GLR36_ARATH
ID GLR36_ARATH Reviewed; 903 AA.
AC Q84W41; Q9SD01;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Glutamate receptor 3.6;
DE AltName: Full=Ligand-gated ion channel 3.6;
DE Flags: Precursor;
GN Name=GLR3.6; OrderedLocusNames=At3g51480; ORFNames=F26O13.120;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23969459; DOI=10.1038/nature12478;
RA Mousavi S.A., Chauvin A., Pascaud F., Kellenberger S., Farmer E.E.;
RT "GLUTAMATE RECEPTOR-LIKE genes mediate leaf-to-leaf wound signalling.";
RL Nature 500:422-426(2013).
CC -!- FUNCTION: Glutamate-gated receptor that probably acts as non-selective
CC cation channel. Mediates leaf-to-leaf wound signaling. May be involved
CC in light-signal transduction and calcium homeostasis via the regulation
CC of calcium influx into cells. {ECO:0000269|PubMed:23969459}.
CC -!- SUBUNIT: May form heteromers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in roots and siliques.
CC {ECO:0000269|PubMed:12082126}.
CC -!- DISRUPTION PHENOTYPE: Reduced wound-activated surface potential changes
CC (WASP) duration in the systemic leaves, resulting in a decreased
CC induction of the regulators of jasmonate-signaling. Glr3.3 and glr3.6
CC double mutant has no detectable changes in surface potential in
CC systemic leaves and the induction of the regulators of jasmonate-
CC signaling is more strongly decreased. {ECO:0000269|PubMed:23969459}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB63012.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL133452; CAB63012.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78797.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64332.1; -; Genomic_DNA.
DR EMBL; BT004264; AAO42266.1; -; mRNA.
DR PIR; T45779; T45779.
DR RefSeq; NP_001326369.1; NM_001339518.1.
DR RefSeq; NP_190716.3; NM_115007.4.
DR AlphaFoldDB; Q84W41; -.
DR SMR; Q84W41; -.
DR BioGRID; 9629; 7.
DR STRING; 3702.AT3G51480.1; -.
DR TCDB; 1.A.10.1.24; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR PaxDb; Q84W41; -.
DR PRIDE; Q84W41; -.
DR EnsemblPlants; AT3G51480.1; AT3G51480.1; AT3G51480.
DR EnsemblPlants; AT3G51480.4; AT3G51480.4; AT3G51480.
DR GeneID; 824311; -.
DR Gramene; AT3G51480.1; AT3G51480.1; AT3G51480.
DR Gramene; AT3G51480.4; AT3G51480.4; AT3G51480.
DR KEGG; ath:AT3G51480; -.
DR Araport; AT3G51480; -.
DR TAIR; locus:2081805; AT3G51480.
DR eggNOG; KOG1052; Eukaryota.
DR HOGENOM; CLU_007358_0_1_1; -.
DR InParanoid; Q84W41; -.
DR OMA; TMDMELF; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q84W41; -.
DR PRO; PR:Q84W41; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84W41; baseline and differential.
DR Genevisible; Q84W41; 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; ISS:UniProtKB.
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:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; IMP:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0009864; P:induced systemic resistance, jasmonic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IMP: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 Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..903
FT /note="Glutamate receptor 3.6"
FT /id="PRO_0000011610"
FT TOPO_DOM 26..576
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..606
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..627
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 628..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..821
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 843..903
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 881..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 903 AA; 100530 MW; 4070A8CFDCDEE580 CRC64;
MKWFLLMLII CNAVPLQGLT KIVSARPQVV NIGSVFTFNS LIGKVIKVAM DAAVEDVNAS
PSILNTTTLR IIMHDTKYNG FMSIMEPLQF MESETVAIIG PQRSTTARVV AHVATELKIP
ILSFSATDPT MSPLQFPFFI RTSQNDLFQM AAIADIVQFY GWREVVAIYG DDDYGRNGVA
ALGDRLSEKR CRISYKAALP PAPTRENITD LLIKVALSES RIIVVHASFI WGLELFNVAR
NLGMMSTGYV WIATNWLSTI IDTDSPLPLD TINNIQGVIT LRLHTPNSIM KQNFVQRWHN
LTHVGLSTYA LYAYDTVWLL AQAIDDFFKK GGNVSFSKNP IISELGGGNL HLDALKVFDG
GKIFLESILQ VDRIGLTGRM KFTSDRNLVN PAFDVLNVIG TGYTTIGYWF NHSGLSVMPA
DEMENTSFSG QKLHSVVWPG HSIKIPRGWV FSNNGRHLRI GVPNRYRFEE VVSVKSNGMI
TGFCVDVFIA AINLLPYAVP FELVAFGNGH DNPSNSELVR LITTGVYDAG VGDITIITER
TKMADFTQPY VESGLVVVAP VRKLGSSAMA FLRPFTPQMW LIAAASFLIV GAVIWCLEHK
HNDEFRGPPR RQVITTFWFS FSTLFFSHRE TTTSNLGRIV LIIWLFVVLI INSSYTASLT
SILTVHQLSS PIKGIETLQT NHDPIGYPQG SFVRDYLIHE LNIHVSRLVP LRSPEEYDKA
LRDGPGKGGV AAVVDERAYI ELFLSNRCEF GIVGQEFTKN GWGFAFPRNS PLAVDVSAAI
LQLSENGDMQ RIRDKWLLRK ACSLQGAEIE VDRLELKSFW GLFVVCGVAC VLALAVYTVL
MIRQFGQQCP EEAEGSIRRR SSPSARIHSF LSFVKEKEED AKARSSRERQ LEDISANGSS
RCN
