GLR11_ARATH
ID GLR11_ARATH Reviewed; 808 AA.
AC Q9M8W7; Q9ZT37;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Glutamate receptor 1.1;
DE Short=AtGLR1;
DE AltName: Full=Ligand-gated ion channel 1.1;
DE Flags: Precursor;
GN Name=GLR1.1; Synonyms=GLR1; OrderedLocusNames=At3g04110; ORFNames=T6K12.27;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9823891; DOI=10.1038/24066;
RA Lam H.-M., Chiu J.C., Hsieh M.-H., Meisel L., Oliveira I.C., Shin M.,
RA Coruzzi G.M.;
RT "Glutamate-receptor genes in plants.";
RL Nature 396:125-126(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11379626; DOI=10.1126/science.292.5521.1486b;
RA Lacombe B., Becker D., Hedrich R., DeSalle R., Hollmann M., Kwak J.M.,
RA Schroeder J.I., Le Novere N., Nam H.G., Spalding E.P., Tester M.,
RA Turano F.J., Chiu J., Coruzzi G.;
RT "The identity of plant glutamate receptors.";
RL Science 292:1486-1487(2001).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=12082126; DOI=10.1093/oxfordjournals.molbev.a004165;
RA Chiu J.C., Brenner E.D., DeSalle R., Nitabach M.N., Holmes T.C.,
RA Coruzzi G.M.;
RT "Phylogenetic and expression analysis of the glutamate-receptor-like gene
RT family in Arabidopsis thaliana.";
RL Mol. Biol. Evol. 19:1066-1082(2002).
RN [7]
RP FUNCTION.
RX PubMed=12738881; DOI=10.1073/pnas.1030961100;
RA Kang J., Turano F.J.;
RT "The putative glutamate receptor 1.1 (AtGLR1.1) functions as a regulator of
RT carbon and nitrogen metabolism in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:6872-6877(2003).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15564521; DOI=10.1093/pcp/pch159;
RA Kang J., Mehta S., Turano F.J.;
RT "The putative glutamate receptor 1.1 (AtGLR1.1) in Arabidopsis thaliana
RT regulates abscisic acid biosynthesis and signaling to control development
RT and water loss.";
RL Plant Cell Physiol. 45:1380-1389(2004).
RN [9]
RP FUNCTION.
RX PubMed=18625242; DOI=10.1016/j.jmb.2008.06.076;
RA Tapken D., Hollmann M.;
RT "Arabidopsis thaliana glutamate receptor ion channel function demonstrated
RT by ion pore transplantation.";
RL J. Mol. Biol. 383:36-48(2008).
CC -!- FUNCTION: Glutamate-gated receptor that probably acts as non-selective
CC cation channel. Can transport sodium, potassium, and calcium ions.
CC Functions as a carbon and nitrogen regulator and/or sensor that
CC regulates carbon and nitrogen metabolism and distinct physiological
CC process such as germination through the control of acid abscisic (ABA)
CC biosynthesis. May be involved in light-signal transduction and calcium
CC homeostasis via the regulation of calcium influx into cells. Seems
CC required for the regulation of the abscisic acid (ABA) signaling
CC pathway that modulates many aspects of plant physiology such as seed
CC germination and response to drought (e.g. stomata opening).
CC {ECO:0000269|PubMed:12738881, ECO:0000269|PubMed:15564521,
CC ECO:0000269|PubMed:18625242}.
CC -!- SUBUNIT: May form heteromers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in roots. First detected in
CC the root-shoot junction, and later in lateral roots and at the margin
CC of matures leaves. {ECO:0000269|PubMed:12082126}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to exogenous abscisic acid
CC (ABA) and higher ABA levels in leaves. {ECO:0000269|PubMed:15564521}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
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DR EMBL; AF079998; AAD09173.1; -; mRNA.
DR EMBL; AC016829; AAF26802.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74038.1; -; Genomic_DNA.
DR EMBL; AK117584; BAC42242.1; -; mRNA.
DR PIR; T51138; T51138.
DR RefSeq; NP_187061.1; NM_111282.3.
DR AlphaFoldDB; Q9M8W7; -.
DR SMR; Q9M8W7; -.
DR BioGRID; 4901; 26.
DR IntAct; Q9M8W7; 15.
DR STRING; 3702.AT3G04110.1; -.
DR TCDB; 1.A.10.1.7; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR PaxDb; Q9M8W7; -.
DR PRIDE; Q9M8W7; -.
DR ProteomicsDB; 248597; -.
DR EnsemblPlants; AT3G04110.1; AT3G04110.1; AT3G04110.
DR GeneID; 819566; -.
DR Gramene; AT3G04110.1; AT3G04110.1; AT3G04110.
DR KEGG; ath:AT3G04110; -.
DR Araport; AT3G04110; -.
DR TAIR; locus:2102975; AT3G04110.
DR eggNOG; KOG1052; Eukaryota.
DR HOGENOM; CLU_007358_0_2_1; -.
DR InParanoid; Q9M8W7; -.
DR OMA; SEIMNFT; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q9M8W7; -.
DR PRO; PR:Q9M8W7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M8W7; baseline and differential.
DR Genevisible; Q9M8W7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; IDA:TAIR.
DR GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0005272; F:sodium channel activity; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR GO; GO:0030003; P:cellular cation homeostasis; IDA:TAIR.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; IDA:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; IDA:UniProtKB.
DR CDD; cd19990; PBP1_GABAb_receptor_plant; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR044440; GABAb_receptor_plant_PBP1.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR017103; Iontropic_Glu_rcpt_pln.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 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; SSF53822; 1.
PE 2: Evidence at transcript level;
KW Abscisic acid signaling pathway; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..808
FT /note="Glutamate receptor 1.1"
FT /id="PRO_0000011592"
FT TOPO_DOM 20..541
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 624..771
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 772..792
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 793..808
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 564
FT /note="S -> P (in Ref. 1; AAD09173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 808 AA; 90509 MW; 9E556E313865A598 CRC64;
MEILFSISIL ALLFSGVVAA PSDDDVFEEV RVGLVVDLSS IQGKILETSF NLALSDFYGI
NNGYRTRVSV LVRDSQGDPI IALAAATDLL KNAKAEAIVG AQSLQEAKLL ATISEKAKVP
VISTFLPNTL SLKKYDNFIQ WTHDTTSEAK GITSLIQDFS CKSVVVIYED ADDWSESLQI
LVENFQDKGI YIARSASFAV SSSGENHMMN QLRKLKVSRA SVFVVHMSEI LVSRLFQCVE
KLGLMEEAFA WILTARTMNY LEHFAITRSM QGVIGFKSYI PVSEEVKNFT SRLRKRMGDD
TETEHSSVII GLRAHDIACI LANAVEKFSV SGKVEASSNV SADLLDTIRH SRFKGLSGDI
QISDNKFISE TFEIVNIGRE KQRRIGLWSG GSFSQRRQIV WPGRSRKIPR HRVLAEKGEK
KVLRVLVTAG NKVPHLVSVR PDPETGVNTV SGFCVEVFKT CIAPFNYELE FIPYRGNNDN
LAYLLSTQRD KYDAAVGDIT ITSNRSLYVD FTLPYTDIGI GILTVKKKSQ GMWTFFDPFE
KSLWLASGAF FVLTGIVVWL VERSVNPEFQ GSWGQQLSMM LWFGFSTIVF AHREKLQKMS
SRFLVIVWVF VVLILTSSYS ANLTSTKTIS RMQLNHQMVF GGSTTSMTAK LGSINAVEAY
AQLLRDGTLN HVINEIPYLS ILIGNYPNDF VMTDRVTNTN GFGFMFQKGS DLVPKVSREI
AKLRSLGMLK DMEKKWFQKL DSLNVHSNTE EVASTNDDDE ASKRFTFREL RGLFIIAGAA
HVLVLALHLF HTRQEVSRLC TKLQSFYK
