GHR1_ARATH
ID GHR1_ARATH Reviewed; 1053 AA.
AC C0LGQ9; F4JIJ5; Q9SUB9; T1T4Z8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase GHR1 {ECO:0000303|PubMed:22730405};
DE EC=2.7.11.1 {ECO:0000269|PubMed:22730405};
DE AltName: Full=Protein GUARD CELL HYDROGEN PEROXIDE-RESISTANT 1 {ECO:0000303|PubMed:22730405};
DE Short=AtGHR1 {ECO:0000303|PubMed:22730405};
DE AltName: Full=Protein RADICAL-INDUCED CELL DEATH 7 {ECO:0000303|PubMed:30361234};
DE Flags: Precursor;
GN Name=GHR1 {ECO:0000303|PubMed:22730405};
GN Synonyms=RCD7 {ECO:0000303|PubMed:30361234};
GN OrderedLocusNames=At4g20940 {ECO:0000312|Araport:AT4G20940};
GN ORFNames=T13K14.100 {ECO:0000312|EMBL:CAB45889.1};
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], FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF
RP CYS-57; CYS-66; CYS-381 AND LYS-798, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, INTERACTION WITH SLAC1 AND ABI2, SUBCELLULAR LOCATION, AND
RP ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=22730405; DOI=10.1105/tpc.112.100107;
RA Hua D., Wang C., He J., Liao H., Duan Y., Zhu Z., Guo Y., Chen Z., Gong Z.;
RT "A plasma membrane receptor kinase, GHR1, mediates abscisic acid- and
RT hydrogen peroxide-regulated stomatal movement in Arabidopsis.";
RL Plant Cell 24:2546-2561(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] OF 17-1053.
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-704, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=27694184; DOI=10.1105/tpc.16.00131;
RA Horak H., Sierla M., Toldsepp K., Wang C., Wang Y.-S., Nuhkat M., Valk E.,
RA Pechter P., Merilo E., Salojaervi J., Overmyer K., Loog M., Brosche M.,
RA Schroeder J.I., Kangasjaervi J., Kollist H.;
RT "A dominant mutation in the HT1 kinase uncovers roles of MAP kinases and
RT GHR1 in CO2-induced stomatal closure.";
RL Plant Cell 28:2493-2509(2016).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-56; GLY-63; GLY-108;
RP ASP-220; ASP-293; ALA-618; ALA-637; SER-680 AND LYS-798, INTERACTION WITH
RP CPK3 AND SLAC1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP PHOSPHORYLATION AT SER-100; SER-102; SER-105; SER-126; SER-262; SER-278;
RP THR-280; SER-281; SER-325; TYR-406; SER-410; THR-415; SER-417; SER-434;
RP SER-613; SER-614; SER-616; THR-669; THR-675; SER-678; SER-680; SER-698;
RP SER-699; SER-700; THR-713; SER-716; SER-718; THR-720; SER-721; SER-724;
RP SER-760; THR-764; SER-769; THR-928; THR-1010; SER-1015; THR-1045; TYR-1047;
RP SER-1051 AND SER-1052.
RC STRAIN=cv. Columbia, and cv. Columbia GL1;
RX PubMed=30361234; DOI=10.1105/tpc.18.00441;
RA Sierla M., Horak H., Overmyer K., Waszczak C., Yarmolinsky D.,
RA Maierhofer T., Vainonen J.P., Denessiouk K., Salojaervi J., Laanemets K.,
RA Toldsepp K., Vahisalu T., Gauthier A., Puukko T., Paulin L., Auvinen P.,
RA Geiger D., Hedrich R., Kollist H., Kangasjaervi J.;
RT "The receptor-like pseudokinase GHR1 is required for stomatal closure.";
RL Plant Cell 30:2813-2837(2018).
RN [8]
RP FUNCTION.
RX PubMed=29463779; DOI=10.1126/scisignal.aam9514;
RA Devireddy A.R., Zandalinas S.I., Gomez-Cadenas A., Blumwald E., Mittler R.;
RT "Coordinating the overall stomatal response of plants: Rapid leaf-to-leaf
RT communication during light stress.";
RL Sci. Signal. 11:0-0(2018).
CC -!- FUNCTION: Receptor kinase acting as an early component in abscisic acid
CC (ABA) signaling (PubMed:22730405). Required for darkness, ABA, high
CC CO(2) and hydrogen peroxide (H(2)O(2)) induction of S-type anion
CC currents in guard cells leading to stomatal closure, possibly via the
CC phosphorylation and activation of the anion channel SLAC1 and as a
CC scaffolding component (PubMed:22730405, PubMed:27694184,
CC PubMed:30361234). Seems to act in parallel with SRK2E/OST1 in the ABA
CC signaling pathway which regulates stomatal movement (PubMed:22730405).
CC Binds ATP (PubMed:30361234). Involved in the local and/or systemic
CC stomatal responses (e.g. stomatal closure) to light stress
CC (PubMed:29463779). {ECO:0000269|PubMed:22730405,
CC ECO:0000269|PubMed:27694184, ECO:0000269|PubMed:29463779,
CC ECO:0000269|PubMed:30361234}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:22730405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:22730405};
CC -!- ACTIVITY REGULATION: Negatively regulated by ABI2.
CC {ECO:0000269|PubMed:22730405}.
CC -!- SUBUNIT: Interacts with SLAC1 (via N-terminus) (PubMed:22730405,
CC PubMed:30361234). Binds to ABI2, but not ABI1 (PubMed:22730405).
CC Interacts with CPK3 (PubMed:30361234). {ECO:0000269|PubMed:22730405,
CC ECO:0000269|PubMed:30361234}.
CC -!- INTERACTION:
CC C0LGQ9; C0LGL4: At2g28960; NbExp=2; IntAct=EBI-16939160, EBI-16946048;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22730405,
CC ECO:0000269|PubMed:30361234}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in guard cells and in the vasculature of
CC roots and leaves. {ECO:0000269|PubMed:22730405,
CC ECO:0000269|PubMed:30361234}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159,
CC ECO:0000303|PubMed:30361234}.
CC -!- PTM: Phosphorylated by HT1; this phosphorylation is inhibited by MPK12
CC and MPK4. {ECO:0000269|PubMed:27694184, ECO:0000269|PubMed:30361234}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions but early wilting (PubMed:22730405). Increased sensitivity
CC to drought stress due to impaired stomatal closure and increased water
CC loss (PubMed:22730405). Abolished CO(2)-mediated and darkness-induced
CC stomatal closure (PubMed:27694184). Defective abscisic acid (ABA) and
CC hydrogen peroxide (H(2)O(2)) induction of stomatal closure associated
CC with an impaired activation of S-type anion currents in guard cells
CC (PubMed:22730405). Impaired stomatal closure after treatment with
CC methyl jasmonate (MeJA), salicylic acid (SA) and flagellin 22 (Flg22)
CC (PubMed:29463779). Altered ABA-mediated inhibition of light-induced
CC stomatal opening (PubMed:22730405). Apoplastic ROS-sensitive plants
CC exhibiting severe tissue damage when exposed to ozone (O3)
CC (PubMed:30361234). {ECO:0000269|PubMed:22730405,
CC ECO:0000269|PubMed:27694184, ECO:0000269|PubMed:29463779,
CC ECO:0000269|PubMed:30361234}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Exhibits protein kinase activity according to PubMed:22730405,
CC but in contradiction, described as an inactive pseudokinase by
CC PubMed:30361234. {ECO:0000305|PubMed:22730405,
CC ECO:0000305|PubMed:30361234}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE84378.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB45889.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79094.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KF531634; AGT59499.1; -; mRNA.
DR EMBL; AL080282; CAB45889.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161554; CAB79094.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84378.2; ALT_INIT; Genomic_DNA.
DR EMBL; FJ708750; ACN59344.1; -; mRNA.
DR PIR; T10636; T10636.
DR RefSeq; NP_001320016.1; NM_001341467.1.
DR AlphaFoldDB; C0LGQ9; -.
DR SMR; C0LGQ9; -.
DR BioGRID; 13133; 47.
DR IntAct; C0LGQ9; 48.
DR STRING; 3702.AT4G20940.1; -.
DR TCDB; 1.A.87.2.4; the mechanosensitive calcium channel (mca) family.
DR iPTMnet; C0LGQ9; -.
DR PaxDb; C0LGQ9; -.
DR PRIDE; C0LGQ9; -.
DR ProteomicsDB; 242849; -.
DR EnsemblPlants; AT4G20940.1; AT4G20940.1; AT4G20940.
DR GeneID; 827842; -.
DR Gramene; AT4G20940.1; AT4G20940.1; AT4G20940.
DR KEGG; ath:AT4G20940; -.
DR Araport; AT4G20940; -.
DR eggNOG; ENOG502QUKN; Eukaryota.
DR InParanoid; C0LGQ9; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; C0LGQ9; -.
DR PRO; PR:C0LGQ9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; C0LGQ9; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0071485; P:cellular response to absence of light; IMP:UniProtKB.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IMP:UniProtKB.
DR GO; GO:1901528; P:hydrogen peroxide mediated signaling pathway involved in stomatal movement; IMP:UniProtKB.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF13516; LRR_6; 2.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; ATP-binding; Cell membrane; Glycoprotein;
KW Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Stress response; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1053
FT /note="LRR receptor-like serine/threonine-protein kinase
FT GHR1"
FT /id="PRO_0000387555"
FT TOPO_DOM 19..630
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 631..651
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 652..1053
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 73..93
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 94..119
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 121..141
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 142..165
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 166..189
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 191..212
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 213..237
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 239..260
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 262..285
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 286..309
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 310..333
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 335..357
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 358..384
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 401..425
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 426..449
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 450..474
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 476..498
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 499..521
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 522..546
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 548..570
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 572..592
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT DOMAIN 770..1053
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 662..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 776..784
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 798
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 100
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 102
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 105
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 126
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 262
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 278
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 280
FT /note="Phosphothreonine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 281
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 325
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 406
FT /note="Phosphotyrosine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 410
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 415
FT /note="Phosphothreonine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 417
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 434
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 613
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 614
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 616
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 669
FT /note="Phosphothreonine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 675
FT /note="Phosphothreonine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 678
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 680
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 698
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 699
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 700
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19376835"
FT MOD_RES 713
FT /note="Phosphothreonine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 716
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 718
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 720
FT /note="Phosphothreonine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 721
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 724
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 760
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 764
FT /note="Phosphothreonine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 769
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 928
FT /note="Phosphothreonine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 1010
FT /note="Phosphothreonine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 1015
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 1045
FT /note="Phosphothreonine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 1047
FT /note="Phosphotyrosine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 1051
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT MOD_RES 1052
FT /note="Phosphoserine; by HT1"
FT /evidence="ECO:0000269|PubMed:30361234"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 56
FT /note="G->D: In ghr1-13; apoplastic ROS-sensitive plants
FT exhibiting increased tissue damage when exposed to ozone
FT (O3) and slightly higher steady-state stomatal conductance;
FT when associated with N-220."
FT /evidence="ECO:0000269|PubMed:30361234"
FT MUTAGEN 57
FT /note="C->A: Abolishes the capacity to complement the water
FT loss phenotype of the ghr1 mutant."
FT /evidence="ECO:0000269|PubMed:22730405"
FT MUTAGEN 63
FT /note="G->D: In ghr1-12; apoplastic ROS-sensitive plants
FT exhibiting increased tissue damage when exposed to ozone
FT (O3). Slightly higher steady-state stomatal conductance."
FT /evidence="ECO:0000269|PubMed:30361234"
FT MUTAGEN 66
FT /note="C->A: Abolishes the capacity to complement the water
FT loss phenotype of the ghr1 mutant."
FT /evidence="ECO:0000269|PubMed:22730405"
FT MUTAGEN 108
FT /note="G->D: In ghr1-7; apoplastic ROS-sensitive plants
FT exhibiting increased tissue damage when exposed to ozone
FT (O3). Slightly higher steady-state stomatal conductance."
FT /evidence="ECO:0000269|PubMed:30361234"
FT MUTAGEN 220
FT /note="D->N: In ghr1-13; apoplastic ROS-sensitive plants
FT exhibiting increased tissue damage when exposed to ozone
FT (O3) and slightly higher steady-state stomatal conductance;
FT when associated with D-56."
FT /evidence="ECO:0000269|PubMed:30361234"
FT MUTAGEN 293
FT /note="D->N: In ghr1-8; apoplastic ROS-sensitive plants
FT exhibiting increased tissue damage when exposed to ozone
FT (O3). Slightly higher steady-state stomatal conductance."
FT /evidence="ECO:0000269|PubMed:30361234"
FT MUTAGEN 381
FT /note="C->A: No effect on the capacity to complement the
FT water loss phenotype of the ghr1 mutant."
FT /evidence="ECO:0000269|PubMed:22730405"
FT MUTAGEN 618
FT /note="A->T: In ghr1-2/rcd7 and ghr1-10; apoplastic ROS-
FT sensitive plants exhibiting increased tissue damage when
FT exposed to ozone (O3). Slightly higher steady-state
FT stomatal conductance."
FT /evidence="ECO:0000269|PubMed:30361234"
FT MUTAGEN 637
FT /note="A->V: In ghr1-15; apoplastic ROS-sensitive plants
FT exhibiting increased tissue damage when exposed to ozone
FT (O3). Slightly higher steady-state stomatal conductance."
FT /evidence="ECO:0000269|PubMed:30361234"
FT MUTAGEN 680
FT /note="S->N: In ghr1-16; apoplastic ROS-sensitive plants
FT exhibiting increased tissue damage when exposed to ozone
FT (O3). Slightly higher steady-state stomatal conductance."
FT /evidence="ECO:0000269|PubMed:30361234"
FT MUTAGEN 798
FT /note="K->E: Loss of phosphorylation activity on SLAC1."
FT /evidence="ECO:0000269|PubMed:22730405"
FT MUTAGEN 798
FT /note="K->W: Impaired ATP binding."
FT /evidence="ECO:0000269|PubMed:22730405"
SQ SEQUENCE 1053 AA; 113881 MW; 9A714A3EC89C02AB CRC64;
MNLSRILLLS MFFLSAMGQL PSQDIMALLE FKKGIKHDPT GFVLNSWNDE SIDFNGCPSS
WNGIVCNGGN VAGVVLDNLG LTADADFSLF SNLTKLVKLS MSNNSLSGVL PNDLGSFKSL
QFLDLSDNLF SSSLPKEIGR SVSLRNLSLS GNNFSGEIPE SMGGLISLQS LDMSSNSLSG
PLPKSLTRLN DLLYLNLSSN GFTGKMPRGF ELISSLEVLD LHGNSIDGNL DGEFFLLTNA
SYVDISGNRL VTTSGKLLPG VSESIKHLNL SHNQLEGSLT SGFQLFQNLK VLDLSYNMLS
GELPGFNYVY DLEVLKLSNN RFSGSLPNNL LKGDSLLLTT LDLSGNNLSG PVSSIMSTTL
HTLDLSSNSL TGELPLLTGG CVLLDLSNNQ FEGNLTRWSK WENIEYLDLS QNHFTGSFPD
ATPQLLRANH LNLSYNKLTG SLPERIPTHY PKLRVLDISS NSLEGPIPGA LLSMPTLEEI
HLQNNGMTGN IGPLPSSGSR IRLLDLSHNR FDGDLPGVFG SLTNLQVLNL AANNLSGSLP
SSMNDIVSLS SLDVSQNHFT GPLPSNLSSN IMAFNVSYND LSGTVPENLK NFPPPSFYPG
NSKLVLPAGS PGSSASEASK NKSTNKLVKV VIIVSCAVAL IILILVAILL FCICKSRRRE
ERSITGKETN RRAQTIPSGS GGGMVVSAED LVASRKGSSS EILSPDEKLA VATGFSPSKT
SNLSWSPGSG DSFPADQQLA RLDVRSPDRL VGELHFLDDS IKLTPEELSR APAEVLGRSS
HGTSYRATLD NGVFLTVKWL REGVAKQRKE FAKEVKKFSN IRHPNVVTLR GYYWGPTQHE
KLILSDYISP GSLASFLYDR PGRKGPPLAW TQRLKIAVDV ARGLNYLHFD RAVPHGNLKA
TNILLDGAEL NARVADYCLH RLMTQAGTVE QILDAGILGY RAPELAASRK PLPSFKSDVY
AFGVILLEIL TGRCAGDVIT GEQEGVDLTD WVRLRVAEGR GAECFDSVLT QEMGSDPVTE
KGMKEVLGIA LRCIRSVSER PGIKTIYEDL SSI
