MPK3_ARATH
ID MPK3_ARATH Reviewed; 370 AA.
AC Q39023; Q9M1E3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Mitogen-activated protein kinase 3 {ECO:0000303|PubMed:8282107};
DE Short=AtMPK3 {ECO:0000303|PubMed:8282107};
DE Short=MAP kinase 3 {ECO:0000303|PubMed:8282107};
DE EC=2.7.11.24 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12220631, ECO:0000269|PubMed:15500467};
GN Name=MPK3 {ECO:0000303|PubMed:8282107};
GN OrderedLocusNames=At3g45640 {ECO:0000312|Araport:AT3G45640};
GN ORFNames=F9K21.220 {ECO:0000312|EMBL:CAB75493.1},
GN T6D9.4 {ECO:0000312|EMBL:AL157735};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [5]
RP INDUCTION.
RX PubMed=8570631; DOI=10.1073/pnas.93.2.765;
RA Mizoguchi T., Irie K., Hirayama T., Hayashida N., Yamaguchi-Shinozaki K.,
RA Matsumoto K., Shinozaki K.;
RT "A gene encoding a mitogen-activated protein kinase kinase kinase is
RT induced simultaneously with genes for a mitogen-activated protein kinase
RT and an S6 ribosomal protein kinase by touch, cold, and water stress in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:765-769(1996).
RN [6]
RP ACTIVITY REGULATION.
RX PubMed=10717008; DOI=10.1073/pnas.97.6.2940;
RA Kovtun Y., Chiu W.-L., Tena G., Sheen J.;
RT "Functional analysis of oxidative stress-activated mitogen-activated
RT protein kinase cascade in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2940-2945(2000).
RN [7]
RP ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=12220631; DOI=10.1016/s0014-5793(02)03162-9;
RA Droillard M.-J., Boudsocq M., Barbier-Brygoo H., Lauriere C.;
RT "Different protein kinase families are activated by osmotic stresses in
RT Arabidopsis thaliana cell suspensions. Involvement of the MAP kinases
RT AtMPK3 and AtMPK6.";
RL FEBS Lett. 527:43-50(2002).
RN [8]
RP PHOSPHORYLATION.
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 [9]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=11875555; DOI=10.1038/415977a;
RA Asai T., Tena G., Plotnikova J., Willmann M.R., Chiu W.-L., Gomez-Gomez L.,
RA Boller T., Ausubel F.M., Sheen J.;
RT "MAP kinase signalling cascade in Arabidopsis innate immunity.";
RL Nature 415:977-983(2002).
RN [10]
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 [11]
RP INTERACTION WITH NDPK2.
RX PubMed=12506203; DOI=10.1073/pnas.252641899;
RA Moon H., Lee B., Choi G., Shin D., Prasad D.T., Lee O., Kwak S.-S.,
RA Kim D.H., Nam J., Bahk J., Hong J.C., Lee S.Y., Cho M.J., Lim C.O.,
RA Yun D.-J.;
RT "NDP kinase 2 interacts with two oxidative stress-activated MAPKs to
RT regulate cellular redox state and enhances multiple stress tolerance in
RT transgenic plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:358-363(2003).
RN [12]
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, INDUCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=15500467; DOI=10.1111/j.1365-313x.2004.02229.x;
RA Ahlfors R., Macioszek V., Rudd J., Brosche M., Schlichting R., Scheel D.,
RA Kangasjarvi J.;
RT "Stress hormone-independent activation and nuclear translocation of
RT mitogen-activated protein kinases in Arabidopsis thaliana during ozone
RT exposure.";
RL Plant J. 40:512-522(2004).
RN [13]
RP FUNCTION.
RX PubMed=15964670; DOI=10.1016/j.envpol.2005.04.017;
RA Miles G.P., Samuel M.A., Zhang Y., Ellis B.E.;
RT "RNA interference-based (RNAi) suppression of AtMPK6, an Arabidopsis
RT mitogen-activated protein kinase, results in hypersensitivity to ozone and
RT misregulation of AtMPK3.";
RL Environ. Pollut. 138:230-237(2005).
RN [14]
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 [15]
RP ACTIVITY REGULATION, AND DEPHOSPHORYLATION.
RX PubMed=17586809; DOI=10.1074/jbc.m701888200;
RA Lee J.S., Ellis B.E.;
RT "Arabidopsis MAPK phosphatase 2 (MKP2) positively regulates oxidative
RT stress tolerance and inactivates the MPK3 and MPK6 MAPKs.";
RL J. Biol. Chem. 282:25020-25029(2007).
RN [16]
RP FUNCTION.
RX PubMed=17259259; DOI=10.1105/tpc.106.048298;
RA Wang H., Ngwenyama N., Liu Y., Walker J.C., Zhang S.;
RT "Stomatal development and patterning are regulated by environmentally
RT responsive mitogen-activated protein kinases in Arabidopsis.";
RL Plant Cell 19:63-73(2007).
RN [17]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH VIP1.
RX PubMed=17947581; DOI=10.1126/science.1148110;
RA Djamei A., Pitzschke A., Nakagami H., Rajh I., Hirt H.;
RT "Trojan horse strategy in Agrobacterium transformation: abusing MAPK
RT defense signaling.";
RL Science 318:453-456(2007).
RN [18]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=18273012; DOI=10.1038/nature06543;
RA Yoo S.D., Cho Y.H., Tena G., Xiong Y., Sheen J.;
RT "Dual control of nuclear EIN3 by bifurcate MAPK cascades in C2H4
RT signalling.";
RL Nature 451:789-795(2008).
RN [19]
RP FUNCTION.
RX PubMed=18378893; DOI=10.1073/pnas.0711301105;
RA Ren D., Liu Y., Yang K.Y., Han L., Mao G., Glazebrook J., Zhang S.;
RT "A fungal-responsive MAPK cascade regulates phytoalexin biosynthesis in
RT Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5638-5643(2008).
RN [20]
RP INTERACTION WITH DSPTP1B/MKP2.
RX PubMed=20626661; DOI=10.1111/j.1365-313x.2010.04297.x;
RA Lumbreras V., Vilela B., Irar S., Sole M., Capellades M., Valls M.,
RA Coca M., Pages M.;
RT "MAPK phosphatase MKP2 mediates disease responses in Arabidopsis and
RT functionally interacts with MPK3 and MPK6.";
RL Plant J. 63:1017-1030(2010).
RN [21]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=21806969; DOI=10.1016/j.bbrc.2011.07.064;
RA Kim S.H., Woo D.H., Kim J.M., Lee S.Y., Chung W.S., Moon Y.H.;
RT "Arabidopsis MKK4 mediates osmotic-stress response via its regulation of
RT MPK3 activity.";
RL Biochem. Biophys. Res. Commun. 412:150-154(2011).
RN [22]
RP FUNCTION.
RX PubMed=23263767; DOI=10.1105/tpc.112.104695;
RA Meng X., Wang H., He Y., Liu Y., Walker J.C., Torii K.U., Zhang S.;
RT "A MAPK cascade downstream of ERECTA receptor-like protein kinase regulates
RT Arabidopsis inflorescence architecture by promoting localized cell
RT proliferation.";
RL Plant Cell 24:4948-4960(2012).
RN [23]
RP INTERACTION WITH VQ4.
RX PubMed=24750137; DOI=10.1111/nph.12817;
RA Pecher P., Eschen-Lippold L., Herklotz S., Kuhle K., Naumann K., Bethke G.,
RA Uhrig J., Weyhe M., Scheel D., Lee J.;
RT "The Arabidopsis thaliana mitogen-activated protein kinases MPK3 and MPK6
RT target a subclass of 'VQ-motif'-containing proteins to regulate immune
RT responses.";
RL New Phytol. 203:592-606(2014).
RN [24]
RP FUNCTION, AND INTERACTION WITH LIP5.
RC STRAIN=cv. Columbia;
RX PubMed=25010425; DOI=10.1371/journal.ppat.1004243;
RA Wang F., Shang Y., Fan B., Yu J.-Q., Chen Z.;
RT "Arabidopsis LIP5, a positive regulator of multivesicular body biogenesis,
RT is a critical target of pathogen-responsive MAPK cascade in plant basal
RT defense.";
RL PLoS Pathog. 10:E1004243-E1004243(2014).
RN [25]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25843888; DOI=10.1016/j.devcel.2015.02.022;
RA Zhang Y., Wang P., Shao W., Zhu J.-K., Dong J.;
RT "The BASL polarity protein controls a MAPK signaling feedback loop in
RT asymmetric cell division.";
RL Dev. Cell 33:136-149(2015).
RN [26]
RP INTERACTION WITH RACK1A; RACK1B AND 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 [27]
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=27746029; DOI=10.1016/j.cub.2016.08.066;
RA Zhang Y., Guo X., Dong J.;
RT "Phosphorylation of the polarity protein BASL differentiates asymmetric
RT cell fate through MAPKs and SPCH.";
RL Curr. Biol. 26:2957-2965(2016).
RN [28]
RP INTERACTION WITH FLZ9.
RX DOI=10.1016/j.cpb.2015.10.004;
RA Nietzsche M., Landgraf R., Tohge T., Boernke F.;
RT "A protein-protein interaction network linking the energy-sensor kinase
RT SnRK1 to multiple signaling pathways in Arabidopsis thaliana.";
RL Curr. Plant Biol. 5:36-44(2016).
RN [29]
RP INTERACTION WITH MKK5.
RC STRAIN=cv. Columbia;
RX PubMed=27913741; DOI=10.1104/pp.16.01386;
RA Li K., Yang F., Zhang G., Song S., Li Y., Ren D., Miao Y., Song C.-P.;
RT "AIK1, a mitogen-activated protein kinase, modulates abscisic acid
RT responses through the MKK5-MPK6 kinase cascade.";
RL Plant Physiol. 173:1391-1408(2017).
RN [30]
RP REVIEW ON MITOGEN-ACTIVATED PROTEIN KINASE CASCADES.
RX PubMed=30349547; DOI=10.3389/fpls.2018.01387;
RA Jagodzik P., Tajdel-Zielinska M., Ciesla A., Marczak M., Ludwikow A.;
RT "Mitogen-activated protein kinase cascades in plant hormone signaling.";
RL Front. Plant Sci. 9:1387-1387(2018).
RN [31]
RP SUBCELLULAR LOCATION.
RX PubMed=31235876; DOI=10.1038/s41477-019-0440-x;
RA Putarjunan A., Ruble J., Srivastava A., Zhao C., Rychel A.L.,
RA Hofstetter A.K., Tang X., Zhu J.K., Tama F., Zheng N., Torii K.U.;
RT "Bipartite anchoring of SCREAM enforces stomatal initiation by coupling MAP
RT kinases to SPEECHLESS.";
RL Nat. Plants 5:742-754(2019).
CC -!- FUNCTION: Involved in oxidative stress-mediated signaling cascade (such
CC as ozone). Involved in the innate immune MAP kinase signaling cascade
CC (MEKK1, MKK4/MKK5 and MPK3/MPK6) downstream of bacterial flagellin
CC receptor FLS2. May be involved in hypersensitive response (HR)-mediated
CC signaling cascade by modulating LIP5 phosphorylation and subsequent
CC multivesicular bodies (MVBs) trafficking. May phosphorylate regulators
CC of WRKY transcription factors. Mediates the phosphorylation of VIP1 and
CC subsequent stress genes transcription in response to Agrobacterium.
CC MKK9-MPK3/MPK6 module phosphorylates and activates EIN3, leading to the
CC promotion of EIN3-mediated transcription in ethylene signaling.
CC MPK3/MPK6 cascade regulates camalexin synthesis through transcriptional
CC regulation of the biosynthetic genes after pathogen infection. YDA-
CC MKK4/MKK5-MPK3/MPK6 module regulates stomatal cell fate before the
CC guard mother cell (GMC) is specified. When activated, reinforces the
CC feedback loop by phosphorylating BASL, and inhibits stomatal fate by
CC phosphorylating SPCH (PubMed:25843888). This MAPK cascade also
CC functions downstream of the ER receptor in regulating coordinated local
CC cell proliferation, which shapes the morphology of plant organs.
CC {ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:15964670,
CC ECO:0000269|PubMed:17259259, ECO:0000269|PubMed:17947581,
CC ECO:0000269|PubMed:18273012, ECO:0000269|PubMed:18378893,
CC ECO:0000269|PubMed:21806969, ECO:0000269|PubMed:23263767,
CC ECO:0000269|PubMed:25010425, ECO:0000269|PubMed:25843888}.
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:12220631, ECO:0000269|PubMed:15500467};
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:12220631,
CC ECO:0000269|PubMed:15500467};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation. Activated by MAP kinase kinases MKK4, MKK5, MKK7 and
CC MKK9. Activated in response to hydrogen peroxide, ozone, salt stress
CC and flagellin bacterial elicitor. Triggered by Agrobacterium upon T-DNA
CC transfer. Repressed by DSPTP1B/MKP2-mediated dephosphorylation.
CC {ECO:0000269|PubMed:10717008, ECO:0000269|PubMed:11875555,
CC ECO:0000269|PubMed:12220631, ECO:0000269|PubMed:15500467,
CC ECO:0000269|PubMed:17586809, ECO:0000269|PubMed:17947581,
CC ECO:0000269|PubMed:18273012, ECO:0000269|PubMed:21806969}.
CC -!- SUBUNIT: Interacts with DSPTP1B/MKP2, NDPK2 and VIP1. The interaction
CC with DSPTP1B/MKP2 is repressed by fungal elicitation (PubMed:12506203,
CC PubMed:17947581, PubMed:20626661). Binds to LIP5 (PubMed:25010425).
CC Interacts with VQ4 (PubMed:24750137). Interacts with RACK1A, RACK1B and
CC RACK1C (PubMed:25731164). Interacts with FLZ9 (Ref.28). Interacts with
CC MKK5 (PubMed:27913741). {ECO:0000269|PubMed:12506203,
CC ECO:0000269|PubMed:17947581, ECO:0000269|PubMed:20626661,
CC ECO:0000269|PubMed:24750137, ECO:0000269|PubMed:25010425,
CC ECO:0000269|PubMed:25731164, ECO:0000269|PubMed:27913741,
CC ECO:0000269|Ref.28}.
CC -!- INTERACTION:
CC Q39023; O80719: At2g47060; NbExp=2; IntAct=EBI-349526, EBI-4436376;
CC Q39023; Q9ZR37: DSPTP1; NbExp=3; IntAct=EBI-349526, EBI-25512239;
CC Q39023; O24408: IAA18; NbExp=3; IntAct=EBI-349526, EBI-2295525;
CC Q39023; Q8LGS1: MARD1; NbExp=4; IntAct=EBI-349526, EBI-4443654;
CC Q39023; O80397: MKK4; NbExp=9; IntAct=EBI-349526, EBI-2358409;
CC Q39023; O64903: NDPK2; NbExp=4; IntAct=EBI-349526, EBI-349517;
CC Q39023; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-349526, EBI-15192297;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15500467}. Nucleus
CC {ECO:0000269|PubMed:15500467, ECO:0000269|PubMed:31235876}. Cytoplasm,
CC cell cortex {ECO:0000269|PubMed:25843888}. Note=Translocated into the
CC nucleus in response to phosphorylation (Probable). Recruited by BASL at
CC the cell cortex in a polarized manner (PubMed:25843888).
CC {ECO:0000269|PubMed:25843888, ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Copolarizes with BASL, YDA and MPK6 in stomatal
CC asymmetric cell division (ACD) cells. {ECO:0000269|PubMed:27746029}.
CC -!- INDUCTION: By touch, cold, salinity stress and ozone.
CC {ECO:0000269|PubMed:15500467, ECO:0000269|PubMed:8570631}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-196 and Tyr-198, which activates the
CC enzyme (By similarity). Dephosphorylated by DSPTP1B/MKP2. {ECO:0000250,
CC ECO:0000269|PubMed:11874576}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159, ECO:0000305}.
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DR EMBL; D21839; BAA04866.1; -; mRNA.
DR EMBL; AL138657; CAB75493.1; -; Genomic_DNA.
DR EMBL; AL157735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE78054.1; -; Genomic_DNA.
DR EMBL; AF386961; AAK62406.1; -; mRNA.
DR EMBL; BT000007; AAN15326.1; -; mRNA.
DR PIR; S40469; S40469.
DR PIR; T47504; T47504.
DR RefSeq; NP_190150.1; NM_114433.3.
DR AlphaFoldDB; Q39023; -.
DR SMR; Q39023; -.
DR BioGRID; 9026; 177.
DR DIP; DIP-768N; -.
DR ELM; Q39023; -.
DR IntAct; Q39023; 21.
DR MINT; Q39023; -.
DR STRING; 3702.AT3G45640.1; -.
DR iPTMnet; Q39023; -.
DR PaxDb; Q39023; -.
DR PRIDE; Q39023; -.
DR ProteomicsDB; 238272; -.
DR EnsemblPlants; AT3G45640.1; AT3G45640.1; AT3G45640.
DR GeneID; 823706; -.
DR Gramene; AT3G45640.1; AT3G45640.1; AT3G45640.
DR KEGG; ath:AT3G45640; -.
DR Araport; AT3G45640; -.
DR TAIR; locus:2085632; AT3G45640.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q39023; -.
DR OMA; MDIPRPE; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; Q39023; -.
DR BRENDA; 2.7.11.24; 399.
DR PRO; PR:Q39023; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q39023; baseline and differential.
DR Genevisible; Q39023; AT.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
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:0009738; P:abscisic acid-activated signaling pathway; TAS:TAIR.
DR GO; GO:0010120; P:camalexin biosynthetic process; IMP:TAIR.
DR GO; GO:0010229; P:inflorescence development; IGI:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0048481; P:plant ovule development; IGI:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0010183; P:pollen tube guidance; IGI:TAIR.
DR GO; GO:0009875; P:pollen-pistil interaction; IGI:TAIR.
DR GO; GO:0080136; P:priming of cellular response to stress; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR GO; GO:0010200; P:response to chitin; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0050826; P:response to freezing; IMP:TAIR.
DR GO; GO:1902065; P:response to L-glutamate; IDA:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IDA:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP: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; Hypersensitive response; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Plant defense;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transferase.
FT CHAIN 1..370
FT /note="Mitogen-activated protein kinase 3"
FT /id="PRO_0000186312"
FT DOMAIN 38..324
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 196..198
FT /note="TXY"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 44..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 198
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT CONFLICT 15
FT /note="E -> D (in Ref. 1; BAA04866)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 42717 MW; 6992A7D97F3C9841 CRC64;
MNTGGGQYTD FPAVETHGGQ FISYDIFGSL FEITSKYRPP IIPIGRGAYG IVCSVLDTET
NELVAMKKIA NAFDNHMDAK RTLREIKLLR HLDHENIIAI RDVVPPPLRR QFSDVYISTE
LMDTDLHQII RSNQSLSEEH CQYFLYQLLR GLKYIHSANI IHRDLKPSNL LLNANCDLKI
CDFGLARPTS ENDFMTEYVV TRWYRAPELL LNSSDYTAAI DVWSVGCIFM ELMNRKPLFP
GKDHVHQMRL LTELLGTPTE SDLGFTHNED AKRYIRQLPN FPRQPLAKLF SHVNPMAIDL
VDRMLTFDPN RRITVEQALN HQYLAKLHDP NDEPICQKPF SFEFEQQPLD EEQIKEMIYQ
EAIALNPTYG
