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Database: UniProt
Entry: A2Z1H6_ORYSI
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Original site: A2Z1H6_ORYSI 
ID   A2Z1H6_ORYSI            Unreviewed;       946 AA.
AC   A2Z1H6;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Glutamate receptor {ECO:0000256|PIRNR:PIRNR037090};
GN   ORFNames=OsI_31459 {ECO:0000313|EMBL:EAZ09187.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946 {ECO:0000313|EMBL:EAZ09187.1, ECO:0000313|Proteomes:UP000007015};
RN   [1] {ECO:0000313|EMBL:EAZ09187.1, ECO:0000313|Proteomes:UP000007015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA   Samudrala R., Wang J., Wong G.K., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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; CM000134; EAZ09187.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2Z1H6; -.
DR   STRING; 39946.A2Z1H6; -.
DR   EnsemblPlants; BGIOSGA029716-TA; BGIOSGA029716-PA; BGIOSGA029716.
DR   Gramene; BGIOSGA029716-TA; BGIOSGA029716-PA; BGIOSGA029716.
DR   HOGENOM; CLU_007358_0_1_1; -.
DR   OMA; NPPHDMQ; -.
DR   Proteomes; UP000007015; Chromosome 9.
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; -; 3.
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   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR18966:SF450; GLUTAMATE RECEPTOR 2.8-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   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:UP000007015};
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..946
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002650668"
FT   TRANSMEM        585..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        638..658
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        825..847
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          456..802
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   REGION          909..946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        750..806
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037090-50"
SQ   SEQUENCE   946 AA;  105705 MW;  03954CFF95CD7BF9 CRC64;
     MERAPERAAI FFLLLSLTVA QYTTESGTGT LNVGVILHLK SLVGKMAHTS IMMAVEDFYA
     VHRSFKTKLV LHIRDSNGDD IQAASEAIDL LENYNVKAIV GPQKSSEATF VSDLGNKSQV
     PVISFTATNP TLSSIDVPYF LRGTLSDVAQ VNTIAALIKA YGWREVVPIY EDTDYGRGII
     PYLADALQEF GAYMPYRSAI SKSANTDQVE QELYKLMTMQ TRIYVVHMSV NIASILFTKA
     KELGMMSKGY AWILTDGISN IVNSLSPSIL EEINGAIGVR FYLPASKELH DFTARWNKRF
     KQDYPNDPPS QLSIFGLWGY DTTWALAQAA EKVNMADAIF QKQKDTKNTT SLGTLGISTI
     GPKLLDSILH SKFRGLSGEF DLRNRQREFS TFQIINVVGS RSKEIGFWTA KQGIFRQLNE
     NKTTNINSVP DLDPVMWPGE VYTVPKGWQI PTNGKKLRVG VRTSGYPELM KVEKNPVTNE
     VTASGYAIDV FEEVLRRLPY AIPYEYVAFD NGQGVNSGSY NDFVYQVHLG VYDTAIGDIT
     IRYNRTSYVD FTLPYTESGV AMIVPVKDDR DKNTWVFLKP LTTDLWFGSI AFFIYTAIVI
     WLLERRINNA ELTGSFFRQL GIAIYFSFFA DRERVDSILS RLVVIVWVFV LLVITSSYTA
     NLSSMLTVQQ LQPTVTDVHE LLKNGEYVGY HNGSYVGDLL KGLGFDRTKI RAYDNSDDFA
     EALTKGSQNG GIAAVVHEVP YIKIFLAKHC KGYTMVGPIY KSEGFGFAFP KRSPLVYDFS
     REILSILEGD SIIHIEKKWI GDQHACQNDG TVVGSSSLNF NSFSGLFLVT GVASTSALLI
     ALLMFLYKNK HRIRNSISRD QTRSRYGPEH INEQNEERVI DSSQVQNLQL TVPDDSEYTC
     QQEEEISIEL SPASGFQPSP DFASQEHRAV ASSTIIASSS SQTPRI
//
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