KSG7_ARATH
ID KSG7_ARATH Reviewed; 380 AA.
AC Q39011; B9DHY9; C0Z326; Q147R2; Q8S9H8; Q9SN42;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Shaggy-related protein kinase eta {ECO:0000303|PubMed:9611268};
DE EC=2.7.11.1 {ECO:0000269|PubMed:11847343, ECO:0000269|PubMed:12428015, ECO:0000269|PubMed:22466366};
DE AltName: Full=ASK-eta {ECO:0000303|PubMed:10080716};
DE AltName: Full=Protein BRASSINOSTEROID INSENSITIVE 2 {ECO:0000303|PubMed:11847343};
DE AltName: Full=Protein ULTRACURVATA 1 {ECO:0000303|PubMed:11820813};
DE AltName: Full=Shaggy-related protein kinase 21 {ECO:0000303|PubMed:28575660};
DE Short=AtSK21 {ECO:0000303|PubMed:28575660};
GN Name=ASK7 {ECO:0000303|PubMed:10080716};
GN Synonyms=BIN2 {ECO:0000303|PubMed:11847343},
GN DWF12 {ECO:0000303|PubMed:12428015}, SK21 {ECO:0000303|PubMed:28575660},
GN UCU1 {ECO:0000303|PubMed:11820813};
GN OrderedLocusNames=At4g18710 {ECO:0000312|Araport:AT4G18710};
GN ORFNames=F28A21.120 {ECO:0000312|EMBL:CAB37456.1};
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Dornelas M.C., Schwebel-Dugue N., Thomas M., Lecharny A., Kreis M.;
RT "Three new cDNAs related to SGG/GSK-3 (SHAGGY/glycogen synthase kinase-3)
RT from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR97-008(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9611268; DOI=10.1016/s0378-1119(98)00147-4;
RA Dornelas M.C., Lejeune B., Dron M., Kreis M.;
RT "The Arabidopsis SHAGGY-related protein kinase (ASK) gene family:
RT structure, organization and evolution.";
RL Gene 212:249-257(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLU-263 AND GLU-264, AND
RP MUTANTS DWF12.
RX PubMed=12428015; DOI=10.1104/pp.010496;
RA Choe S., Schmitz R.J., Fujioka S., Takatsuto S., Lee M.-O., Yoshida S.,
RA Feldmann K.A., Tax F.E.;
RT "Arabidopsis brassinosteroid-insensitive dwarf12 mutants are semidominant
RT and defective in a glycogen synthase kinase 3beta-like kinase.";
RL Plant Physiol. 130:1506-1515(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLU-264 AND PRO-284, AND
RP MUTANTS UCU1.
RX PubMed=11820813; DOI=10.1006/dbio.2001.0543;
RA Perez-Perez J.M., Ponce M.R., Micol J.L.;
RT "The UCU1 Arabidopsis gene encodes a SHAGGY/GSK3-like kinase required for
RT cell expansion along the proximodistal axis.";
RL Dev. Biol. 242:161-173(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF LYS-69 AND
RP THR-261, AND MUTANTS BIN2.
RX PubMed=11847343; DOI=10.1126/science.1065769;
RA Li J., Nam K.H.;
RT "Regulation of brassinosteroid signaling by a GSK3/SHAGGY-like kinase.";
RL Science 295:1299-1301(2002).
RN [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clone.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=10080716; DOI=10.1023/a:1006102812280;
RA Dornelas M.C., Wittich P., von Recklinghausen I., van Lammeren A.,
RA Kreis M.;
RT "Characterization of three novel members of the Arabidopsis SHAGGY-related
RT protein kinase (ASK) multigene family.";
RL Plant Mol. Biol. 39:137-147(1999).
RN [13]
RP FUNCTION, MUTAGENESIS OF ARG-80, AND INTERACTION WITH BZR1 AND BZR2/BES1.
RX PubMed=12427989; DOI=10.1104/pp.102.010918;
RA Zhao J., Peng P., Schmitz R.J., Decker A.D., Tax F.E., Li J.;
RT "Two putative BIN2 substrates are nuclear components of brassinosteroid
RT signaling.";
RL Plant Physiol. 130:1221-1229(2002).
RN [14]
RP FUNCTION, AND INTERACTION WITH BZR1.
RX PubMed=12114546; DOI=10.1073/pnas.152342599;
RA He J.-X., Gendron J.M., Yang Y., Li J., Wang Z.-Y.;
RT "The GSK3-like kinase BIN2 phosphorylates and destabilizes BZR1, a positive
RT regulator of the brassinosteroid signaling pathway in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10185-10190(2002).
RN [15]
RP FUNCTION, INTERACTION WITH BEET CURLY TOP VIRUS AL4 AND TOMATO GOLDEN
RP MOSAIC VIRUS AL4, AND AUTOPHOSPHORYLATION.
RX PubMed=17280695; DOI=10.1016/j.virol.2006.12.034;
RA Piroux N., Saunders K., Page A., Stanley J.;
RT "Geminivirus pathogenicity protein C4 interacts with Arabidopsis thaliana
RT shaggy-related protein kinase AtSKeta, a component of the brassinosteroid
RT signalling pathway.";
RL Virology 362:428-440(2007).
RN [16]
RP INTERACTION WITH BHLH150.
RX PubMed=20023194; DOI=10.1105/tpc.109.072504;
RA Wang H., Zhu Y., Fujioka S., Asami T., Li J., Li J.;
RT "Regulation of Arabidopsis brassinosteroid signaling by atypical basic
RT helix-loop-helix proteins.";
RL Plant Cell 21:3781-3791(2009).
RN [17]
RP ACTIVITY REGULATION, INTERACTION WITH BSU1, AND PHOSPHORYLATION AT TYR-200.
RX PubMed=21855796; DOI=10.1016/j.molcel.2011.05.037;
RA Kim T.W., Guan S., Burlingame A.L., Wang Z.Y.;
RT "The CDG1 kinase mediates brassinosteroid signal transduction from BRI1
RT receptor kinase to BSU1 phosphatase and GSK3-like kinase BIN2.";
RL Mol. Cell 43:561-571(2011).
RN [18]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-263, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AUTOPHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=22466366; DOI=10.1038/ncb2471;
RA Gudesblat G.E., Schneider-Pizon J., Betti C., Mayerhofer J., Vanhoutte I.,
RA van Dongen W., Boeren S., Zhiponova M., de Vries S., Jonak C.,
RA Russinova E.;
RT "SPEECHLESS integrates brassinosteroid and stomata signalling pathways.";
RL Nat. Cell Biol. 14:548-554(2012).
RN [19]
RP FUNCTION, AND INTERACTION WITH YDA.
RX PubMed=22307275; DOI=10.1038/nature10794;
RA Kim T.W., Michniewicz M., Bergmann D.C., Wang Z.Y.;
RT "Brassinosteroid regulates stomatal development by GSK3-mediated inhibition
RT of a MAPK pathway.";
RL Nature 482:419-422(2012).
RN [20]
RP FUNCTION, AND INTERACTION WITH MKK4.
RX PubMed=23341468; DOI=10.1074/jbc.m112.384453;
RA Khan M., Rozhon W., Bigeard J., Pflieger D., Husar S., Pitzschke A.,
RA Teige M., Jonak C., Hirt H., Poppenberger B.;
RT "Brassinosteroid-regulated GSK3/Shaggy-like kinases phosphorylate mitogen-
RT activated protein (MAP) kinase kinases, which control stomata development
RT in Arabidopsis thaliana.";
RL J. Biol. Chem. 288:7519-7527(2013).
RN [21]
RP FUNCTION, INTERACTION WITH BSK1; BSK6; BSK8 AND BSK11, AND MUTAGENESIS OF
RP LYS-69.
RX PubMed=23496207; DOI=10.1111/tpj.12175;
RA Sreeramulu S., Mostizky Y., Sunitha S., Shani E., Nahum H., Salomon D.,
RA Hayun L.B., Gruetter C., Rauh D., Ori N., Sessa G.;
RT "BSKs are partially redundant positive regulators of brassinosteroid
RT signaling in Arabidopsis.";
RL Plant J. 74:905-919(2013).
RN [22]
RP UBIQUITINATION, ACTIVITY REGULATION, INTERACTION WITH KIB1 AND KIB2, AND
RP MUTAGENESIS OF TYR-200 AND GLU-263.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=28575660; DOI=10.1016/j.molcel.2017.05.012;
RA Zhu J.-Y., Li Y., Cao D.-M., Yang H., Oh E., Bi Y., Zhu S., Wang Z.-Y.;
RT "The F-box protein KIB1 mediates brassinosteroid-induced inactivation and
RT degradation of GSK3-like kinases in Arabidopsis.";
RL Mol. Cell 66:648-657(2017).
RN [23]
RP FUNCTION, AND INTERACTION WITH WRKY46; WRKY54 AND WRKY70.
RC STRAIN=cv. Columbia;
RX PubMed=28576847; DOI=10.1105/tpc.17.00364;
RA Chen J., Nolan T.M., Ye H., Zhang M., Tong H., Xin P., Chu J., Chu C.,
RA Li Z., Yin Y.;
RT "Arabidopsis WRKY46, WRKY54, and WRKY70 transcription factors are involved
RT in brassinosteroid-regulated plant growth and drought responses.";
RL Plant Cell 29:1425-1439(2017).
RN [24]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=28652362; DOI=10.1073/pnas.1703258114;
RA Breda A.S., Hazak O., Hardtke C.S.;
RT "Phosphosite charge rather than shootward localization determines OCTOPUS
RT activity in root protophloem.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E5721-E5730(2017).
RN [25]
RP FUNCTION, MUTAGENESIS OF LYS-69, INTERACTION WITH POLAR AND BASL,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=30429609; DOI=10.1038/s41586-018-0714-x;
RA Houbaert A., Zhang C., Tiwari M., Wang K., de Marcos Serrano A.,
RA Savatin D.V., Urs M.J., Zhiponova M.K., Gudesblat G.E., Vanhoutte I.,
RA Eeckhout D., Boeren S., Karimi M., Betti C., Jacobs T., Fenoll C., Mena M.,
RA de Vries S., De Jaeger G., Russinova E.;
RT "POLAR-guided signalling complex assembly and localization drive asymmetric
RT cell division.";
RL Nature 563:574-578(2018).
CC -!- FUNCTION: Negative regulator in brassinosteroid signal transduction
CC pathway important for plant growth. May be also involved in auxin
CC signaling pathway. Phosphorylates and increases the degradation of BZR1
CC and BZR2/BES1 by the proteasome. Phosphorylates BHLH150, beet curly top
CC virus C4 and tomato golden mosaic virus AC4 on threonine and serine
CC residues. Upon brassinosteroid signaling, inhibits stomatal development
CC by phosphorylating and inhibiting the MAPKK kinase YDA and the MAPK
CC kinases MKK4 and MKK5 (PubMed:11847343, PubMed:12114546,
CC PubMed:12427989, PubMed:17280695, PubMed:22307275, PubMed:23341468).
CC Phosphorylates BSK1, BSK3, BSK5, BSK6, BSK8 AND BSK11 in vitro
CC (PubMed:23496207). Phoyphorylates and destabilizes WRKY46, WRKY54 and
CC WRKY70 (PubMed:28576847). Mediates BASL nuclear exclusion; kinase
CC activity is required for this function (PubMed:30429609). Required
CC first at the cortical polarity site, to restrict MAPK signaling and
CC promote asymmetric cell division (ACD), and second in the nucleus of
CC stomatal lineage ground cells (SLGCs) or meristemoids, to limit cell
CC division and to promote differentiation into pavement or stomatal guard
CC cells, respectively, likely by initiating BASL polarization
CC (PubMed:30429609). Phosphorylates BASL, YDA and SPCH in vitro and POLAR
CC in vivo (PubMed:30429609). Phosphorylates and inhibits SPCH in the
CC nucleus of SLGC undergoing ACD, thus negatively regulating stomatal
CC development (PubMed:30429609, PubMed:22466366).
CC {ECO:0000269|PubMed:11847343, ECO:0000269|PubMed:12114546,
CC ECO:0000269|PubMed:12427989, ECO:0000269|PubMed:17280695,
CC ECO:0000269|PubMed:22307275, ECO:0000269|PubMed:22466366,
CC ECO:0000269|PubMed:23341468, ECO:0000269|PubMed:23496207,
CC ECO:0000269|PubMed:28576847, ECO:0000269|PubMed:30429609}.
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:11847343, ECO:0000269|PubMed:12428015,
CC ECO:0000269|PubMed:22466366};
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:11847343,
CC ECO:0000269|PubMed:12428015, ECO:0000269|PubMed:22466366};
CC -!- ACTIVITY REGULATION: Inactivated by an unknown mechanism after binding
CC of brassinosteroids to the brassinosteroid receptor complex (Probable).
CC Inhibited by lithium. Inhibited by dephosphorylation at Tyr-200 by BSU1
CC (PubMed:21855796). Competitive inhibition by KIB1 that reduces
CC substrate (e.g. BZR1) access (PubMed:28575660). Repressed by bikinin
CC (PubMed:22466366). {ECO:0000269|PubMed:21855796,
CC ECO:0000269|PubMed:22466366, ECO:0000269|PubMed:28575660, ECO:0000305}.
CC -!- SUBUNIT: Interacts in vitro with the C-terminal fragment of BZR1 and
CC with BES1/BZR2, but not through the kinase domain. Interacts with
CC BHLH150, beet curly top virus AL4/C4 and tomato golden mosaic virus
CC AL4/AC4. Interacts with YDA. Interacts with MKK4. Interacts with KIB1
CC and KIB2 in a brassinosteroid (BR)-dependent manner (PubMed:28575660).
CC Interacts with BSK1, BSK6, BSK8 and BSK11 (PubMed:23496207). Binds to
CC WRKY46, WRKY54 and WRKY70 (PubMed:28576847). Component of a complex
CC made of POLAR, BASL, ASK7/BIN2 and ASK3/SK12 (PubMed:30429609). Binds
CC to POLAR and BASL (PubMed:30429609). {ECO:0000269|PubMed:12114546,
CC ECO:0000269|PubMed:12427989, ECO:0000269|PubMed:17280695,
CC ECO:0000269|PubMed:20023194, ECO:0000269|PubMed:22307275,
CC ECO:0000269|PubMed:23341468, ECO:0000269|PubMed:23496207,
CC ECO:0000269|PubMed:28575660, ECO:0000269|PubMed:28576847,
CC ECO:0000269|PubMed:30429609}.
CC -!- INTERACTION:
CC Q39011; Q9C9A5: ARABIDOPSIS MYB-LIKE 2; NbExp=2; IntAct=EBI-1798250, EBI-1546577;
CC Q39011; Q94JM3: ARF2; NbExp=6; IntAct=EBI-1798250, EBI-1799262;
CC Q39011; P93022: ARF7; NbExp=2; IntAct=EBI-1798250, EBI-632284;
CC Q39011; Q39011: ASK7; NbExp=5; IntAct=EBI-1798250, EBI-1798250;
CC Q39011; A0A384LCJ3: AXX17_At3g53170; NbExp=3; IntAct=EBI-1798250, EBI-25523891;
CC Q39011; Q8S307: BZR1; NbExp=2; IntAct=EBI-1798250, EBI-1803261;
CC Q39011; Q9LN63: BZR2; NbExp=2; IntAct=EBI-1798250, EBI-617078;
CC Q39011; Q8L8A6: GRF5; NbExp=3; IntAct=EBI-1798250, EBI-1396652;
CC Q39011; Q9AT61: LBD13; NbExp=3; IntAct=EBI-1798250, EBI-4432427;
CC Q39011; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-1798250, EBI-4426144;
CC Q39011; Q9LEZ9: TCP17; NbExp=4; IntAct=EBI-1798250, EBI-15192327;
CC Q39011; Q9FII5: TDR; NbExp=2; IntAct=EBI-1798250, EBI-15730235;
CC Q39011; Q9CAD5: YDA; NbExp=4; IntAct=EBI-1798250, EBI-15967064;
CC Q39011; O64722: ZHD3; NbExp=3; IntAct=EBI-1798250, EBI-1806244;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:30429609}. Cytoplasm {ECO:0000269|PubMed:28652362,
CC ECO:0000269|PubMed:30429609}. Nucleus {ECO:0000269|PubMed:28652362,
CC ECO:0000269|PubMed:30429609}. Cell membrane
CC {ECO:0000269|PubMed:28652362, ECO:0000269|PubMed:30429609}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC Note=Spotty cytoplasmic as well as nuclear localization
CC (PubMed:28652362). Recruited to the plasma membrane by OPS
CC (PubMed:28652362). Localized throughout the plasma membrane in
CC asymmetric cell division (ACD) precursors (PubMed:30429609).
CC Accumulates transiently in a polarized pattern at the plasma membrane
CC immediately before ACD, relocalizing to well-defined foci, in a POLAR-
CC dependent and in the presence of BASL (PubMed:30429609). Mostly
CC abundant and more polarized at the cell cortex of stomatal lineage
CC cells with asymmetric cell division (ACD) potential (PubMed:30429609).
CC {ECO:0000269|PubMed:28652362, ECO:0000269|PubMed:30429609}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q39011-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q39011-2; Sequence=VSP_060065;
CC -!- TISSUE SPECIFICITY: In the two outer cell layers of the developing seed
CC coat and restricted to the suspensor cells in developing embryos
CC (PubMed:10080716). Mostly expressed in stomatal lineage cells with
CC asymmetric cell division (ACD) potential (PubMed:30429609). Observed in
CC small cells of non-protruding hypocotyl cell files and of developing
CC cotyledon epidermis (PubMed:22466366). {ECO:0000269|PubMed:10080716,
CC ECO:0000269|PubMed:22466366, ECO:0000269|PubMed:30429609}.
CC -!- DEVELOPMENTAL STAGE: Detected throughout the epidermis in young
CC seedlings, and accumulates progressively during epidermal cell
CC maturation, especially in stomatal lineage cells with asymmetric cell
CC division (ACD) potential. {ECO:0000269|PubMed:30429609}.
CC -!- PTM: Autophosphorylated mainly on threonine and serine residues.
CC {ECO:0000269|PubMed:17280695, ECO:0000269|PubMed:22466366}.
CC -!- PTM: Ubiquitination and subsequent proteasomal degradation mediated by
CC KIB1. {ECO:0000269|PubMed:28575660}.
CC -!- DISRUPTION PHENOTYPE: Increased stability of SPCH and formation of
CC excessive stomatal and non-stomatal cell.
CC {ECO:0000269|PubMed:22466366}.
CC -!- MISCELLANEOUS: Unlike other GSK3 kinases, does not require a priming
CC phosphorylation event or the presence of a scaffold protein to
CC phosphorylate its substrates.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. GSK-3 subfamily. {ECO:0000305}.
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DR EMBL; X94939; CAA64409.1; -; mRNA.
DR EMBL; Y08947; CAA70144.1; -; Genomic_DNA.
DR EMBL; AY157149; AAN71719.1; -; Genomic_DNA.
DR EMBL; AL035526; CAB37456.1; -; Genomic_DNA.
DR EMBL; AL161549; CAB78873.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84079.1; -; Genomic_DNA.
DR EMBL; AY075699; AAL77705.1; -; mRNA.
DR EMBL; BT026031; ABG48387.1; -; mRNA.
DR EMBL; AY086529; AAM63594.1; -; mRNA.
DR EMBL; AK318990; BAH57105.1; -; mRNA.
DR EMBL; AK317697; BAH20356.1; -; mRNA.
DR PIR; T04863; T04863.
DR RefSeq; NP_193606.1; NM_117987.4. [Q39011-1]
DR AlphaFoldDB; Q39011; -.
DR SMR; Q39011; -.
DR BioGRID; 12898; 36.
DR DIP; DIP-46010N; -.
DR IntAct; Q39011; 17.
DR MINT; Q39011; -.
DR STRING; 3702.AT4G18710.1; -.
DR iPTMnet; Q39011; -.
DR PaxDb; Q39011; -.
DR PRIDE; Q39011; -.
DR ProteomicsDB; 237104; -. [Q39011-1]
DR EnsemblPlants; AT4G18710.1; AT4G18710.1; AT4G18710. [Q39011-1]
DR GeneID; 827605; -.
DR Gramene; AT4G18710.1; AT4G18710.1; AT4G18710. [Q39011-1]
DR KEGG; ath:AT4G18710; -.
DR Araport; AT4G18710; -.
DR TAIR; locus:2124082; AT4G18710.
DR eggNOG; KOG0658; Eukaryota.
DR InParanoid; Q39011; -.
DR OMA; HYTTKID; -.
DR OrthoDB; 990896at2759; -.
DR PhylomeDB; Q39011; -.
DR BRENDA; 2.7.11.26; 399.
DR PRO; PR:Q39011; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q39011; baseline and differential.
DR Genevisible; Q39011; AT.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004672; F:protein kinase activity; TAS:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0009729; P:detection of brassinosteroid stimulus; IMP:TAIR.
DR GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR GO; GO:1900458; P:negative regulation of brassinosteroid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IDA:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0048765; P:root hair cell differentiation; IGI:TAIR.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd14137; STKc_GSK3; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR039192; STKc_GSK3.
DR Pfam; PF00069; Pkinase; 1.
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 Alternative splicing; ATP-binding; Brassinosteroid signaling pathway;
KW Cell membrane; Cytoplasm; Host-virus interaction; Kinase; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..380
FT /note="Shaggy-related protein kinase eta"
FT /id="PRO_0000086222"
FT DOMAIN 40..324
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 46..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 200
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:21855796"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 261
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..6
FT /note="Missing (in isoform 2)"
FT /id="VSP_060065"
FT MUTAGEN 69
FT /note="K->R: Abolishes kinase activity. Altered BASL
FT exclusion from nucleus."
FT /evidence="ECO:0000269|PubMed:11847343,
FT ECO:0000269|PubMed:23496207, ECO:0000269|PubMed:30429609"
FT MUTAGEN 80
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:12427989"
FT MUTAGEN 200
FT /note="Y->F: Normal interaction with KIB1."
FT /evidence="ECO:0000269|PubMed:28575660"
FT MUTAGEN 261
FT /note="T->I: In bin2-2; brassinosteroid-insensitive dwarf
FT mutant; increased kinase activity."
FT /evidence="ECO:0000269|PubMed:11847343"
FT MUTAGEN 263
FT /note="E->K: In dwf12-2D/bin2-1; brassinosteroid-
FT insensitive dwarf mutant; increased kinase activity.
FT Reduced interaction with KIB1. Strongly reduced number of
FT stomata in hypocotyls as well as decreased stomatal index
FT in leaves."
FT /evidence="ECO:0000269|PubMed:11847343,
FT ECO:0000269|PubMed:12428015, ECO:0000269|PubMed:22466366,
FT ECO:0000269|PubMed:28575660"
FT MUTAGEN 264
FT /note="E->K: In dwf12-1D/ucu1-1/ucu1-2; brassinosteroid-
FT insensitive dwarf mutant."
FT /evidence="ECO:0000269|PubMed:11820813,
FT ECO:0000269|PubMed:12428015"
FT MUTAGEN 284
FT /note="P->S: In ucu1-3; leaves rolled spirally downward."
FT /evidence="ECO:0000269|PubMed:11820813"
FT CONFLICT 105
FT /note="S -> E (in Ref. 1; CAA64409 and 2; CAA70144)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="S -> T (in Ref. 1; CAA64409 and 2; CAA70144)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="M -> S (in Ref. 1; CAA64409 and 2; CAA70144)"
FT /evidence="ECO:0000305"
FT CONFLICT 157..159
FT /note="NVA -> SCP (in Ref. 1; CAA64409 and 2; CAA70144)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="A -> P (in Ref. 1; CAA64409 and 2; CAA70144)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="H -> N (in Ref. 1; CAA64409 and 2; CAA70144)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="R -> K (in Ref. 1; CAA64409 and 2; CAA70144)"
FT /evidence="ECO:0000305"
FT CONFLICT 298..300
FT /note="IDF -> VDL (in Ref. 1; CAA64409 and 2; CAA70144)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="L -> H (in Ref. 8; AAL77705)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="F -> L (in Ref. 1; CAA64409 and 2; CAA70144)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 43099 MW; 86C2FD5F77201168 CRC64;
MADDKEMPAA VVDGHDQVTG HIISTTIGGK NGEPKQTISY MAERVVGTGS FGIVFQAKCL
ETGETVAIKK VLQDRRYKNR ELQLMRVMDH PNVVCLKHCF FSTTSKDELF LNLVMEYVPE
SLYRVLKHYS SANQRMPLVY VKLYMYQIFR GLAYIHNVAG VCHRDLKPQN LLVDPLTHQV
KICDFGSAKQ LVKGEANISY ICSRFYRAPE LIFGATEYTT SIDIWSAGCV LAELLLGQPL
FPGENAVDQL VEIIKVLGTP TREEIRCMNP HYTDFRFPQI KAHPWHKIFH KRMPPEAIDF
ASRLLQYSPS LRCTALEACA HPFFDELREP NARLPNGRPF PPLFNFKQEV AGSSPELVNK
LIPDHIKRQL GLSFLNQSGT
