MPK4_ARATH
ID MPK4_ARATH Reviewed; 376 AA.
AC Q39024; B2BDE5; B2BDE6; B2BDE8; B2BDG2; O04597; Q45V20; Q9M136;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Mitogen-activated protein kinase 4 {ECO:0000303|PubMed:8282107};
DE Short=AtMPK4 {ECO:0000303|PubMed:8282107};
DE Short=MAP kinase 4 {ECO:0000303|PubMed:8282107};
DE EC=2.7.11.24 {ECO:0000269|PubMed:10036776, ECO:0000269|PubMed:10759527};
GN Name=MPK4 {ECO:0000303|PubMed:8282107};
GN OrderedLocusNames=At4g01370 {ECO:0000312|Araport:AT4G01370};
GN ORFNames=F2N1.1, F2N1_2-t;
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. Columbia;
RX PubMed=8282107; DOI=10.1016/0014-5793(93)80852-l;
RA Mizoguchi T., Hayashida N., Yamaguchi-Shinozaki K., Kamada H.,
RA Shinozaki K.;
RT "ATMPKs: a gene family of plant MAP kinases in Arabidopsis thaliana.";
RL FEBS Lett. 336:440-444(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-115 AND VAL-293.
RC STRAIN=cv. Aa-0, cv. Ak-1, cv. Bay-0, cv. C24, cv. Columbia, cv. Cvi-0,
RC cv. Di-0, cv. Ei-2, cv. Gu-0, cv. HOG, cv. Landsberg erecta, cv. Lz-0,
RC cv. N13 Konchezero, cv. Nd-1, cv. Sha, cv. Sorbo, cv. Tsu-0,
RC cv. Wassilewskija, cv. Wei-0, and cv. Yo-0;
RX PubMed=19064707; DOI=10.1534/genetics.108.097279;
RA Caldwell K.S., Michelmore R.W.;
RT "Arabidopsis thaliana genes encoding defense signaling and recognition
RT proteins exhibit contrasting evolutionary dynamics.";
RL Genetics 181:671-684(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sharma P.K., Kumar R., Garg G.K., Khan G.;
RT "MAP kinase 4 genomic sequence from Arabidopsis thaliana.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP SUBUNIT, AND INTERACTION WITH MEKK1; MKK1 AND MKK2.
RX PubMed=9878570; DOI=10.1006/bbrc.1998.9796;
RA Ichimura K., Mizoguchi T., Irie K., Morris P.C., Giraudat J., Matsumoto K.,
RA Shinozaki K.;
RT "Isolation of ATMEKK1 (a MAP kinase kinase kinase)-interacting proteins and
RT analysis of a MAP kinase cascade in Arabidopsis.";
RL Biochem. Biophys. Res. Commun. 253:532-543(1998).
RN [9]
RP ACTIVITY REGULATION, DEPHOSPHORYLATION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=10036776; DOI=10.1046/j.1365-313x.1998.00327.x;
RA Gupta R., Huang Y., Kieber J., Luan S.;
RT "Identification of a dual-specificity protein phosphatase that inactivates
RT a MAP kinase from Arabidopsis.";
RL Plant J. 16:581-589(1998).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF THR-201 AND TYR-203.
RX PubMed=11163186; DOI=10.1016/s0092-8674(00)00213-0;
RA Petersen M., Brodersen P., Naested H., Andreasson E., Lindhart U.,
RA Johansen B., Nielsen H.B., Lacy M., Austin M.J., Parker J.E., Sharma S.B.,
RA Klessig D.F., Martienssen R., Mattsson O., Jensen A.B., Mundy J.;
RT "Arabidopsis MAP kinase 4 negatively regulates systemic acquired
RT resistance.";
RL Cell 103:1111-1120(2000).
RN [11]
RP ACTIVITY REGULATION, AND PHOSPHORYLATION AT THR-201 AND TYR-203.
RX PubMed=11123804; DOI=10.1046/j.1365-313x.2000.00913.x;
RA Ichimura K., Mizoguchi T., Yoshida R., Yuasa T., Shinozaki K.;
RT "Various abiotic stresses rapidly activate Arabidopsis MAP kinases ATMPK4
RT and ATMPK6.";
RL Plant J. 24:655-665(2000).
RN [12]
RP ACTIVITY REGULATION, PHOSPHORYLATION, MUTAGENESIS OF ASP-187, AND CATALYTIC
RP ACTIVITY.
RX PubMed=10759527; DOI=10.1104/pp.122.4.1301;
RA Huang Y., Li H., Gupta R., Morris P.C., Luan S., Kieber J.J.;
RT "ATMPK4, an Arabidopsis homolog of mitogen-activated protein kinase, is
RT activated in vitro by AtMEK1 through threonine phosphorylation.";
RL Plant Physiol. 122:1301-1310(2000).
RN [13]
RP ACTIVITY REGULATION.
RX PubMed=11500556; DOI=10.1104/pp.126.4.1579;
RA Desikan R., Hancock J.T., Ichimura K., Shinozaki K., Neill S.J.;
RT "Harpin induces activation of the Arabidopsis mitogen-activated protein
RT kinases AtMPK4 and AtMPK6.";
RL Plant Physiol. 126:1579-1587(2001).
RN [14]
RP ACTIVITY REGULATION.
RX PubMed=11874576; DOI=10.1046/j.0960-7412.2001.01246.x;
RA Matsuoka D., Nanmori T., Sato K., Fukami Y., Kikkawa U., Yasuda T.;
RT "Activation of AtMEK1, an Arabidopsis mitogen-activated protein kinase
RT kinase, in vitro and in vivo: analysis of active mutants expressed in E.
RT coli and generation of the active form in stress response in seedlings.";
RL Plant J. 29:637-647(2002).
RN [15]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12119167; DOI=10.1016/s1360-1385(02)02302-6;
RG MAPK group;
RT "Mitogen-activated protein kinase cascades in plants: a new nomenclature.";
RL Trends Plant Sci. 7:301-308(2002).
RN [16]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=15358537; DOI=10.1016/j.febslet.2004.08.001;
RA Droillard M.-J., Boudsocq M., Barbier-Brygoo H., Lauriere C.;
RT "Involvement of MPK4 in osmotic stress response pathways in cell
RT suspensions and plantlets of Arabidopsis thaliana: activation by
RT hypoosmolarity and negative role in hyperosmolarity tolerance.";
RL FEBS Lett. 574:42-48(2004).
RN [17]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH MKK2.
RX PubMed=15225555; DOI=10.1016/j.molcel.2004.06.023;
RA Teige M., Scheikl E., Eulgem T., Doczi R., Ichimura K., Shinozaki K.,
RA Dangl J.L., Hirt H.;
RT "The MKK2 pathway mediates cold and salt stress signaling in Arabidopsis.";
RL Mol. Cell 15:141-152(2004).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MKS1.
RX PubMed=15990873; DOI=10.1038/sj.emboj.7600737;
RA Andreasson E., Jenkins T., Brodersen P., Thorgrimsen S., Petersen N.H.T.,
RA Zhu S., Qiu J.-L., Micheelsen P., Rocher A., Petersen M., Newman M.-A.,
RA Bjoern Nielsen H., Hirt H., Somssich I.E., Mattsson O., Mundy J.;
RT "The MAP kinase substrate MKS1 is a regulator of plant defense responses.";
RL EMBO J. 24:2579-2589(2005).
RN [19]
RP GENE FAMILY.
RX PubMed=16537113; DOI=10.1016/j.tplants.2006.02.007;
RA Hamel L.P., Nicole M.C., Sritubtim S., Morency M.J., Ellis M., Ehlting J.,
RA Beaudoin N., Barbazuk B., Klessig D., Lee J., Martin G., Mundy J.,
RA Ohashi Y., Scheel D., Sheen J., Xing T., Zhang S., Seguin A., Ellis B.E.;
RT "Ancient signals: comparative genomics of plant MAPK and MAPKK gene
RT families.";
RL Trends Plant Sci. 11:192-198(2006).
RN [20]
RP ACTIVITY REGULATION.
RX PubMed=17506336; DOI=10.1094/mpmi-20-5-0589;
RA Brader G., Djamei A., Teige M., Palva E.T., Hirt H.;
RT "The MAP kinase kinase MKK2 affects disease resistance in Arabidopsis.";
RL Mol. Plant Microbe Interact. 20:589-596(2007).
RN [21]
RP ACTIVITY REGULATION, AND INTERACTION WITH AP2C1.
RX PubMed=17630279; DOI=10.1105/tpc.106.049585;
RA Schweighofer A., Kazanaviciute V., Scheikl E., Teige M., Doczi R., Hirt H.,
RA Schwanninger M., Kant M., Schuurink R., Mauch F., Buchala A., Cardinale F.,
RA Meskiene I.;
RT "The PP2C-type phosphatase AP2C1, which negatively regulates MPK4 and MPK6,
RT modulates innate immunity, jasmonic acid, and ethylene levels in
RT Arabidopsis.";
RL Plant Cell 19:2213-2224(2007).
RN [22]
RP FUNCTION, INTERACTION WITH MEKK1; MKK1 AND MKK2, AND DISRUPTION PHENOTYPE.
RX PubMed=18982020; DOI=10.1038/cr.2008.300;
RA Gao M., Liu J., Bi D., Zhang Z., Cheng F., Chen S., Zhang Y.;
RT "MEKK1, MKK1/MKK2 and MPK4 function together in a mitogen-activated protein
RT kinase cascade to regulate innate immunity in plants.";
RL Cell Res. 18:1190-1198(2008).
RN [23]
RP INTERACTION WITH MKK1; MKK2 AND MKK6.
RX PubMed=19513235; DOI=10.4161/psb.3.12.6848;
RA Lee J.S., Huh K.W., Bhargava A., Ellis B.E.;
RT "Comprehensive analysis of protein-protein interactions between Arabidopsis
RT MAPKs and MAPK kinases helps define potential MAPK signalling modules.";
RL Plant Signal. Behav. 3:1037-1041(2008).
RN [24]
RP FUNCTION, INTERACTION WITH MAP65-1, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20215588; DOI=10.1105/tpc.109.071746;
RA Beck M., Komis G., Mueller J., Menzel D., Samaj J.;
RT "Arabidopsis homologs of nucleus- and phragmoplast-localized kinase 2 and 3
RT and mitogen-activated protein kinase 4 are essential for microtubule
RT organization.";
RL Plant Cell 22:755-771(2010).
RN [25]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND ACTIVITY
RP REGULATION.
RX PubMed=21098735; DOI=10.1105/tpc.110.077164;
RA Kosetsu K., Matsunaga S., Nakagami H., Colcombet J., Sasabe M., Soyano T.,
RA Takahashi Y., Hirt H., Machida Y.;
RT "The MAP kinase MPK4 is required for cytokinesis in Arabidopsis thaliana.";
RL Plant Cell 22:3778-3790(2010).
RN [26]
RP FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION BY MKK6, AND INTERACTION
RP WITH MKK6.
RX PubMed=20802223; DOI=10.1093/pcp/pcq135;
RA Takahashi Y., Soyano T., Kosetsu K., Sasabe M., Machida Y.;
RT "HINKEL kinesin, ANP MAPKKKs and MKK6/ANQ MAPKK, which phosphorylates and
RT activates MPK4 MAPK, constitute a pathway that is required for cytokinesis
RT in Arabidopsis thaliana.";
RL Plant Cell Physiol. 51:1766-1776(2010).
RN [27]
RP FUNCTION, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, INTERACTION WITH MKK1
RP AND MKK6, AND TISSUE SPECIFICITY.
RX PubMed=21575092; DOI=10.1111/j.1365-313x.2011.04642.x;
RA Zeng Q., Chen J.G., Ellis B.E.;
RT "AtMPK4 is required for male-specific meiotic cytokinesis in Arabidopsis.";
RL Plant J. 67:895-906(2011).
RN [28]
RP FUNCTION, AND INTERACTION WITH MEKK2.
RX PubMed=22643122; DOI=10.1105/tpc.112.097253;
RA Kong Q., Qu N., Gao M., Zhang Z., Ding X., Yang F., Li Y., Dong O.X.,
RA Chen S., Li X., Zhang Y.;
RT "The MEKK1-MKK1/MKK2-MPK4 kinase cascade negatively regulates immunity
RT mediated by a mitogen-activated protein kinase kinase kinase in
RT Arabidopsis.";
RL Plant Cell 24:2225-2236(2012).
RN [29]
RP INTERACTION WITH PAT1.
RX PubMed=25603932; DOI=10.15252/embj.201488645;
RA Roux M.E., Rasmussen M.W., Palma K., Lolle S., Regue A.M., Bethke G.,
RA Glazebrook J., Zhang W., Sieburth L., Larsen M.R., Mundy J., Petersen M.;
RT "The mRNA decay factor PAT1 functions in a pathway including MAP kinase 4
RT and immune receptor SUMM2.";
RL EMBO J. 34:593-608(2015).
RN [30]
RP LACK OF INTERACTION WITH RACK1A; RACK1B OR RACK1C.
RX PubMed=25731164; DOI=10.1038/nature14243;
RA Cheng Z., Li J.F., Niu Y., Zhang X.C., Woody O.Z., Xiong Y., Djonovic S.,
RA Millet Y., Bush J., McConkey B.J., Sheen J., Ausubel F.M.;
RT "Pathogen-secreted proteases activate a novel plant immune pathway.";
RL Nature 521:213-216(2015).
RN [31]
RP FUNCTION, AND INTERACTION WITH ASR3.
RC STRAIN=cv. Columbia;
RX PubMed=25770109; DOI=10.1105/tpc.114.134809;
RA Li B., Jiang S., Yu X., Cheng C., Chen S., Cheng Y., Yuan J.S., Jiang D.,
RA He P., Shan L.;
RT "Phosphorylation of trihelix transcriptional repressor ASR3 by MAP KINASE4
RT negatively regulates Arabidopsis immunity.";
RL Plant Cell 27:839-856(2015).
RN [32]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH HT1.
RC STRAIN=cv. Columbia;
RX PubMed=27694184; DOI=10.1105/tpc.16.00131;
RA Horak H., Sierla M., Toldsepp K., Wang C., Wang Y.-S., Nuhkat M., Valk E.,
RA Pechter P., Merilo E., Salojaervi J., Overmyer K., Loog M., Brosche M.,
RA Schroeder J.I., Kangasjaervi J., Kollist H.;
RT "A dominant mutation in the HT1 kinase uncovers roles of MAP kinases and
RT GHR1 in CO2-induced stomatal closure.";
RL Plant Cell 28:2493-2509(2016).
RN [33]
RP FUNCTION, AND MUTAGENESIS OF GLY-55.
RC STRAIN=cv. Columbia, and cv. Cvi-0;
RX PubMed=27923039; DOI=10.1371/journal.pbio.2000322;
RA Jakobson L., Vaahtera L., Toldsepp K., Nuhkat M., Wang C., Wang Y.S.,
RA Horak H., Valk E., Pechter P., Sindarovska Y., Tang J., Xiao C., Xu Y.,
RA Gerst Talas U., Garcia-Sosa A.T., Kangasjaervi S., Maran U., Remm M.,
RA Roelfsema M.R., Hu H., Kangasjaervi J., Loog M., Schroeder J.I.,
RA Kollist H., Brosche M.;
RT "Natural variation in Arabidopsis Cvi-0 accession reveals an important role
RT of MPK12 in guard cell CO2 signaling.";
RL PLoS Biol. 14:E2000322-E2000322(2016).
CC -!- FUNCTION: The ANPs-MKK6-MPK4 module is involved in the regulation of
CC plant cytokinesis during meiosis and mitosis. Essential to promote the
CC progression of cytokinesis and for cellularization (formation of the
CC cell plate) during male-specific meiosis. Involved in cortical
CC microtubules organization and stabilization by regulating the
CC phosphorylation state of microtubule-associated proteins such as MAP65-
CC 1. Involved in root hair development process. Negative regulator of
CC systemic acquired resistance (SAR) and salicylic acid- (SA) mediated
CC defense response. Required for jasmonic acid- (JA) mediated defense
CC gene expression. May regulate activity of transcription factor
CC controlling pathogenesis-related (PR) gene expression. Seems to act
CC independently of the SAR regulatory protein NPR1 (Nonexpresser of PR1).
CC Phosphorylates MKS1 and transcription factors WRKY25 and WRKY33. The
CC MEKK1, MKK1/MKK2 and MPK4 function in a signaling pathway that
CC modulates the expression of genes responding to biotic and abiotic
CC stresses and also plays an important role in pathogen defense by
CC negatively regulating innate immunity (PubMed:11163186,
CC PubMed:15225555, PubMed:15358537, PubMed:15990873, PubMed:18982020,
CC PubMed:20215588, PubMed:20802223, PubMed:21098735, PubMed:21575092,
CC PubMed:25770109). Phosphorylates MEKK2 upon treatment with flg22
CC (PubMed:22643122). Involved in stomatal movement regulation by
CC repressing HT1 and HT1-mediated GHR1 phosphorylation (PubMed:27694184,
CC PubMed:27923039). {ECO:0000269|PubMed:11163186,
CC ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:15358537,
CC ECO:0000269|PubMed:15990873, ECO:0000269|PubMed:18982020,
CC ECO:0000269|PubMed:20215588, ECO:0000269|PubMed:20802223,
CC ECO:0000269|PubMed:21098735, ECO:0000269|PubMed:21575092,
CC ECO:0000269|PubMed:22643122, ECO:0000269|PubMed:25770109,
CC ECO:0000269|PubMed:27694184, ECO:0000269|PubMed:27923039}.
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=2.7.11.24;
CC Evidence={ECO:0000269|PubMed:10036776, ECO:0000269|PubMed:10759527};
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=2.7.11.24; Evidence={ECO:0000269|PubMed:10036776,
CC ECO:0000269|PubMed:10759527};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation. Activated by the MAP kinase kinases MKK1 and MKK2.
CC Activated in response to touch, wounding, low temperature, low
CC humidity, salt stress and the bacterial elicitors flagellin and harpin.
CC Activated upon Pseudomonas syringae pv. tomato DC3000 infection.
CC Repressed by the protein phosphatase 2C AP2C1. Repressed by DSPTP1-
CC mediated dephosphorylation. Activated by the MAP kinase kinase MKK6 in
CC vitro. {ECO:0000269|PubMed:10036776, ECO:0000269|PubMed:10759527,
CC ECO:0000269|PubMed:11123804, ECO:0000269|PubMed:11500556,
CC ECO:0000269|PubMed:11874576, ECO:0000269|PubMed:15225555,
CC ECO:0000269|PubMed:15358537, ECO:0000269|PubMed:17506336,
CC ECO:0000269|PubMed:17630279, ECO:0000269|PubMed:20802223,
CC ECO:0000269|PubMed:21098735, ECO:0000269|PubMed:21575092}.
CC -!- SUBUNIT: Interacts with MEKK1, MKK1, MKK2 and MKK6. May form a ternary
CC complex composed of MEKK1 and MKK1/MKK2 and MPK4. Interacts with MKS1
CC and AP2C1. May form a ternary or larger complex with MKS1 and WRKY25
CC and/or WRKY33. Interacts with MAP65-1 (PubMed:15225555,
CC PubMed:15990873, PubMed:17630279, PubMed:18982020, PubMed:19513235,
CC PubMed:20215588, PubMed:20802223, PubMed:21575092, PubMed:9878570). No
CC interactions with RACK1A, RACK1B or RACK1C (PubMed:25731164). Interacts
CC directly with ASR3 and mediates its phosphorylation (PubMed:25770109).
CC Binds to MEKK2 (PubMed:22643122). Interacts with PAT1
CC (PubMed:25603932). Binds to HT1 (PubMed:27694184).
CC {ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:15990873,
CC ECO:0000269|PubMed:17630279, ECO:0000269|PubMed:18982020,
CC ECO:0000269|PubMed:19513235, ECO:0000269|PubMed:20215588,
CC ECO:0000269|PubMed:20802223, ECO:0000269|PubMed:21575092,
CC ECO:0000269|PubMed:22643122, ECO:0000269|PubMed:25603932,
CC ECO:0000269|PubMed:25731164, ECO:0000269|PubMed:25770109,
CC ECO:0000269|PubMed:27694184, ECO:0000269|PubMed:9878570}.
CC -!- INTERACTION:
CC Q39024; O80871: At2g30020; NbExp=3; IntAct=EBI-994375, EBI-16897073;
CC Q39024; Q84JD1: At5g07260; NbExp=3; IntAct=EBI-994375, EBI-25510874;
CC Q39024; A0A178UJ48: AXX17_At5g14090; NbExp=3; IntAct=EBI-994375, EBI-25518229;
CC Q39024; O81472: MEKK2; NbExp=3; IntAct=EBI-994375, EBI-6271434;
CC Q39024; Q94A06: MKK1; NbExp=11; IntAct=EBI-994375, EBI-994464;
CC Q39024; Q9S7U9: MKK2; NbExp=10; IntAct=EBI-994375, EBI-994350;
CC Q39024; Q9FJV0: MKK6; NbExp=4; IntAct=EBI-994375, EBI-1238868;
CC Q39024; Q8LGD5: MKS1; NbExp=9; IntAct=EBI-994375, EBI-1392198;
CC Q39024; O22921: WRKY25; NbExp=2; IntAct=EBI-994375, EBI-1392386;
CC Q39024; Q8S8P5: WRKY33; NbExp=2; IntAct=EBI-994375, EBI-1392374;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton.
CC Note=Translocated into the nucleus in response to phosphorylation
CC (Probable). Localized to the cell plate. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in the veins and stomatal
CC guard cells of leaf plates, petioles, stem, roots and flowers.
CC {ECO:0000269|PubMed:11163186, ECO:0000269|PubMed:20215588,
CC ECO:0000269|PubMed:21575092}.
CC -!- DEVELOPMENTAL STAGE: Observed in root epidermal cells and root hairs,
CC especially in the root hair formation zone. During root hair
CC development, both observed in root hair bulges and in young outgrowing
CC root hairs. {ECO:0000269|PubMed:20215588}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-201 and Tyr-203, which activates the
CC enzyme. Autophosphorylated on serine and tyrosine residues.
CC Dephosphorylated by DSPTP1. Phosphorylated by MKK6 in vitro.
CC {ECO:0000269|PubMed:10759527, ECO:0000269|PubMed:11123804,
CC ECO:0000269|PubMed:20802223}.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants with cytokinetic defects in leaf
CC epidermal cells. Abnormally developed and branched root hairs. Retarded
CC root growth with the protrusion of many epidermal cells from roots.
CC Heavily bundled and disoriented cortical microtubules resistant to
CC oryzalin. Exhibits a seedling-lethality phenotype. Defects in the
CC formation of the cell plate. Abnormal mature pollen grains. Abolished
CC CO(2)-mediated stomatal closure (PubMed:27694184).
CC {ECO:0000269|PubMed:18982020, ECO:0000269|PubMed:20215588,
CC ECO:0000269|PubMed:21098735, ECO:0000269|PubMed:21575092,
CC ECO:0000269|PubMed:27694184}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61033.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D21840; BAA04867.1; -; mRNA.
DR EMBL; EF470667; ABR46145.1; -; Genomic_DNA.
DR EMBL; EF470668; ABR46146.1; -; Genomic_DNA.
DR EMBL; EF470669; ABR46147.1; -; Genomic_DNA.
DR EMBL; EF470670; ABR46148.1; -; Genomic_DNA.
DR EMBL; EF470671; ABR46149.1; -; Genomic_DNA.
DR EMBL; EF470672; ABR46150.1; -; Genomic_DNA.
DR EMBL; EF470673; ABR46151.1; -; Genomic_DNA.
DR EMBL; EF470674; ABR46152.1; -; Genomic_DNA.
DR EMBL; EF470675; ABR46153.1; -; Genomic_DNA.
DR EMBL; EF470676; ABR46154.1; -; Genomic_DNA.
DR EMBL; EF470677; ABR46155.1; -; Genomic_DNA.
DR EMBL; EF470678; ABR46156.1; -; Genomic_DNA.
DR EMBL; EF470679; ABR46157.1; -; Genomic_DNA.
DR EMBL; EF470680; ABR46158.1; -; Genomic_DNA.
DR EMBL; EF470681; ABR46159.1; -; Genomic_DNA.
DR EMBL; EF470682; ABR46160.1; -; Genomic_DNA.
DR EMBL; EF470683; ABR46161.1; -; Genomic_DNA.
DR EMBL; EF470684; ABR46162.1; -; Genomic_DNA.
DR EMBL; EF470685; ABR46163.1; -; Genomic_DNA.
DR EMBL; EF470686; ABR46164.1; -; Genomic_DNA.
DR EMBL; DQ112072; AAZ20637.1; -; Genomic_DNA.
DR EMBL; AF007269; AAB61033.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161491; CAB80946.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82016.1; -; Genomic_DNA.
DR EMBL; AF360231; AAK25941.1; -; mRNA.
DR EMBL; AY040031; AAK64089.1; -; mRNA.
DR EMBL; AY088537; AAM66070.1; -; mRNA.
DR PIR; S40470; S40470.
DR RefSeq; NP_192046.1; NM_116367.3.
DR AlphaFoldDB; Q39024; -.
DR SMR; Q39024; -.
DR BioGRID; 13440; 168.
DR IntAct; Q39024; 11.
DR MINT; Q39024; -.
DR STRING; 3702.AT4G01370.1; -.
DR iPTMnet; Q39024; -.
DR PaxDb; Q39024; -.
DR PRIDE; Q39024; -.
DR ProteomicsDB; 250946; -.
DR EnsemblPlants; AT4G01370.1; AT4G01370.1; AT4G01370.
DR GeneID; 828151; -.
DR Gramene; AT4G01370.1; AT4G01370.1; AT4G01370.
DR KEGG; ath:AT4G01370; -.
DR Araport; AT4G01370; -.
DR TAIR; locus:2124943; AT4G01370.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q39024; -.
DR OMA; HSCMCRC; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; Q39024; -.
DR BRENDA; 2.7.11.24; 399.
DR PRO; PR:Q39024; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q39024; baseline and differential.
DR Genevisible; Q39024; AT.
DR GO; GO:0009504; C:cell plate; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
DR GO; GO:0004707; F:MAP kinase activity; IDA:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IMP:UniProtKB.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:UniProtKB.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:UniProtKB.
DR GO; GO:0006972; P:hyperosmotic response; IMP:TAIR.
DR GO; GO:0042539; P:hypotonic salinity response; IDA:TAIR.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0009861; P:jasmonic acid and ethylene-dependent systemic resistance; IMP:TAIR.
DR GO; GO:0009868; P:jasmonic acid and ethylene-dependent systemic resistance, jasmonic acid mediated signaling pathway; TAS:TAIR.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IDA:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IDA:TAIR.
DR GO; GO:0009620; P:response to fungus; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IDA:TAIR.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 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 ATP-binding; Cytoplasm; Cytoskeleton; Immunity; Innate immunity; Kinase;
KW Microtubule; Nucleotide-binding; Nucleus; Phosphoprotein; Plant defense;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transferase.
FT CHAIN 1..376
FT /note="Mitogen-activated protein kinase 4"
FT /id="PRO_0000186313"
FT DOMAIN 43..329
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 201..203
FT /note="TXY"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 49..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11123804"
FT MOD_RES 203
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11123804"
FT VARIANT 115
FT /note="E -> Q (in strain: cv. C24, cv. Lz-0, cv. Wei-0, cv.
FT Yo-0)"
FT /evidence="ECO:0000269|PubMed:19064707"
FT VARIANT 293
FT /note="A -> V (in strain: cv. Ak-1, cv. Bay-0, cv. Di-0,
FT cv. Landsberg erecta, cv. Tsu-0, cv. Wei-0)"
FT /evidence="ECO:0000269|PubMed:19064707"
FT MUTAGEN 55
FT /note="G->R: Altered inhibition of HT1 activity."
FT /evidence="ECO:0000269|PubMed:27923039"
FT MUTAGEN 187
FT /note="D->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:10759527"
FT MUTAGEN 201
FT /note="T->A: Loss of kinase activity; when associated with
FT Y-203."
FT /evidence="ECO:0000269|PubMed:11163186"
FT MUTAGEN 203
FT /note="Y->F: Loss of kinase activity; when associated with
FT T-201."
FT /evidence="ECO:0000269|PubMed:11163186"
FT CONFLICT 313
FT /note="D -> E (in Ref. 1; BAA04867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 42852 MW; 448F65C25C95AAEB CRC64;
MSAESCFGSS GDQSSSKGVA THGGSYVQYN VYGNLFEVSR KYVPPLRPIG RGAYGIVCAA
TNSETGEEVA IKKIGNAFDN IIDAKRTLRE IKLLKHMDHE NVIAVKDIIK PPQRENFNDV
YIVYELMDTD LHQIIRSNQP LTDDHCRFFL YQLLRGLKYV HSANVLHRDL KPSNLLLNAN
CDLKLGDFGL ARTKSETDFM TEYVVTRWYR APELLLNCSE YTAAIDIWSV GCILGETMTR
EPLFPGKDYV HQLRLITELI GSPDDSSLGF LRSDNARRYV RQLPQYPRQN FAARFPNMSA
GAVDLLEKML VFDPSRRITV DEALCHPYLA PLHDINEEPV CVRPFNFDFE QPTLTEENIK
ELIYRETVKF NPQDSV
