGK VAVIVDEIPY LKVFLSRYCQ NYTMIGPTYK FDGFGYAFPR
     GSPLTPDISR GILKFASDSK MVELQKTLYG DMSCPDKDDS QISSSLTLHS FQGLFIITGA
     SSMLALILHA VITVYNNQHD LSSDNSLTSW RRWLAIISKL FHEGDSPNTP DKDELAMANV
     DSIIESPLSI PNHVIERLDS GTDTGSLPEV EGTADRDLSV QDAEPTPSAY VHSERGHNGV
     ASLSRSGSSI RRRQRIME
//
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