BAK1_ARATH
ID BAK1_ARATH Reviewed; 615 AA.
AC Q94F62; C0LGS0; Q9SZC0;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1 {ECO:0000303|PubMed:12150929};
DE Short=AtBAK1 {ECO:0000303|PubMed:12150929};
DE Short=BRI1-associated receptor kinase 1 {ECO:0000303|PubMed:12150929};
DE EC=2.7.10.1 {ECO:0000255|PROSITE-ProRule:PRU10027};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Protein ELONGATED;
DE AltName: Full=Somatic embryogenesis receptor kinase 3 {ECO:0000303|PubMed:11706164};
DE Short=AtSERK3 {ECO:0000303|PubMed:11706164};
DE AltName: Full=Somatic embryogenesis receptor-like kinase 3 {ECO:0000303|PubMed:11706164};
DE Flags: Precursor;
GN Name=BAK1 {ECO:0000303|PubMed:12150929};
GN Synonyms=ELG, SERK3 {ECO:0000303|PubMed:11706164};
GN OrderedLocusNames=At4g33430 {ECO:0000312|Araport:AT4G33430};
GN ORFNames=F17M5.190 {ECO:0000312|EMBL:CAB38801.1};
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].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11706164; DOI=10.1104/pp.010324;
RA Hecht V.F.G., Vielle-Calzada J.-P., Hartog M.V., Schmidt E.D.L.,
RA Boutilier K., Grossniklaus U., de Vries S.C.;
RT "The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1 gene is expressed
RT in developing ovules and embryos and enhances embryogenic competence in
RT culture.";
RL Plant Physiol. 127:803-816(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-317, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BRI1,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=12150929; DOI=10.1016/s0092-8674(02)00812-7;
RA Li J., Wen J., Lease K.A., Doke J.T., Tax F.E., Walker J.C.;
RT "BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1
RT and modulates brassinosteroid signaling.";
RL Cell 110:213-222(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [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 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 [5]
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 [6]
RP IDENTIFICATION.
RX PubMed=11523644; DOI=10.1007/s004250000471;
RA Baudino S., Hansen S., Brettschneider R., Hecht V.F.G., Dresselhaus T.,
RA Loerz H., Dumas C., Rogowsky P.M.;
RT "Molecular characterisation of two novel maize LRR receptor-like kinases,
RT which belong to the SERK gene family.";
RL Planta 213:1-10(2001).
RN [7]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH BRI1.
RX PubMed=12150928; DOI=10.1016/s0092-8674(02)00814-0;
RA Nam K.H., Li J.;
RT "BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling.";
RL Cell 110:203-212(2002).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH BRI1.
RX PubMed=15548744; DOI=10.1105/tpc.104.025387;
RA Russinova E., Borst J.-W., Kwaaitaal M., Cano-Delgado A., Yin Y., Chory J.,
RA de Vries S.C.;
RT "Heterodimerization and endocytosis of Arabidopsis brassinosteroid
RT receptors BRI1 and AtSERK3 (BAK1).";
RL Plant Cell 16:3216-3229(2004).
RN [9]
RP PHOSPHORYLATION AT SER-290; THR-446; THR-449 AND THR-455, AND INTERACTION
RP WITH BRI1.
RX PubMed=15894717; DOI=10.1105/tpc.105.031393;
RA Wang X., Goshe M.B., Soderblom E.J., Phinney B.S., Kuchar J.A., Li J.,
RA Asami T., Yoshida S., Huber S.C., Clouse S.D.;
RT "Identification and functional analysis of in vivo phosphorylation sites of
RT the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase.";
RL Plant Cell 17:1685-1703(2005).
RN [10]
RP MUTAGENESIS OF ASP-122.
RX PubMed=16126860; DOI=10.1104/pp.105.064444;
RA Whippo C.W., Hangarter R.P.;
RT "A brassinosteroid-hypersensitive mutant of BAK1 indicates that a
RT convergence of photomorphogenic and hormonal signaling modulates
RT phototropism.";
RL Plant Physiol. 139:448-457(2005).
RN [11]
RP IDENTIFICATION IN THE SERK1 COMPLEX.
RX PubMed=16473966; DOI=10.1105/tpc.105.039412;
RA Karlova R., Boeren S., Russinova E., Aker J., Vervoort J., de Vries S.C.;
RT "The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 protein
RT complex includes BRASSINOSTEROID-INSENSITIVE1.";
RL Plant Cell 18:626-638(2006).
RN [12]
RP INTERACTION WITH FLS2.
RX PubMed=17626179; DOI=10.1073/pnas.0705306104;
RA Heese A., Hann D.R., Gimenez-Ibanez S., Jones A.M.E., He K., Li J.,
RA Schroeder J.I., Peck S.C., Rathjen J.P.;
RT "The receptor-like kinase SERK3/BAK1 is a central regulator of innate
RT immunity in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12217-12222(2007).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17600708; DOI=10.1016/j.cub.2007.05.036;
RA He K., Gou X., Yuan T., Lin H., Asami T., Yoshida S., Russell S.D., Li J.;
RT "BAK1 and BKK1 regulate brassinosteroid-dependent growth and
RT brassinosteroid-independent cell-death pathways.";
RL Curr. Biol. 17:1109-1115(2007).
RN [14]
RP FUNCTION.
RX PubMed=17583510; DOI=10.1016/j.cub.2007.05.046;
RA Kemmerling B., Schwedt A., Rodriguez P., Mazzotta S., Frank M., Qamar S.A.,
RA Mengiste T., Betsuyaku S., Parker J.E., Mussig C., Thomma B.P.,
RA Albrecht C., de Vries S.C., Hirt H., Nurnberger T.;
RT "The BRI1-associated kinase 1, BAK1, has a brassinolide-independent role in
RT plant cell-death control.";
RL Curr. Biol. 17:1116-1122(2007).
RN [15]
RP INTERACTION WITH FLS2, AND DISRUPTION PHENOTYPE.
RX PubMed=17625569; DOI=10.1038/nature05999;
RA Chinchilla D., Zipfel C., Robatzek S., Kemmerling B., Nuernberger T.,
RA Jones J.D.G., Felix G., Boller T.;
RT "A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant
RT defence.";
RL Nature 448:497-500(2007).
RN [16]
RP MUTAGENESIS OF THR-312; LYS-317 AND THR-546, AND INTERACTION WITH THE
RP KINASE-INTERACTING FHA DOMAIN OF KAPP.
RX PubMed=17302430; DOI=10.1021/bi061763n;
RA Ding Z., Wang H., Liang X., Morris E.R., Gallazzi F., Pandit S.,
RA Skolnick J., Walker J.C., Van Doren S.R.;
RT "Phosphoprotein and phosphopeptide interactions with the FHA domain from
RT Arabidopsis kinase-associated protein phosphatase.";
RL Biochemistry 46:2684-2696(2007).
RN [17]
RP SUBUNIT.
RX PubMed=17905839; DOI=10.1529/biophysj.107.112003;
RA Hink M.A., Shah K., Russinova E., de Vries S.C., Visser A.J.;
RT "Fluorescence fluctuation analysis of Arabidopsis thaliana somatic
RT embryogenesis receptor-like kinase and brassinosteroid insensitive 1
RT receptor oligomerization.";
RL Biophys. J. 94:1052-1062(2008).
RN [18]
RP INTERACTION WITH PSEUDOMONAS SYRINGAE AVRPTO AND AVRPTOB/HOPAB2.
RX PubMed=18621007; DOI=10.1016/j.chom.2008.05.017;
RA Shan L., He P., Li J., Heese A., Peck S.C., Nurnberger T., Martin G.B.,
RA Sheen J.;
RT "Bacterial effectors target the common signaling partner BAK1 to disrupt
RT multiple MAMP receptor-signaling complexes and impede plant immunity.";
RL Cell Host Microbe 4:17-27(2008).
RN [19]
RP FUNCTION, PHOSPHORYLATION AT SER-286; SER-290; THR-312; THR-446; THR-449;
RP THR-450 AND THR-455, INTERACTION WITH BRI1, AND MUTAGENESIS OF THR-455.
RX PubMed=18694562; DOI=10.1016/j.devcel.2008.06.011;
RA Wang X., Kota U., He K., Blackburn K., Li J., Goshe M.B., Huber S.C.,
RA Clouse S.D.;
RT "Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex
RT impacts early events in brassinosteroid signaling.";
RL Dev. Cell 15:220-235(2008).
RN [20]
RP FUNCTION.
RX PubMed=18667726; DOI=10.1104/pp.108.123216;
RA Albrecht C., Russinova E., Kemmerling B., Kwaaitaal M., de Vries S.C.;
RT "Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE proteins serve
RT brassinosteroid-dependent and -independent signaling pathways.";
RL Plant Physiol. 148:611-619(2008).
RN [21]
RP INTERACTION WITH ERD13.
RX PubMed=19118534; DOI=10.1016/j.bbrc.2008.11.156;
RA Ryu H.Y., Kim S.Y., Park H.M., You J.Y., Kim B.H., Lee J.S., Nam K.H.;
RT "Modulations of AtGSTF10 expression induce stress tolerance and BAK1-
RT mediated cell death.";
RL Biochem. Biophys. Res. Commun. 379:417-422(2009).
RN [22]
RP INTERACTION WITH MSBP1, AND SUBCELLULAR LOCATION.
RX PubMed=19532123; DOI=10.1038/cr.2009.66;
RA Song L., Shi Q.M., Yang X.H., Xu Z.H., Xue H.W.;
RT "Membrane steroid-binding protein 1 (MSBP1) negatively regulates
RT brassinosteroid signaling by enhancing the endocytosis of BAK1.";
RL Cell Res. 19:864-876(2009).
RN [23]
RP AUTOPHOSPHORYLATION, AND PHOSPHORYLATION AT SER-290; THR-446; THR-449;
RP THR-450; THR-455; THR-589; SER-595; SER-604 AND SER-612.
RX PubMed=19105183; DOI=10.1002/pmic.200701059;
RA Karlova R., Boeren S., van Dongen W., Kwaaitaal M., Aker J., Vervoort J.,
RA de Vries S.C.;
RT "Identification of in vitro phosphorylation sites in the Arabidopsis
RT thaliana somatic embryogenesis receptor-like kinases.";
RL Proteomics 9:368-379(2009).
RN [24]
RP MUTAGENESIS OF LEU-32; LEU-46; CYS-64; LEU-94; LEU-121; SER-172; LYS-317;
RP THR-446; THR-449; THR-450 AND THR-455.
RX PubMed=19277500; DOI=10.1007/s10059-009-0023-1;
RA Yun H.S., Bae Y.H., Lee Y.J., Chang S.C., Kim S.-K., Li J., Nam K.H.;
RT "Analysis of phosphorylation of the BRI1/BAK1 complex in arabidopsis
RT reveals amino acid residues critical for receptor formation and activation
RT of BR signaling.";
RL Mol. Cells 27:183-190(2009).
RN [25]
RP FUNCTION, AND AUTOPHOSPHORYLATION.
RX PubMed=19124768; DOI=10.1073/pnas.0810249106;
RA Oh M.-H., Wang X., Kota U., Goshe M.B., Clouse S.D., Huber S.C.;
RT "Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a
RT component of brassinosteroid signaling in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:658-663(2009).
RN [26]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY FLAGELLIN AND HARPIN, AND
RP INTERACTION WITH PEPR1 AND PEPR2.
RX PubMed=20018402; DOI=10.1016/j.ejcb.2009.11.001;
RA Postel S., Kuefner I., Beuter C., Mazzotta S., Schwedt A., Borlotti A.,
RA Halter T., Kemmerling B., Nuernberger T.;
RT "The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated
RT in Arabidopsis development and immunity.";
RL Eur. J. Cell Biol. 89:169-174(2010).
RN [27]
RP INTERACTION WITH FLS2, AND PHOSPHORYLATION.
RX PubMed=20103591; DOI=10.1074/jbc.m109.096842;
RA Schulze B., Mentzel T., Jehle A.K., Mueller K., Beeler S., Boller T.,
RA Felix G., Chinchilla D.;
RT "Rapid heteromerization and phosphorylation of ligand-activated plant
RT transmembrane receptors and their associated kinase BAK1.";
RL J. Biol. Chem. 285:9444-9451(2010).
RN [28]
RP FUNCTION.
RX PubMed=20404519; DOI=10.4161/psb.11500;
RA Lu D., Wu S., He P., Shan L.;
RT "Phosphorylation of receptor-like cytoplasmic kinases by bacterial
RT flagellin.";
RL Plant Signal. Behav. 5:598-600(2010).
RN [29]
RP RETRACTED PAPER.
RX PubMed=20876109; DOI=10.1073/pnas.0915064107;
RA Oh M.H., Wang X., Wu X., Zhao Y., Clouse S.D., Huber S.C.;
RT "Autophosphorylation of Tyr-610 in the receptor kinase BAK1 plays a role in
RT brassinosteroid signaling and basal defense gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17827-17832(2010).
RN [30]
RP RETRACTION NOTICE OF PUBMED:20876109.
RX PubMed=27325779; DOI=10.1073/pnas.1608778113;
RA Oh M.H., Wang X., Wu X., Zhao Y., Clouse S.D., Huber S.C.;
RL Proc. Natl. Acad. Sci. U.S.A. 113:E3987-E3987(2016).
RN [31]
RP FUNCTION, AND INTERACTION WITH EFR AND FLS2.
RC STRAIN=cv. Columbia;
RX PubMed=21693696; DOI=10.1105/tpc.111.084301;
RA Roux M., Schwessinger B., Albrecht C., Chinchilla D., Jones A., Holton N.,
RA Malinovsky F.G., Tor M., de Vries S., Zipfel C.;
RT "The Arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and
RT BKK1/SERK4 are required for innate immunity to hemibiotrophic and
RT biotrophic pathogens.";
RL Plant Cell 23:2440-2455(2011).
RN [32]
RP RETRACTED PAPER.
RX PubMed=21350342; DOI=10.4161/psb.6.3.14337;
RA Oh M.H., Wu X., Clouse S.D., Huber S.C.;
RT "Functional importance of BAK1 tyrosine phosphorylation in vivo.";
RL Plant Signal. Behav. 6:400-405(2011).
RN [33]
RP RETRACTION NOTICE OF PUBMED:21350342.
RX PubMed=27603314; DOI=10.1080/15592324.2016.1211452;
RA Oh M.H., Wu X., Clouse S.D., Huber S.C.;
RL Plant Signal. Behav. 11:e1211452-e1211452(2016).
RN [34]
RP INTERACTION WITH TMK4/BARK1.
RX PubMed=23921992; DOI=10.1093/pcp/pct106;
RA Kim M.H., Kim Y., Kim J.W., Lee H.S., Lee W.S., Kim S.K., Wang Z.Y.,
RA Kim S.H.;
RT "Identification of Arabidopsis BAK1-associating receptor-like kinase 1
RT (BARK1) and characterization of its gene expression and brassinosteroid-
RT regulated root phenotypes.";
RL Plant Cell Physiol. 54:1620-1634(2013).
RN [35]
RP FUNCTION, MUTAGENESIS OF SER-290; THR-312; LYS-317; THR-446; THR-449;
RP THR-450 AND THR-455, INTERACTION WITH BIR2, AND AUTOPHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=24388849; DOI=10.1016/j.cub.2013.11.047;
RA Halter T., Imkampe J., Mazzotta S., Wierzba M., Postel S., Buecherl C.,
RA Kiefer C., Stahl M., Chinchilla D., Wang X., Nuernberger T., Zipfel C.,
RA Clouse S., Borst J.W., Boeren S., de Vries S.C., Tax F., Kemmerling B.;
RT "The leucine-rich repeat receptor kinase BIR2 is a negative regulator of
RT BAK1 in plant immunity.";
RL Curr. Biol. 24:134-143(2014).
RN [36]
RP FUNCTION, AND INTERACTION WITH BIR2.
RX PubMed=24556575; DOI=10.1016/j.jsb.2014.02.005;
RA Blaum B.S., Mazzotta S., Noeldeke E.R., Halter T., Madlung J.,
RA Kemmerling B., Stehle T.;
RT "Structure of the pseudokinase domain of BIR2, a regulator of BAK1-mediated
RT immune signaling in Arabidopsis.";
RL J. Struct. Biol. 186:112-121(2014).
RN [37]
RP INTERACTION WITH ERECTA; ERL1 AND TMM.
RX PubMed=26320950; DOI=10.1016/j.cub.2015.07.068;
RA Meng X., Chen X., Mang H., Liu C., Yu X., Gao X., Torii K.U., He P.,
RA Shan L.;
RT "Differential function of Arabidopsis SERK family receptor-like kinases in
RT stomatal patterning.";
RL Curr. Biol. 25:2361-2372(2015).
RN [38]
RP FUNCTION, SUBUNIT, AND COMPONENT OF THE RLP23-SOBIR1-BAK1 COMPLEX.
RX PubMed=27251392; DOI=10.1038/nplants.2015.140;
RA Albert I., Boehm H., Albert M., Feiler C.E., Imkampe J., Wallmeroth N.,
RA Brancato C., Raaymakers T.M., Oome S., Zhang H., Krol E., Grefen C.,
RA Gust A.A., Chai J., Hedrich R., Van den Ackerveken G., Nuernberger T.;
RT "An RLP23-SOBIR1-BAK1 complex mediates NLP-triggered immunity.";
RL Nat. Plants 1:15140-15140(2015).
RN [39]
RP FUNCTION, INTERACTION WITH CNGC17 AND PSKR1, AND SUBCELLULAR LOCATION.
RX PubMed=26071421; DOI=10.1105/tpc.15.00306;
RA Ladwig F., Dahlke R.I., Stuehrwohldt N., Hartmann J., Harter K., Sauter M.;
RT "Phytosulfokine regulates growth in Arabidopsis through a response module
RT at the plasma membrane that includes CYCLIC NUCLEOTIDE-GATED CHANNEL17, H+-
RT ATPase, and BAK1.";
RL Plant Cell 27:1718-1729(2015).
RN [40]
RP FUNCTION, AND INTERACTION WITH RGI3/RGFR1 AND RGI4/RGFR2/SKM2.
RC STRAIN=cv. Columbia;
RX PubMed=27229311; DOI=10.1038/cr.2016.62;
RA Song W., Liu L., Wang J., Wu Z., Zhang H., Tang J., Lin G., Wang Y.,
RA Wen X., Li W., Han Z., Guo H., Chai J.;
RT "Signature motif-guided identification of receptors for peptide hormones
RT essential for root meristem growth.";
RL Cell Res. 26:674-685(2016).
RN [41]
RP INTERACTION WITH IOS1.
RX PubMed=27317676; DOI=10.1105/tpc.16.00313;
RA Yeh Y.-H., Panzeri D., Kadota Y., Huang Y.-C., Huang P.-Y., Tao C.-N.,
RA Roux M., Chien H.-C., Chin T.-C., Chu P.-W., Zipfel C., Zimmerli L.;
RT "The Arabidopsis malectin-like/LRR-RLK IOS1 is critical for BAK1-dependent
RT and BAK1-independent pattern-triggered immunity.";
RL Plant Cell 28:1701-1721(2016).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 250-590 IN COMPLEX WITH
RP HOPAB2/AVRPTOB, PHOSPHORYLATION AT THR-446; THR-449 AND THR-450, AND
RP MUTAGENESIS OF LYS-317; THR-449; THR-450; ALA-451; VAL-452; THR-455;
RP ILE-456; HIS-458; LEU-464 AND ALA-495.
RX PubMed=22169508; DOI=10.1016/j.chom.2011.10.013;
RA Cheng W., Munkvold K.R., Gao H., Mathieu J., Schwizer S., Wang S.,
RA Yan Y.B., Wang J., Martin G.B., Chai J.;
RT "Structural analysis of Pseudomonas syringae AvrPtoB bound to host BAK1
RT reveals two similar kinase-interacting domains in a type III Effector.";
RL Cell Host Microbe 10:616-626(2011).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 258-583 IN COMPLEX WITH ATP
RP ANALOG, PHOSPHORYLATION AT SER-290; THR-312; THR-446; THR-449; THR-450 AND
RP THR-455, AND MUTAGENESIS OF TYR-363; ASP-416; ASN-421; LYS-439; THR-450;
RP ARG-453 AND HIS-458.
RX PubMed=22547027; DOI=10.1038/cr.2012.74;
RA Yan L., Ma Y., Liu D., Wei X., Sun Y., Chen X., Zhao H., Zhou J., Wang Z.,
RA Shui W., Lou Z.;
RT "Structural basis for the impact of phosphorylation on the activation of
RT plant receptor-like kinase BAK1.";
RL Cell Res. 22:1304-1308(2012).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 1-220 IN COMPLEX WITH FLS2 AND
RP FLG22, DISULFIDE BONDS, SUBUNIT, AND MUTAGENESIS OF ASP-30; PHE-60; TYR-96
RP AND PHE-144.
RX PubMed=24114786; DOI=10.1126/science.1243825;
RA Sun Y., Li L., Macho A.P., Han Z., Hu Z., Zipfel C., Zhou J.M., Chai J.;
RT "Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1
RT immune complex.";
RL Science 342:624-628(2013).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 26-220 IN COMPLEX WITH
RP BRASSINOLIDE, AND DISULFIDE BONDS.
RA Sun Y., Han Z., Chai J.;
RT "Structural insight into BL-induced activation of the BRI1-BAK1 complex.";
RL Submitted (AUG-2013) to the PDB data bank.
CC -!- FUNCTION: Dual specificity kinase acting on both serine/threonine- and
CC tyrosine-containing substrates. Controls the expression of genes
CC associated with innate immunity in the absence of pathogens or
CC elicitors. Involved in brassinosteroid (BR) signal transduction.
CC Phosphorylates BRI1. May be involved in changing the equilibrium
CC between plasma membrane-located BRI1 homodimers and endocytosed BRI1-
CC BAK1 heterodimers. Interaction with MSBP1 stimulates the endocytosis of
CC BAK1 and suppresses brassinosteroid signaling. Acts in pathogen-
CC associated molecular pattern (PAMP)-triggered immunity (PTI) via its
CC interactions with FLS2 and EFR, and the phosphorylation of BIK1.
CC Involved in programmed cell death (PCD) control. Positively regulates
CC the BR-dependent plant growth pathway and negatively regulates the BR-
CC independent cell-death pathway (PubMed:17583510, PubMed:17600708,
CC PubMed:18667726, PubMed:18694562, PubMed:19124768, PubMed:20018402,
CC PubMed:20404519, PubMed:21693696). Phosphorylates BIR2 and thus
CC promotes interaction with BIR2 (PubMed:24388849, PubMed:24556575). This
CC interaction prevents interaction with FLS2 in the absence of pathogen-
CC associated molecular patterns (PAMP) (PubMed:24388849,
CC PubMed:24556575). Component of the RLP23-SOBIR1-BAK1 complex that
CC mediates NLP-triggered immunity (PubMed:27251392). Required for PSK
CC promotion of seedling growth and protoplast expansion
CC (PubMed:26071421). CNGC17 and AHAs form a functional cation-
CC translocating unit that is activated by PSKR1/BAK1 and possibly other
CC BAK1/RLK complexes (PubMed:26071421). Probably required during small
CC peptide (e.g. RGF1) signaling (Probable). {ECO:0000269|PubMed:17583510,
CC ECO:0000269|PubMed:17600708, ECO:0000269|PubMed:18667726,
CC ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:19124768,
CC ECO:0000269|PubMed:20018402, ECO:0000269|PubMed:20404519,
CC ECO:0000269|PubMed:21693696, ECO:0000269|PubMed:24388849,
CC ECO:0000269|PubMed:24556575, ECO:0000269|PubMed:26071421,
CC ECO:0000269|PubMed:27251392, ECO:0000305|PubMed:27229311}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC -!- SUBUNIT: Interacts constitutively with BIR2, thereby preventing
CC interaction with the ligand-binding LRR-RLK FLS2. Upon infection,
CC pathogen-associated molecular patterns (PAMP) perception leads to BIR2
CC release from the BAK1 complex and enables the recruitment of BAK1 into
CC the FLS2 complex (PubMed:24388849, PubMed:24556575). Heterodimer with
CC FLS2 (PubMed:24114786). Monomer. Heterodimer with BRI1 in the
CC endosomes. Component of the SERK1 signaling complex, composed of KAPP,
CC CDC48A, GRF6 or GRF7, SERK1, SERK2, SERK3/BAK1 and BRI1. Interacts with
CC the P.syringae AvrPto and hopAB2/AvrPtoB, ERD13, PEPR1 and PEPR2.
CC Interacts (via extracellular region) with MSBP1. Interacts with the EF-
CC Tu receptor EFR and FLS2 in a specific ligand-induced manner. Interacts
CC with TMK4/BARK1. Part of a functional complex containing PSKR1, BAK1,
CC CNGC17, and AHA (PubMed:26071421). Interacts with CNGC17 and PSKR1
CC (PubMed:26071421). Binds to IOS1 which triggers FLS2-BAK1 complex
CC formation upon microbe-associated molecular patterns (MAMPs) treatment
CC (PubMed:27317676). Interacts with ERECTA in a EPF2-induced manner.
CC Interacts with ERL1 in a EPF1-induced manner. Interacts with TMM
CC (PubMed:26320950). Component of a trimeric complex composed of RLP23,
CC SOBIR1 and BAK1. BAK1 is recruited into a pre-formed RLP23-SOBIR1
CC complex in a ligand-dependent manner (PubMed:27251392). In the presence
CC of the signal peptide RGF1, interacts with RGI3/RGFR1 and
CC RGI4/RGFR2/SKM2 (PubMed:27229311). {ECO:0000269|PubMed:12150928,
CC ECO:0000269|PubMed:12150929, ECO:0000269|PubMed:15548744,
CC ECO:0000269|PubMed:15894717, ECO:0000269|PubMed:16473966,
CC ECO:0000269|PubMed:17302430, ECO:0000269|PubMed:17625569,
CC ECO:0000269|PubMed:17626179, ECO:0000269|PubMed:17905839,
CC ECO:0000269|PubMed:18621007, ECO:0000269|PubMed:18694562,
CC ECO:0000269|PubMed:19118534, ECO:0000269|PubMed:19532123,
CC ECO:0000269|PubMed:20018402, ECO:0000269|PubMed:20103591,
CC ECO:0000269|PubMed:21693696, ECO:0000269|PubMed:23921992,
CC ECO:0000269|PubMed:24114786, ECO:0000269|PubMed:24388849,
CC ECO:0000269|PubMed:24556575, ECO:0000269|PubMed:26071421,
CC ECO:0000269|PubMed:26320950, ECO:0000269|PubMed:27229311,
CC ECO:0000269|PubMed:27251392, ECO:0000269|PubMed:27317676}.
CC -!- INTERACTION:
CC Q94F62; O04567: At1g27190; NbExp=2; IntAct=EBI-617138, EBI-1238687;
CC Q94F62; C0LGI5: At1g69990; NbExp=4; IntAct=EBI-617138, EBI-20651225;
CC Q94F62; Q9ZQR3: At2g14510; NbExp=2; IntAct=EBI-617138, EBI-20651957;
CC Q94F62; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-617138, EBI-16902452;
CC Q94F62; Q9ASS4: At5g48380; NbExp=6; IntAct=EBI-617138, EBI-6298290;
CC Q94F62; Q94F62: BAK1; NbExp=4; IntAct=EBI-617138, EBI-617138;
CC Q94F62; O48814: BIK1; NbExp=5; IntAct=EBI-617138, EBI-1238176;
CC Q94F62; O22476: BRI1; NbExp=9; IntAct=EBI-617138, EBI-1797828;
CC Q94F62; Q9ZWC8: BRL1; NbExp=7; IntAct=EBI-617138, EBI-590903;
CC Q94F62; Q9LJF3: BRL3; NbExp=2; IntAct=EBI-617138, EBI-20651413;
CC Q94F62; C0LGT6: EFR; NbExp=3; IntAct=EBI-617138, EBI-8801168;
CC Q94F62; Q42371: ERECTA; NbExp=4; IntAct=EBI-617138, EBI-16940407;
CC Q94F62; C0LGW6: ERL1; NbExp=4; IntAct=EBI-617138, EBI-16914248;
CC Q94F62; Q6XAT2: ERL2; NbExp=4; IntAct=EBI-617138, EBI-16895926;
CC Q94F62; Q9FL28: FLS2; NbExp=19; IntAct=EBI-617138, EBI-1799448;
CC Q94F62; C0LGX3: HSL2; NbExp=2; IntAct=EBI-617138, EBI-16904927;
CC Q94F62; Q9C8I6: IOS1; NbExp=2; IntAct=EBI-617138, EBI-16924837;
CC Q94F62; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-617138, EBI-20651739;
CC Q94F62; Q9LFS4: NIK1; NbExp=4; IntAct=EBI-617138, EBI-16146189;
CC Q94F62; Q8RY65: NIK2; NbExp=2; IntAct=EBI-617138, EBI-20664696;
CC Q94F62; Q9ZVR7: PSKR1; NbExp=5; IntAct=EBI-617138, EBI-16172949;
CC Q94F62; Q9C7S5: PSY1R; NbExp=2; IntAct=EBI-617138, EBI-16904988;
CC Q94F62; Q9ZRF9: RPK1; NbExp=4; IntAct=EBI-617138, EBI-1238953;
CC Q94F62; Q94AG2: SERK1; NbExp=6; IntAct=EBI-617138, EBI-1555537;
CC Q94F62; Q9SKG5: SERK4; NbExp=4; IntAct=EBI-617138, EBI-6290483;
CC Q94F62; Q8LPS5: SERK5; NbExp=4; IntAct=EBI-617138, EBI-16887868;
CC Q94F62; Q06BH3: SRF1; NbExp=2; IntAct=EBI-617138, EBI-16955764;
CC Q94F62; Q6R2K3: SRF3; NbExp=2; IntAct=EBI-617138, EBI-20651925;
CC Q94F62; Q6R2K1: SRF5; NbExp=4; IntAct=EBI-617138, EBI-20651875;
CC Q94F62; Q9C8M9: SRF6; NbExp=4; IntAct=EBI-617138, EBI-16954301;
CC Q94F62; Q9LUL4: SRF7; NbExp=2; IntAct=EBI-617138, EBI-16964596;
CC Q94F62; Q8RWZ1: SUB; NbExp=4; IntAct=EBI-617138, EBI-17072125;
CC Q94F62; P21184: fliC; Xeno; NbExp=5; IntAct=EBI-617138, EBI-16077660;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12150928,
CC ECO:0000269|PubMed:12150929, ECO:0000269|PubMed:15548744,
CC ECO:0000269|PubMed:26071421}; Single-pass type I membrane protein
CC {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:15548744}; Single-
CC pass type I membrane protein {ECO:0000255}. Note=Endocytosis enhanced
CC upon interaction with MSBP1. {ECO:0000269|PubMed:19532123}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q94F62-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:12150929}.
CC -!- INDUCTION: Up-regulated by flagellin and harpin.
CC {ECO:0000269|PubMed:20018402}.
CC -!- DOMAIN: Contains one leucine-zipper motif and one pair of
CC conservatively spaced Cys (Cys pair) involved in forming heterodimers.
CC -!- PTM: Autophosphorylated on Ser-290, Thr-312, Thr-446, Thr-449, Thr-455
CC and Tyr-610. Probable autophosphorylation on additional Tyr residues.
CC Transphosphorylated by BRI1. It is not sure whether Thr-589 or Ser-595
CC is the target of the phosphorylation. The phosphorylations on Thr and
CC Tyr are induced by brassinolide. Phosphorylation at Ser-286, Ser-290
CC Thr-446 or Thr-449 is not critical for flagellin signaling.
CC {ECO:0000269|PubMed:12150928, ECO:0000269|PubMed:12150929,
CC ECO:0000269|PubMed:15894717, ECO:0000269|PubMed:18694562,
CC ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:20103591,
CC ECO:0000269|PubMed:24388849}.
CC -!- DISRUPTION PHENOTYPE: Semi-dwarfed phenotype, altered leaf morphology
CC and reduced sensitivity to brassinolide and flagellin. Enhanced
CC chlorosis and lesion formation upon pathogen infection. Bak1 and bkk1
CC double mutants are seedling lethal. {ECO:0000269|PubMed:12150929,
CC ECO:0000269|PubMed:17600708, ECO:0000269|PubMed:17625569,
CC ECO:0000269|PubMed:20018402}.
CC -!- MISCELLANEOUS: Interaction with BRI1 activates both receptor kinases
CC and the full activation of either receptor kinase requires
CC transphosphorylation by their partners. This interaction in vitro is
CC magnesium dependent. Instantaneous heteromeric complex formation
CC between FLS2 and BAK1 and reciprocal transphosphorylation after binding
CC of the flagellin flg22 ligand to FLS2. The kinase activity is not
CC required for the complex formation.
CC -!- MISCELLANEOUS: The interaction with the bacterial effectors AvrPto and
CC AvrPtoB/hopAB2 interfers with FLS2 binding and plant immunity.
CC -!- MISCELLANEOUS: Phosphorylated residues T-450 and T-455 have stronger
CC functional effects than other phosphorylated residues by interacting
CC with both the catalytic and activation loops to achieve a
CC conformational stability, locking BAK1 kinase in the active
CC conformation. {ECO:0000305|PubMed:22547027}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: An article reported the role of autophosphorylation of Tyr-610
CC in brassinosteroid signaling; however, this paper was later retracted.
CC A second article from the same group reported the role of
CC phosphorylation; however, this paper was also retracted.
CC {ECO:0000305|PubMed:20876109, ECO:0000305|PubMed:21350342,
CC ECO:0000305|PubMed:27325779, ECO:0000305|PubMed:27603314}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB38801.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80060.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF384970; AAK68074.1; -; mRNA.
DR EMBL; FJ708762; ACN59355.1; -; mRNA.
DR EMBL; AL035678; CAB38801.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161583; CAB80060.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86223.1; -; Genomic_DNA.
DR PIR; T05994; T05994.
DR RefSeq; NP_567920.1; NM_119497.5. [Q94F62-1]
DR PDB; 3TL8; X-ray; 2.50 A; A/D/G/H=250-590.
DR PDB; 3UIM; X-ray; 2.20 A; A=258-583.
DR PDB; 3ULZ; X-ray; 2.60 A; A=258-583.
DR PDB; 4M7E; X-ray; 3.60 A; C/D=26-220.
DR PDB; 4MN8; X-ray; 3.06 A; B=1-220.
DR PDBsum; 3TL8; -.
DR PDBsum; 3UIM; -.
DR PDBsum; 3ULZ; -.
DR PDBsum; 4M7E; -.
DR PDBsum; 4MN8; -.
DR AlphaFoldDB; Q94F62; -.
DR SMR; Q94F62; -.
DR BioGRID; 14764; 71.
DR DIP; DIP-34976N; -.
DR IntAct; Q94F62; 79.
DR iPTMnet; Q94F62; -.
DR PRIDE; Q94F62; -.
DR ProteomicsDB; 241199; -. [Q94F62-1]
DR EnsemblPlants; AT4G33430.1; AT4G33430.1; AT4G33430. [Q94F62-1]
DR GeneID; 829480; -.
DR Gramene; AT4G33430.1; AT4G33430.1; AT4G33430. [Q94F62-1]
DR KEGG; ath:AT4G33430; -.
DR Araport; AT4G33430; -.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; Q94F62; -.
DR PhylomeDB; Q94F62; -.
DR PRO; PR:Q94F62; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94F62; baseline and differential.
DR Genevisible; Q94F62; AT.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
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 InterPro; IPR031048; SERK.
DR PANTHER; PTHR47988:SF23; PTHR47988:SF23; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
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 3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW Disulfide bond; Endosome; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Plant defense; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..615
FT /note="BRASSINOSTEROID INSENSITIVE 1-associated receptor
FT kinase 1"
FT /id="PRO_0000024304"
FT TOPO_DOM 26..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 67..90
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 91..115
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 117..139
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 140..163
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 165..188
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 190..209
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT DOMAIN 289..576
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 57..64
FT /note="Cys pair"
FT /evidence="ECO:0000255"
FT ACT_SITE 416
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 59..62
FT /ligand="brassinolide"
FT /ligand_id="ChEBI:CHEBI:28277"
FT /evidence="ECO:0000269|Ref.45"
FT BINDING 295..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22547027"
FT BINDING 317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 364..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22547027"
FT BINDING 418
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22547027"
FT SITE 52
FT /note="Interacts with flagellin flg22"
FT /evidence="ECO:0000269|PubMed:24114786"
FT SITE 54
FT /note="Interacts with flagellin flg22; via amide nitrogen"
FT /evidence="ECO:0000269|PubMed:24114786"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18694562"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:19105183,
FT ECO:0000269|PubMed:22547027"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18694562,
FT ECO:0000269|PubMed:22547027"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 446
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:19105183,
FT ECO:0000269|PubMed:22169508, ECO:0000269|PubMed:22547027"
FT MOD_RES 449
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:19105183,
FT ECO:0000269|PubMed:22169508, ECO:0000269|PubMed:22547027"
FT MOD_RES 450
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18694562,
FT ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:22169508,
FT ECO:0000269|PubMed:22547027"
FT MOD_RES 455
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15894717,
FT ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:19105183,
FT ECO:0000269|PubMed:22547027"
FT MOD_RES 463
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 546
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 589
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105183"
FT CARBOHYD 79
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 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 57..64
FT /evidence="ECO:0000269|PubMed:24114786, ECO:0000269|Ref.45"
FT MUTAGEN 30
FT /note="D->Y: No effect on flg22 induced FLS2-BAK1
FT heterodimerization."
FT /evidence="ECO:0000269|PubMed:24114786"
FT MUTAGEN 32
FT /note="L->E: Loss of binding to BRI1, but no effect on
FT kinase activity."
FT /evidence="ECO:0000269|PubMed:19277500"
FT MUTAGEN 46
FT /note="L->E: Loss of binding to BRI1 and loss of kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:19277500"
FT MUTAGEN 60
FT /note="F->A: Loss of flg22 induced FLS2-BAK1
FT heterodimerization."
FT /evidence="ECO:0000269|PubMed:24114786"
FT MUTAGEN 64
FT /note="C->Y: No effect."
FT /evidence="ECO:0000269|PubMed:19277500"
FT MUTAGEN 94
FT /note="L->E: No effect."
FT /evidence="ECO:0000269|PubMed:19277500"
FT MUTAGEN 96
FT /note="Y->A: Loss of flg22 induced FLS2-BAK1
FT heterodimerization."
FT /evidence="ECO:0000269|PubMed:24114786"
FT MUTAGEN 121
FT /note="L->E: No effect."
FT /evidence="ECO:0000269|PubMed:19277500"
FT MUTAGEN 122
FT /note="D->N: Hypersensitivity to brassinosteroids and
FT enhanced high-light phototropism."
FT /evidence="ECO:0000269|PubMed:16126860"
FT MUTAGEN 144
FT /note="F->A: Loss of flg22 induced FLS2-BAK1
FT heterodimerization."
FT /evidence="ECO:0000269|PubMed:24114786"
FT MUTAGEN 172
FT /note="S->F: No effect."
FT /evidence="ECO:0000269|PubMed:19277500"
FT MUTAGEN 286
FT /note="S->A: No effect."
FT MUTAGEN 286
FT /note="S->D: Loss of kinase activity."
FT MUTAGEN 290
FT /note="S->A: Reduced kinase activity. Reduced interaction
FT with BIR2."
FT /evidence="ECO:0000269|PubMed:24388849"
FT MUTAGEN 290
FT /note="S->D: Normal interaction with BIR2."
FT /evidence="ECO:0000269|PubMed:24388849"
FT MUTAGEN 312
FT /note="T->A: No effect on the kinase activity or on the
FT binding to the FHA domain of KAPP. Reduced interaction with
FT BIR2."
FT /evidence="ECO:0000269|PubMed:17302430,
FT ECO:0000269|PubMed:24388849"
FT MUTAGEN 312
FT /note="T->D: Reduced interaction with BIR2."
FT /evidence="ECO:0000269|PubMed:24388849"
FT MUTAGEN 317
FT /note="K->E: Loss of kinase activity and loss of
FT interaction with hopAB2/AvrPtoB, but no effect on the
FT binding to the FHA domain of KAPP. Reduced interaction with
FT BIR2."
FT /evidence="ECO:0000269|PubMed:12150929,
FT ECO:0000269|PubMed:17302430, ECO:0000269|PubMed:19277500,
FT ECO:0000269|PubMed:22169508, ECO:0000269|PubMed:24388849"
FT MUTAGEN 363
FT /note="Y->G,A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:22547027"
FT MUTAGEN 416
FT /note="D->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:22547027"
FT MUTAGEN 421
FT /note="N->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:22547027"
FT MUTAGEN 439
FT /note="K->A: No effect on some phosphorylation sites."
FT /evidence="ECO:0000269|PubMed:22547027"
FT MUTAGEN 446
FT /note="T->A,D: No effect. Reduced interaction with BIR2.
FT Loss of kinase activity; when associated with D-449 and D-
FT 450."
FT /evidence="ECO:0000269|PubMed:19277500,
FT ECO:0000269|PubMed:24388849"
FT MUTAGEN 449
FT /note="T->A,D: Slight decrease of kinase activity but loss
FT of interaction with hopAB2/AvrPtoB. Reduced interaction
FT with BIR2. Loss of kinase activity; when associated with A-
FT 446 and D-450."
FT /evidence="ECO:0000269|PubMed:19277500,
FT ECO:0000269|PubMed:22169508, ECO:0000269|PubMed:24388849"
FT MUTAGEN 450
FT /note="T->A,D: Loss of interaction with hopAB2/AvrPtoB and
FT loss of phosphorylation. Reduced interaction with BIR2.
FT Loss of kinase activity; when associated with A-446 and D-
FT 449."
FT /evidence="ECO:0000269|PubMed:19277500,
FT ECO:0000269|PubMed:22169508, ECO:0000269|PubMed:22547027,
FT ECO:0000269|PubMed:24388849"
FT MUTAGEN 451
FT /note="A->E: Loss of kinase activity and loss of
FT interaction with hopAB2/AvrPtoB. Reduced interaction with
FT BIR2."
FT /evidence="ECO:0000269|PubMed:22169508,
FT ECO:0000269|PubMed:24388849"
FT MUTAGEN 452
FT /note="V->D: Strongly decreased kinase activity and loss of
FT interaction with hopAB2/AvrPtoB."
FT /evidence="ECO:0000269|PubMed:22169508"
FT MUTAGEN 453
FT /note="R->A: No effect on some phosphorylation sites."
FT /evidence="ECO:0000269|PubMed:22547027"
FT MUTAGEN 455
FT /note="T->A,D,E: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:18694562,
FT ECO:0000269|PubMed:19277500"
FT MUTAGEN 455
FT /note="T->N: Loss of kinase activity and loss of
FT interaction with hopAB2/AvrPtoB."
FT /evidence="ECO:0000269|PubMed:22169508"
FT MUTAGEN 456
FT /note="I->D: Loss of kinase activity and loss of
FT interaction with hopAB2/AvrPtoB."
FT /evidence="ECO:0000269|PubMed:22169508"
FT MUTAGEN 458
FT /note="H->D: Loss of kinase activity, loss of
FT phosphorylation and loss of interaction with
FT hopAB2/AvrPtoB."
FT /evidence="ECO:0000269|PubMed:22169508,
FT ECO:0000269|PubMed:22547027"
FT MUTAGEN 464
FT /note="L->D: Loss of kinase activity and loss of
FT interaction with hopAB2/AvrPtoB."
FT /evidence="ECO:0000269|PubMed:22169508"
FT MUTAGEN 495
FT /note="A->E: Loss of kinase activity and loss of
FT interaction with hopAB2/AvrPtoB."
FT /evidence="ECO:0000269|PubMed:22169508"
FT MUTAGEN 546
FT /note="T->A: 60% decrease of binding to the FHA domain of
FT KAPP."
FT /evidence="ECO:0000269|PubMed:17302430"
FT CONFLICT 12
FT /note="W -> G (in Ref. 1; AAK68074)"
FT /evidence="ECO:0000305"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:4MN8"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:4MN8"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:4MN8"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:3UIM"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:3UIM"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:3TL8"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:3UIM"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:3UIM"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:3UIM"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:3UIM"
FT HELIX 330..336
FT /evidence="ECO:0007829|PDB:3UIM"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:3UIM"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:3UIM"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:3UIM"
FT HELIX 371..376
FT /evidence="ECO:0007829|PDB:3UIM"
FT HELIX 387..406
FT /evidence="ECO:0007829|PDB:3UIM"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:3UIM"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:3UIM"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:3UIM"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:3TL8"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:3UIM"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:3UIM"
FT HELIX 461..466
FT /evidence="ECO:0007829|PDB:3UIM"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:3UIM"
FT HELIX 471..487
FT /evidence="ECO:0007829|PDB:3UIM"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:3UIM"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:3UIM"
FT HELIX 505..509
FT /evidence="ECO:0007829|PDB:3UIM"
FT TURN 510..513
FT /evidence="ECO:0007829|PDB:3UIM"
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:3TL8"
FT HELIX 524..526
FT /evidence="ECO:0007829|PDB:3TL8"
FT STRAND 527..530
FT /evidence="ECO:0007829|PDB:3ULZ"
FT HELIX 532..545
FT /evidence="ECO:0007829|PDB:3UIM"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:3UIM"
FT HELIX 556..564
FT /evidence="ECO:0007829|PDB:3UIM"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:3UIM"
FT HELIX 577..581
FT /evidence="ECO:0007829|PDB:3TL8"
SQ SEQUENCE 615 AA; 68161 MW; 547B3F38FB46E1DD CRC64;
MERRLMIPCF FWLILVLDLV LRVSGNAEGD ALSALKNSLA DPNKVLQSWD ATLVTPCTWF
HVTCNSDNSV TRVDLGNANL SGQLVMQLGQ LPNLQYLELY SNNITGTIPE QLGNLTELVS
LDLYLNNLSG PIPSTLGRLK KLRFLRLNNN SLSGEIPRSL TAVLTLQVLD LSNNPLTGDI
PVNGSFSLFT PISFANTKLT PLPASPPPPI SPTPPSPAGS NRITGAIAGG VAAGAALLFA
VPAIALAWWR RKKPQDHFFD VPAEEDPEVH LGQLKRFSLR ELQVASDNFS NKNILGRGGF
GKVYKGRLAD GTLVAVKRLK EERTQGGELQ FQTEVEMISM AVHRNLLRLR GFCMTPTERL
LVYPYMANGS VASCLRERPE SQPPLDWPKR QRIALGSARG LAYLHDHCDP KIIHRDVKAA
NILLDEEFEA VVGDFGLAKL MDYKDTHVTT AVRGTIGHIA PEYLSTGKSS EKTDVFGYGV
MLLELITGQR AFDLARLAND DDVMLLDWVK GLLKEKKLEA LVDVDLQGNY KDEEVEQLIQ
VALLCTQSSP MERPKMSEVV RMLEGDGLAE RWEEWQKEEM FRQDFNYPTH HPAVSGWIIG
DSTSQIENEY PSGPR
