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Database: UniProt
Entry: I1H4H1_BRADI
LinkDB: I1H4H1_BRADI
Original site: I1H4H1_BRADI 
ID   I1H4H1_BRADI            Unreviewed;       945 AA.
AC   I1H4H1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Glutamate receptor {ECO:0000256|PIRNR:PIRNR037090};
GN   Name=100836921 {ECO:0000313|EnsemblPlants:KQK21239};
GN   ORFNames=BRADI_1g59600v3 {ECO:0000313|EMBL:KQK21239.1};
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:KQK21239.1};
RN   [1] {ECO:0000313|EMBL:KQK21239.1, ECO:0000313|EnsemblPlants:KQK21239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK21239.1,
RC   ECO:0000313|EnsemblPlants:KQK21239};
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:KQK21239.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK21239.1};
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:KQK21239}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK21239};
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; CM000880; KQK21239.1; -; Genomic_DNA.
DR   RefSeq; XP_003561526.1; XM_003561478.3.
DR   AlphaFoldDB; I1H4H1; -.
DR   STRING; 15368.I1H4H1; -.
DR   EnsemblPlants; KQK21239; KQK21239; BRADI_1g59600v3.
DR   GeneID; 100836921; -.
DR   Gramene; KQK21239; KQK21239; BRADI_1g59600v3.
DR   KEGG; bdi:100836921; -.
DR   eggNOG; KOG1052; Eukaryota.
DR   HOGENOM; CLU_007358_0_1_1; -.
DR   InParanoid; I1H4H1; -.
DR   OMA; AYKKHQI; -.
DR   OrthoDB; 1011589at2759; -.
DR   Proteomes; UP000008810; Chromosome 1.
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   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
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   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR18966:SF487; GLUTAMATE RECEPTOR 3.4; 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; PR01176; GABABRECEPTR.
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   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..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..945
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014094295"
FT   TRANSMEM        586..606
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        648..674
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        831..851
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          466..807
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   REGION          865..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          914..945
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..928
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..945
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        756..810
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037090-50"
SQ   SEQUENCE   945 AA;  101361 MW;  9BA22D47959033C6 CRC64;
     MADLLLLLLR VLCLCSVVPL AVAAARPGNV TIGALFTFNS VIGRSAAAAI DLAVADVNRD
     AAVLNGTRLS VVAQDTKCSG FVGTIQALQL MEKKVVAVVG PQSSGIAHVV SHVVNELHVP
     LLTFAATDPA LASSQYPYLL RAARGDDASQ MAAVADIVAF YGWRQVAAVY ADTDHGRGGV
     DALGDALEPH RARIALRAPF PPGAGSAAMA DLLVQVSLAE SRVIVVHVSP DSGLAVFSAA
     RSLGMMAAGY VWIATDWLAA AIDSSSSSSH PANHPKSTMG LIQGVLTLRR YSPDSPAKRA
     LAMASRSKHL NAYGLAAYDS VWTAARAIDA FLADGLDVTF SDDPRLQAEQ SGSNSTLRLG
     ALKVFDQGPR LLEKLLLSNS TGITGALRFG ADRSLVDPVY EVLNVGGTGV RRVGFWSNRT
     RLSLAAPDTK KNGSSSQQGL YSVIWPGETT ATPRGWVFPN NGRPLRIGVP WRTTYRQFVS
     KDGTSPDGAS GYCVDVFKAA VSLLPYPVPF SFVLFGDGEK NPSYGDLVSK VANDEFDAAV
     GDVSIVTNRT RVVDFTQPYV ESGLVIVSPV KEKNPNAWAF LKPFTGAMWA VTGAFFLFVG
     AVVWVLEHRF NPDFRGSPRK QLVTIFWFSF STMFFAHREN TVSTLGRMVL IIWLFVVLII
     NSSYTASLTS ILTVQQLSTG IQGLDGLIAS AEPIGYQVGS FAKSYMMEEL NVPESRLKEL
     AIDDYASSLQ LGPHNGGVAA IVDELPYVDL FLSTNCQFKT VGQEFTKSGW GFAFQRDSPL
     AVDLSTAILT LSENGDLQRI HDKWLNPGQC DGATQGADVT AAADRLNLGS FWGLFLISGV
     ACFLALLVYF ARILCQYGKY KLAGGEPPGE DDPSSSSSSV SPERKPPVRR PERLRSIREL
     MTFVDMKEAE VKRAIRRKSS DDGRRQPDRS IASSAGASSF SVSTV
//
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