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 27-MAR-2024, entry version 107. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.C0LGQ5; -. DR GlyCosmos; C0LGQ5; 20 sites, No reported glycans. DR PaxDb; 3702-AT4G20140-1; -. 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; AT4G20140; GSO1. DR eggNOG; ENOG502QRD1; Eukaryota. DR HOGENOM; CLU_000288_22_0_1; -. DR InParanoid; C0LGQ5; -. DR OMA; NPNFCTW; -. DR OrthoDB; 1211134at2759; -. DR PhylomeDB; C0LGQ5; -. DR PRO; PR:C0LGQ5; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; C0LGQ5; baseline and differential. DR GO; GO:0048226; C:Casparian strip; IMP:UniProtKB. 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:0160073; P:Casparian strip assembly; IMP:UniProtKB. DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB. DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0055075; P:potassium ion homeostasis; IMP:UniProtKB. 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: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 Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 5. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR48053; LEUCINE RICH REPEAT FAMILY PROTEIN, EXPRESSED; 1. DR PANTHER; PTHR48053:SF118; OS07G0498400 PROTEIN; 1. DR Pfam; PF00560; LRR_1; 10. DR Pfam; PF13855; LRR_8; 4. DR Pfam; PF08263; LRRNT_2; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR00019; LEURICHRPT. DR SMART; SM00365; LRR_SD22; 5. DR SMART; SM00369; LRR_TYP; 16. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF52058; L domain-like; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF52047; RNI-like; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; C0LGQ5; AT. 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 FT R-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 //