GSO1_ARATH
ID GSO1_ARATH Reviewed; 1249 AA.
AC C0LGQ5; Q9SN91;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase GSO1 {ECO:0000303|PubMed:18088309};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Protein GASSHO 1 {ECO:0000303|PubMed:18088309};
DE AltName: Full=Protein SCHENGEN 3 {ECO:0000303|PubMed:25233277};
DE Flags: Precursor;
GN Name=GSO1 {ECO:0000303|PubMed:18088309};
GN Synonyms=SGN3 {ECO:0000303|PubMed:25233277};
GN OrderedLocusNames=At4g20140 {ECO:0000312|Araport:AT4G20140};
GN ORFNames=F1C12.60 {ECO:0000312|EMBL:CAA18239.1};
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 [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 [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=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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=18088309; DOI=10.1111/j.1365-313x.2007.03395.x;
RA Tsuwamoto R., Fukuoka H., Takahata Y.;
RT "GASSHO1 and GASSHO2 encoding a putative leucine-rich repeat transmembrane-
RT type receptor kinase are essential for the normal development of the
RT epidermal surface in Arabidopsis embryos.";
RL Plant J. 54:30-42(2008).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND REPRESSION BY
RP WOUNDING.
RC STRAIN=cv. Columbia;
RX PubMed=24123341; DOI=10.1002/dvdy.24066;
RA Racolta A., Bryan A.C., Tax F.E.;
RT "The receptor-like kinases GSO1 and GSO2 together regulate root growth in
RT Arabidopsis through control of cell division and cell fate specification.";
RL Dev. Dyn. 243:257-278(2014).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF PRO-160; GLY-287; GLY-719;
RP GLY-1101 AND GLY-1150, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=25233277; DOI=10.7554/elife.03115;
RA Pfister A., Barberon M., Alassimone J., Kalmbach L., Lee Y., Vermeer J.E.,
RA Yamazaki M., Li G., Maurel C., Takano J., Kamiya T., Salt D.E., Roppolo D.,
RA Geldner N.;
RT "A receptor-like kinase mutant with absent endodermal diffusion barrier
RT displays selective nutrient homeostasis defects.";
RL Elife 3:E03115-E03115(2014).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH CIF1 AND CIF2.
RX PubMed=28104889; DOI=10.1126/science.aai9057;
RA Nakayama T., Shinohara H., Tanaka M., Baba K., Ogawa-Ohnishi M.,
RA Matsubayashi Y.;
RT "A peptide hormone required for Casparian strip diffusion barrier formation
RT in Arabidopsis roots.";
RL Science 355:284-286(2017).
CC -!- FUNCTION: Together with GSO2, receptor-like serine/threonine-kinase
CC required during the development of the epidermal surface in embryos and
CC cotyledons (PubMed:18088309). In coordination with GSO2, regulates root
CC growth through control of cell division and cell fate specification.
CC Controls seedling root growth by modulating sucrose response after
CC germination (PubMed:24123341). Receptor of the peptide hormones CIF1
CC and CIF2 required for contiguous Casparian strip diffusion barrier
CC formation in roots (PubMed:28104889). Required for localizing CASP
CC proteins into the Casparian strip following an uninterrupted, ring-like
CC domain, to trigger endodermal differentiation and thus regulate
CC potassium ion (K) homeostasis. Involved in the maintenance of water
CC transport and root pressure. May also be involved in the regulation of
CC suberin accumulation in the endodermis (PubMed:25233277).
CC {ECO:0000269|PubMed:18088309, ECO:0000269|PubMed:24123341,
CC ECO:0000269|PubMed:25233277, ECO:0000269|PubMed:28104889}.
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:0000255|PROSITE-ProRule:PRU00159};
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:0000255|PROSITE-ProRule:PRU00159};
CC -!- SUBUNIT: Interacts with CIF1 and CIF2. {ECO:0000269|PubMed:28104889}.
CC -!- INTERACTION:
CC C0LGQ5; C0LGR6: At4g29180; NbExp=2; IntAct=EBI-16905069, EBI-20654480;
CC C0LGQ5; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-16905069, EBI-16902452;
CC C0LGQ5; Q42371: ERECTA; NbExp=3; IntAct=EBI-16905069, EBI-16940407;
CC C0LGQ5; Q9FRI1: LRR-RLK; NbExp=3; IntAct=EBI-16905069, EBI-17071528;
CC C0LGQ5; Q93ZS4: NIK3; NbExp=2; IntAct=EBI-16905069, EBI-17121474;
CC C0LGQ5; Q9FZ59: PEPR2; NbExp=2; IntAct=EBI-16905069, EBI-20652612;
CC C0LGQ5; Q9LZV7: PXC2; NbExp=2; IntAct=EBI-16905069, EBI-1238200;
CC C0LGQ5; Q8LPS5: SERK5; NbExp=2; IntAct=EBI-16905069, EBI-16887868;
CC C0LGQ5; Q9SKB2: SOBIR1; NbExp=2; IntAct=EBI-16905069, EBI-16905883;
CC C0LGQ5; Q06BH3: SRF1; NbExp=2; IntAct=EBI-16905069, EBI-16955764;
CC C0LGQ5; Q6R2K3: SRF3; NbExp=2; IntAct=EBI-16905069, EBI-20651925;
CC C0LGQ5; Q9LUL4: SRF7; NbExp=2; IntAct=EBI-16905069, EBI-16964596;
CC C0LGQ5; Q9M2R4: T10K17.40; NbExp=3; IntAct=EBI-16905069, EBI-20657109;
CC C0LGQ5; P43298: TMK1; NbExp=2; IntAct=EBI-16905069, EBI-2023970;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25233277};
CC Single-pass type I membrane protein {ECO:0000255}. Note=Localized into
CC a broader band at the endodermal plasma membrane, embedding growing
CC CASP microdomains. In endodermal cells, first observed on all cell
CC sides, but quickly relocated in the transversal and anticlinal sides of
CC the plasma membrane, but excluded from the Casparian strip membrane
CC domain (CSD). {ECO:0000269|PubMed:25233277}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in siliques, seeds, developing
CC embryos and seedlings, detected in flower buds and roots, but not in
CC leaves or stems. {ECO:0000269|PubMed:18088309}.
CC -!- DEVELOPMENTAL STAGE: In flower buds, localized in filaments and
CC stigmas. During embryogenesis, uniform expression from the globular
CC embryo to the mature cotyledonary embryo. After germination, detected
CC in whole cotyledons and in the hypocotyl. During the 6 first days after
CC germination (DAG), highly expressed in roots throughout the elongation
CC zone (EZ) and differentiation zone, but restricted to the endodermis
CC and vasculature. Accumulates progressively in the quiescent center
CC (QC). Down-regulated at sites of lateral root primordia (LRP)
CC initiation. Absent at sites of deliberate wounding in the root. Mostly
CC observed in the inner layers of the mature root, the QC and shoot
CC apical meristem (SAM) (PubMed:24123341). Expressed early during
CC endodermal differentiation, shortly after the onset of endodermal cells
CC elongation (PubMed:25233277). {ECO:0000269|PubMed:18088309,
CC ECO:0000269|PubMed:24123341, ECO:0000269|PubMed:25233277}.
CC -!- INDUCTION: Repressed by wounding. {ECO:0000269|PubMed:24123341}.
CC -!- DISRUPTION PHENOTYPE: Dramatic defect in endodermal barrier formation
CC leading to altered potassium ion (K) homeostasis and hypersensitivity
CC to low potassium conditions. Casparian strips are repeatedly
CC interrupted, forming irregularly-sized holes of several micrometer in
CC length, probably due to abnormal CASP proteins patterning. Suppresses
CC the enhanced suberin production when combined to other Casparian strip-
CC defective mutants such as esb1 and casp1 casp3. Extremely sensitive to
CC changes in environmental conditions such as high temperatures and under
CC long-day (LD) conditions leading to dwarf plants. Normal transpiration
CC but altered water transport and root pressure (PubMed:25233277). No
CC visible phenotype during embryogenesis and seedling development. Gso1
CC and gso2 double mutants produce slightly contorted seeds, with
CC abnormally shaped embryos and seedlings; adhesion between cotyledons
CC and the peripheral tissue of the endosperm, short hypocotyl, and
CC concave cotyledons sometimes fused, with compressed epidermal cells,
CC endosperm tissue partially adherent to the surface of the cotyledons,
CC and a rough surface. In addition, seedlings of gso1 gso2 have also root
CC growth and patterning defects characterized by abnormal numbers of
CC cells in longitudinal files and radial cell layers, as well as aberrant
CC stem cell division planes. Root growth arrest and cell divisions
CC defects are rescued by exogenous application of sucrose, but not
CC patterning defects (PubMed:24123341). The double mutant gso1 gso2
CC exhibits a repeatedly interrupted, discontinuous Casparian strip due to
CC patch-like localization of the CASPs proteins as a result of partial
CC fusion of individual CASP containing islands in the Casparian strip
CC membrane domain (CSD) (PubMed:28104889). {ECO:0000269|PubMed:18088309,
CC ECO:0000269|PubMed:24123341, ECO:0000269|PubMed:25233277,
CC ECO:0000269|PubMed:28104889}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18239.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79014.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022224; CAA18239.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161552; CAB79014.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84279.1; -; Genomic_DNA.
DR EMBL; FJ708746; ACN59340.1; -; mRNA.
DR PIR; T05322; T05322.
DR RefSeq; NP_193747.2; NM_118133.3.
DR PDB; 6S6Q; X-ray; 2.95 A; A/B=18-870.
DR PDBsum; 6S6Q; -.
DR AlphaFoldDB; C0LGQ5; -.
DR SMR; C0LGQ5; -.
DR BioGRID; 13052; 57.
DR IntAct; C0LGQ5; 71.
DR STRING; 3702.AT4G20140.1; -.
DR PaxDb; C0LGQ5; -.
DR PRIDE; C0LGQ5; -.
DR ProteomicsDB; 247223; -.
DR EnsemblPlants; AT4G20140.1; AT4G20140.1; AT4G20140.
DR GeneID; 827760; -.
DR Gramene; AT4G20140.1; AT4G20140.1; AT4G20140.
DR KEGG; ath:AT4G20140; -.
DR Araport; AT4G20140; -.
DR TAIR; locus:2120362; AT4G20140.
DR eggNOG; ENOG502QRD1; Eukaryota.
DR HOGENOM; CLU_000288_22_0_1; -.
DR InParanoid; C0LGQ5; -.
DR OMA; THKPLFR; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; C0LGQ5; -.
DR PRO; PR:C0LGQ5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; C0LGQ5; baseline and differential.
DR Genevisible; C0LGQ5; AT.
DR GO; GO:0048226; C:Casparian strip; IMP:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
DR GO; GO:0055075; P:potassium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0051302; P:regulation of cell division; IMP:UniProtKB.
DR GO; GO:0042659; P:regulation of cell fate specification; IMP:UniProtKB.
DR GO; GO:1903224; P:regulation of endodermal cell differentiation; IMP:UniProtKB.
DR GO; GO:2000280; P:regulation of root development; IMP:UniProtKB.
DR GO; GO:2000067; P:regulation of root morphogenesis; IMP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR GO; GO:0090708; P:specification of plant organ axis polarity; IMP:UniProtKB.
DR GO; GO:0030104; P:water homeostasis; IMP:UniProtKB.
DR GO; GO:0006833; P:water transport; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 5.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 16.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Cell wall biogenesis/degradation;
KW Developmental protein; Glycoprotein; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1249
FT /note="LRR receptor-like serine/threonine-protein kinase
FT GSO1"
FT /id="PRO_0000387513"
FT TOPO_DOM 19..876
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 898..1249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 94..118
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 119..142
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 144..166
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 168..190
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 191..214
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 216..238
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 239..262
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 264..285
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 286..310
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 312..334
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 336..359
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 360..383
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 385..407
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 408..431
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 433..455
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 457..479
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 480..503
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 505..527
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 528..551
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 553..574
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 576..598
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 599..622
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 623..646
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 648..670
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 671..694
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 696..718
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT REPEAT 719..742
FT /note="LRR 27"
FT /evidence="ECO:0000255"
FT REPEAT 744..766
FT /note="LRR 28"
FT /evidence="ECO:0000255"
FT REPEAT 767..791
FT /note="LRR 29"
FT /evidence="ECO:0000255"
FT REPEAT 792..815
FT /note="LRR 30"
FT /evidence="ECO:0000255"
FT REPEAT 817..838
FT /note="LRR 31"
FT /evidence="ECO:0000255"
FT DOMAIN 951..1240
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 1084
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 957..965
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 979
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 948
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 1027
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 1071
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 1129
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 1136
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 822
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 160
FT /note="P->L: In sgn3-5; altered CASP proteins localization
FT in Casparian strips."
FT /evidence="ECO:0000269|PubMed:25233277"
FT MUTAGEN 287
FT /note="G->R: In sgn3-8; altered CASP proteins localization
FT in Casparian strips; when associated with R-1101."
FT /evidence="ECO:0000269|PubMed:25233277"
FT MUTAGEN 719
FT /note="G->R: In sgn3-12; altered CASP proteins localization
FT in Casparian strips; when associated with E-1150."
FT /evidence="ECO:0000269|PubMed:25233277"
FT MUTAGEN 1101
FT /note="G->R: In sgn3-8; altered CASP proteins localization
FT in Casparian strips; when associated with R-287."
FT /evidence="ECO:0000269|PubMed:25233277"
FT MUTAGEN 1150
FT /note="G->E: In sgn3-18; altered CASP proteins localization
FT in Casparian strips. In sgn3-12; altered CASP proteins
FT localization in Casparian strips; when associated with R-
FT 719."
FT /evidence="ECO:0000269|PubMed:25233277"
FT MUTAGEN 1150
FT /note="G->R: In sgn3-17; altered CASP proteins localization
FT in Casparian strips."
FT /evidence="ECO:0000269|PubMed:25233277"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:6S6Q"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 281..285
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 305..309
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:6S6Q"
FT TURN 329..332
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 378..382
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 402..406
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 426..430
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 450..454
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 474..478
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 498..502
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 513..518
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 522..526
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 537..543
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 546..550
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 556..558
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 578..581
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 584..590
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 593..597
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 608..613
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 617..621
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 627..629
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 633..637
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 641..645
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 656..661
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 665..669
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 675..677
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 680..683
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 689..693
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 698..701
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 713..717
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 737..741
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 747..749
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 761..765
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 786..790
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 796..798
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 801..806
FT /evidence="ECO:0007829|PDB:6S6Q"
FT TURN 811..813
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 820..822
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 825..828
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 834..836
FT /evidence="ECO:0007829|PDB:6S6Q"
FT HELIX 841..844
FT /evidence="ECO:0007829|PDB:6S6Q"
FT STRAND 850..852
FT /evidence="ECO:0007829|PDB:6S6Q"
SQ SEQUENCE 1249 AA; 137288 MW; 9B4C4928C8A10E95 CRC64;
MQPLVLLLLF ILCFSGLGQP GIINNDLQTL LEVKKSLVTN PQEDDPLRQW NSDNINYCSW
TGVTCDNTGL FRVIALNLTG LGLTGSISPW FGRFDNLIHL DLSSNNLVGP IPTALSNLTS
LESLFLFSNQ LTGEIPSQLG SLVNIRSLRI GDNELVGDIP ETLGNLVNLQ MLALASCRLT
GPIPSQLGRL VRVQSLILQD NYLEGPIPAE LGNCSDLTVF TAAENMLNGT IPAELGRLEN
LEILNLANNS LTGEIPSQLG EMSQLQYLSL MANQLQGLIP KSLADLGNLQ TLDLSANNLT
GEIPEEFWNM SQLLDLVLAN NHLSGSLPKS ICSNNTNLEQ LVLSGTQLSG EIPVELSKCQ
SLKQLDLSNN SLAGSIPEAL FELVELTDLY LHNNTLEGTL SPSISNLTNL QWLVLYHNNL
EGKLPKEISA LRKLEVLFLY ENRFSGEIPQ EIGNCTSLKM IDMFGNHFEG EIPPSIGRLK
ELNLLHLRQN ELVGGLPASL GNCHQLNILD LADNQLSGSI PSSFGFLKGL EQLMLYNNSL
QGNLPDSLIS LRNLTRINLS HNRLNGTIHP LCGSSSYLSF DVTNNGFEDE IPLELGNSQN
LDRLRLGKNQ LTGKIPWTLG KIRELSLLDM SSNALTGTIP LQLVLCKKLT HIDLNNNFLS
GPIPPWLGKL SQLGELKLSS NQFVESLPTE LFNCTKLLVL SLDGNSLNGS IPQEIGNLGA
LNVLNLDKNQ FSGSLPQAMG KLSKLYELRL SRNSLTGEIP VEIGQLQDLQ SALDLSYNNF
TGDIPSTIGT LSKLETLDLS HNQLTGEVPG SVGDMKSLGY LNVSFNNLGG KLKKQFSRWP
ADSFLGNTGL CGSPLSRCNR VRSNNKQQGL SARSVVIISA ISALTAIGLM ILVIALFFKQ
RHDFFKKVGH GSTAYTSSSS SSQATHKPLF RNGASKSDIR WEDIMEATHN LSEEFMIGSG
GSGKVYKAEL ENGETVAVKK ILWKDDLMSN KSFSREVKTL GRIRHRHLVK LMGYCSSKSE
GLNLLIYEYM KNGSIWDWLH EDKPVLEKKK KLLDWEARLR IAVGLAQGVE YLHHDCVPPI
VHRDIKSSNV LLDSNMEAHL GDFGLAKVLT ENCDTNTDSN TWFACSYGYI APEYAYSLKA
TEKSDVYSMG IVLMEIVTGK MPTDSVFGAE MDMVRWVETH LEVAGSARDK LIDPKLKPLL
PFEEDAACQV LEIALQCTKT SPQERPSSRQ ACDSLLHVYN NRTAGYKKL
