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 24-JAN-2024, entry version 202. 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. RC Cvi-0, cv. Di-0, cv. Ei-2, cv. Gu-0, cv. HOG, cv. Landsberg erecta, RC cv. Lz-0, 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 PDB; 7W5C; X-ray; 2.20 A; A=18-372. DR PDBsum; 7W5C; -. DR AlphaFoldDB; Q39024; -. DR SMR; Q39024; -. DR BioGRID; 13440; 168. DR IntAct; Q39024; 11. DR MINT; Q39024; -. DR STRING; 3702.Q39024; -. DR iPTMnet; Q39024; -. DR PaxDb; 3702-AT4G01370-1; -. 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; AT4G01370; MPK4. DR eggNOG; KOG0660; Eukaryota. DR HOGENOM; CLU_000288_181_1_1; -. DR InParanoid; Q39024; -. DR OMA; QNMTHEV; -. DR OrthoDB; 5474493at2759; -. 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 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: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: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 CDD; cd07858; STKc_TEY_MAPK; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF439; MITOGEN-ACTIVATED PROTEIN KINASE 11-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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. DR Genevisible; Q39024; AT. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Cytoskeleton; Immunity; KW Innate immunity; Kinase; Microtubule; Nucleotide-binding; Nucleus; KW Phosphoprotein; Plant defense; Reference proteome; KW Serine/threonine-protein kinase; Stress response; 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" FT STRAND 19..21 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 22..24 FT /evidence="ECO:0007829|PDB:7W5C" FT STRAND 26..31 FT /evidence="ECO:0007829|PDB:7W5C" FT STRAND 34..39 FT /evidence="ECO:0007829|PDB:7W5C" FT STRAND 42..51 FT /evidence="ECO:0007829|PDB:7W5C" FT STRAND 53..62 FT /evidence="ECO:0007829|PDB:7W5C" FT TURN 63..66 FT /evidence="ECO:0007829|PDB:7W5C" FT STRAND 67..74 FT /evidence="ECO:0007829|PDB:7W5C" FT TURN 75..78 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 81..96 FT /evidence="ECO:0007829|PDB:7W5C" FT STRAND 105..108 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:7W5C" FT STRAND 120..125 FT /evidence="ECO:0007829|PDB:7W5C" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 131..136 FT /evidence="ECO:0007829|PDB:7W5C" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 143..162 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:7W5C" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:7W5C" FT STRAND 183..185 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 212..215 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 224..239 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 249..260 FT /evidence="ECO:0007829|PDB:7W5C" FT TURN 265..270 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 274..282 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 291..294 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 300..309 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 314..316 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 320..324 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:7W5C" FT TURN 330..332 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:7W5C" FT HELIX 356..370 FT /evidence="ECO:0007829|PDB:7W5C" 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 //