M2K5_ARATH
ID M2K5_ARATH Reviewed; 348 AA.
AC Q8RXG3; O80398; Q96517;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Mitogen-activated protein kinase kinase 5 {ECO:0000303|PubMed:10048483};
DE Short=AtMAP2Kalpha {ECO:0000303|Ref.2};
DE Short=AtMEK5 {ECO:0000303|PubMed:11687590};
DE Short=AtMKK5 {ECO:0000303|PubMed:10048483};
DE Short=MAP kinase kinase 5 {ECO:0000303|PubMed:10048483};
DE EC=2.7.12.2 {ECO:0000269|PubMed:11875555};
GN Name=MKK5 {ECO:0000303|PubMed:10048483};
GN Synonyms=MEK5 {ECO:0000303|PubMed:11687590};
GN OrderedLocusNames=At3g21220 {ECO:0000312|Araport:AT3G21220};
GN ORFNames=MXL8.8 {ECO:0000312|EMBL:BAB01714.1};
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10048483; DOI=10.1093/dnares/5.6.341;
RA Ichimura K., Mizoguchi T., Hayashida N., Seki M., Shinozaki K.;
RT "Molecular cloning and characterization of three cDNAs encoding putative
RT mitogen-activated protein kinase kinases (MAPKKs) in Arabidopsis
RT thaliana.";
RL DNA Res. 5:341-348(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Root;
RA Hamal A., Jouannic S., Leprince A.-S., Kreis M., Henry Y.;
RT "Molecular characterization and expression of an Arabidopsis thaliana L.
RT MAP kinase kinase cDNA AtMAP2Kalpha.";
RL Plant Sci. 140:41-52(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND MUTAGENESIS OF LYS-99; THR-215 AND SER-221.
RX PubMed=11687590; DOI=10.1074/jbc.m109495200;
RA Ren D., Yang H., Zhang S.;
RT "Cell death mediated by MAPK is associated with hydrogen peroxide
RT production in Arabidopsis.";
RL J. Biol. Chem. 277:559-565(2002).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT
RP THR-215 AND SER-221, AND MUTAGENESIS OF LYS-99; THR-215 AND SER-221.
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 [8]
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 [9]
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 [10]
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 [11]
RP FUNCTION.
RX PubMed=18268539; DOI=10.1038/cr.2008.29;
RA Liu H., Wang Y., Xu J., Su T., Liu G., Ren D.;
RT "Ethylene signaling is required for the acceleration of cell death induced
RT by the activation of AtMEK5 in Arabidopsis.";
RL Cell Res. 18:422-432(2008).
RN [12]
RP INTERACTION WITH MPK6.
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 [13]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18809915; DOI=10.1073/pnas.0805539105;
RA Cho S.K., Larue C.T., Chevalier D., Wang H., Jinn T.-L., Zhang S.,
RA Walker J.C.;
RT "Regulation of floral organ abscission in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15629-15634(2008).
RN [14]
RP INTERACTION WITH P.SYRINGAE HOPF2, ADP-RIBOSYLATION AT ARG-313, MUTAGENESIS
RP OF ARG-313, ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=20571112; DOI=10.1105/tpc.110.075697;
RA Wang Y., Li J., Hou S., Wang X., Li Y., Ren D., Chen S., Tang X.,
RA Zhou J.M.;
RT "A Pseudomonas syringae ADP-ribosyltransferase inhibits Arabidopsis
RT mitogen-activated protein kinase kinases.";
RL Plant Cell 22:2033-2044(2010).
RN [15]
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 [16]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=23341468; DOI=10.1074/jbc.m112.384453;
RA Khan M., Rozhon W., Bigeard J., Pflieger D., Husar S., Pitzschke A.,
RA Teige M., Jonak C., Hirt H., Poppenberger B.;
RT "Brassinosteroid-regulated GSK3/Shaggy-like kinases phosphorylate mitogen-
RT activated protein (MAP) kinase kinases, which control stomata development
RT in Arabidopsis thaliana.";
RL J. Biol. Chem. 288:7519-7527(2013).
RN [17]
RP FUNCTION, INTERACTION WITH BZR1, AND MUTAGENESIS OF LYS-99.
RX PubMed=24019147; DOI=10.1074/mcp.m113.029256;
RA Wang C., Shang J.X., Chen Q.X., Oses-Prieto J.A., Bai M.Y., Yang Y.,
RA Yuan M., Zhang Y.L., Mu C.C., Deng Z., Wei C.Q., Burlingame A.L.,
RA Wang Z.Y., Sun Y.;
RT "Identification of BZR1-interacting proteins as potential components of the
RT brassinosteroid signaling pathway in Arabidopsis through tandem affinity
RT purification.";
RL Mol. Cell. Proteomics 12:3653-3665(2013).
RN [18]
RP FUNCTION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23677921; DOI=10.1093/pcp/pct072;
RA Xing Y., Cao Q., Zhang Q., Qin L., Jia W., Zhang J.;
RT "MKK5 regulates high light-induced gene expression of Cu/Zn superoxide
RT dismutase 1 and 2 in Arabidopsis.";
RL Plant Cell Physiol. 54:1217-1227(2013).
RN [19]
RP INTERACTION WITH BASL.
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 [20]
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 [21]
RP INTERACTION WITH MAPKKK5, PHOSPHORYLATION BY MAPKKK5, AND MUTAGENESIS OF
RP LYS-99; THR-215 AND SER-221.
RC STRAIN=cv. Columbia;
RX PubMed=27679653; DOI=10.15252/embj.201694248;
RA Yamada K., Yamaguchi K., Shirakawa T., Nakagami H., Mine A., Ishikawa K.,
RA Fujiwara M., Narusaka M., Narusaka Y., Ichimura K., Kobayashi Y.,
RA Matsui H., Nomura Y., Nomoto M., Tada Y., Fukao Y., Fukamizo T., Tsuda K.,
RA Shirasu K., Shibuya N., Kawasaki T.;
RT "The Arabidopsis CERK1-associated kinase PBL27 connects chitin perception
RT to MAPK activation.";
RL EMBO J. 35:2468-2483(2016).
RN [22]
RP FUNCTION, MUTAGENESIS OF LYS-99, DISRUPTION PHENOTYPE, INTERACTION WITH
RP MAPKKK20; MPK6 AND MPK3, PHOSPHORYLATION, AND ACTIVITY REGULATION.
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 [23]
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).
CC -!- FUNCTION: Mitogen-activated protein kinase kinase (MAPKK) which
CC regulates abscisic acid (ABA) responses in a MAPKKK20-MKK5-MPK6 cascade
CC involved in root growth (e.g. root cell division and elongation) and
CC stomatal response, probably via MAPK6 activation by protein
CC phosphorylation (PubMed:27913741). Involved in the second phase of
CC hydrogen peroxide generation during hypersensitive response-like cell
CC death. Involved in the innate immune MAP kinase signaling cascade
CC (MEKK1, MKK4/MKK5 and MPK3/MPK6) downstream of bacterial flagellin
CC receptor FLS2. Activates by phosphorylation the downstream MPK3 and
CC MPK6. YDA-MKK4/MKK5-MPK3/MPK6 module regulates stomatal cell fate
CC before the guard mother cell (GMC) is specified. 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. MKK4
CC and MKK5 participate in the regulation of floral organ abscission.
CC Target of the Pseudomonas syringae type III effector HopF2, that
CC inhibits the activation of the downstream MPK6 and PAMP-triggered
CC immunity. Plays a critical role in high light stress tolerance by the
CC mediation of the Cu/Zn SODs CSD1 and CSD2 gene expression.
CC Phosphorylates BZR1 in vitro. {ECO:0000269|PubMed:11687590,
CC ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:17259259,
CC ECO:0000269|PubMed:18268539, ECO:0000269|PubMed:18809915,
CC ECO:0000269|PubMed:20571112, ECO:0000269|PubMed:23263767,
CC ECO:0000269|PubMed:23341468, ECO:0000269|PubMed:23677921,
CC ECO:0000269|PubMed:24019147, ECO:0000269|PubMed:27913741}.
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=2.7.12.2;
CC Evidence={ECO:0000269|PubMed:11875555};
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=2.7.12.2; Evidence={ECO:0000269|PubMed:11875555};
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=2.7.12.2;
CC Evidence={ECO:0000269|PubMed:11875555};
CC -!- ACTIVITY REGULATION: Activated through serine and threonine
CC phosphorylation by MEKK1 and MAPKKK20 in response to abscisic acid
CC (ABA). Inhibited through phosphorylation by GSK3/Shaggy-like kinase
CC ASKs. Inhibited through ADP-Ribosylation by P.syringae HopF2. Activated
CC after high light stress. {ECO:0000269|PubMed:11875555,
CC ECO:0000269|PubMed:20571112, ECO:0000269|PubMed:23341468,
CC ECO:0000269|PubMed:23677921}.
CC -!- SUBUNIT: Interacts with P.syringae type III effector HopF2
CC (PubMed:20571112). Interacts with BZR1 (PubMed:24019147). Interacts
CC with MPK6 and MPK3 (PubMed:19513235, PubMed:27913741). Interacts with
CC RACK1A, RACK1B and RACK1C (PubMed:25731164). Interacts with MAPKKK5
CC mainly in the cytosol (PubMed:27679653). Binds to BASL
CC (PubMed:25843888). Interacts with MAPKKK20 (PubMed:27913741).
CC {ECO:0000269|PubMed:19513235, ECO:0000269|PubMed:20571112,
CC ECO:0000269|PubMed:24019147, ECO:0000269|PubMed:25731164,
CC ECO:0000269|PubMed:25843888, ECO:0000269|PubMed:27679653,
CC ECO:0000269|PubMed:27913741}.
CC -!- INTERACTION:
CC Q8RXG3; Q39026: MPK6; NbExp=4; IntAct=EBI-2358458, EBI-349548;
CC -!- TISSUE SPECIFICITY: Expressed higher in stems and leaves than in
CC flowers and roots. {ECO:0000269|PubMed:10048483, ECO:0000269|Ref.2}.
CC -!- PTM: Phosphorylation at Thr-215 and Ser-221 by MAP kinase kinase
CC kinases positively regulates kinase activity (PubMed:11875555).
CC Phosphorylated by MAPKKK5 and MAPKKK20 in response to abscisic acid
CC (ABA) (PubMed:27679653, PubMed:27913741). {ECO:0000269|PubMed:11875555,
CC ECO:0000269|PubMed:27679653, ECO:0000269|PubMed:27913741}.
CC -!- PTM: ADP-ribosylation at Arg-313 by P.syringae type III effector HopF2
CC reduces the ability of the protein to phosphorylate downstream MPK6.
CC {ECO:0000269|PubMed:11875555}.
CC -!- DISRUPTION PHENOTYPE: RNAi double mutants MKK4 and MKK5 have a strong
CC abscission defect. RNAi mutant MKK5 shows super-sensitivity to high
CC light stress. Insensitivity to abscisic acid (ABA) in terms of root
CC growth inhibition (e.g. root cell division and elongation) and stomatal
CC response leading to increased water loss under dehydrated conditions
CC (PubMed:27913741). Impaired ABA-mediated increased activity of MPK6
CC (PubMed:27913741). {ECO:0000269|PubMed:18809915,
CC ECO:0000269|PubMed:23677921, ECO:0000269|PubMed:27913741}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL91161.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM47877.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB015316; BAA28831.1; -; mRNA.
DR EMBL; Y07694; CAA68958.1; -; mRNA.
DR EMBL; AB023045; BAB01714.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76478.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64001.1; -; Genomic_DNA.
DR EMBL; AY081272; AAL91161.1; ALT_FRAME; mRNA.
DR EMBL; AY114558; AAM47877.1; ALT_INIT; mRNA.
DR PIR; T51340; T51340.
DR PIR; T52635; T52635.
DR RefSeq; NP_001319606.1; NM_001338511.1.
DR RefSeq; NP_188759.1; NM_113017.4.
DR AlphaFoldDB; Q8RXG3; -.
DR SMR; Q8RXG3; -.
DR BioGRID; 7008; 7.
DR IntAct; Q8RXG3; 1.
DR STRING; 3702.AT3G21220.1; -.
DR iPTMnet; Q8RXG3; -.
DR PaxDb; Q8RXG3; -.
DR PRIDE; Q8RXG3; -.
DR ProteomicsDB; 238789; -.
DR EnsemblPlants; AT3G21220.1; AT3G21220.1; AT3G21220.
DR EnsemblPlants; AT3G21220.2; AT3G21220.2; AT3G21220.
DR GeneID; 821676; -.
DR Gramene; AT3G21220.1; AT3G21220.1; AT3G21220.
DR Gramene; AT3G21220.2; AT3G21220.2; AT3G21220.
DR KEGG; ath:AT3G21220; -.
DR Araport; AT3G21220; -.
DR TAIR; locus:2094761; AT3G21220.
DR eggNOG; KOG0581; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q8RXG3; -.
DR OMA; ASQEFRH; -.
DR OrthoDB; 688282at2759; -.
DR PhylomeDB; Q8RXG3; -.
DR BRENDA; 2.7.12.2; 399.
DR PRO; PR:Q8RXG3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RXG3; baseline and differential.
DR Genevisible; Q8RXG3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IEA:UniProtKB-EC.
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:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0098542; P:defense response to other organism; IMP:TAIR.
DR GO; GO:0010227; P:floral organ abscission; IMP:TAIR.
DR GO; GO:0010229; P:inflorescence development; IGI:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:UniProtKB.
DR GO; GO:0010365; P:positive regulation of ethylene biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010082; P:regulation of root meristem growth; IMP:UniProtKB.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0051510; P:regulation of unidimensional cell growth; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR 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 Abscisic acid signaling pathway; ADP-ribosylation; ATP-binding;
KW Hypersensitive response; Kinase; Nucleotide-binding; Phosphoprotein;
KW Plant defense; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..348
FT /note="Mitogen-activated protein kinase kinase 5"
FT /id="PRO_0000245824"
FT DOMAIN 70..325
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 76..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 6
FT /note="Phosphoserine; by ASK7"
FT /evidence="ECO:0000250"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11875555"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11875555"
FT MOD_RES 221
FT /note="Phosphoserine; by ASK7"
FT /evidence="ECO:0000250"
FT MOD_RES 225
FT /note="Phosphothreonine; by ASK7"
FT /evidence="ECO:0000250|UniProtKB:O80397"
FT MOD_RES 313
FT /note="ADP-ribosylarginine; by HopF2"
FT /evidence="ECO:0000269|PubMed:20571112"
FT MUTAGEN 99
FT /note="K->M: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:11687590,
FT ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:24019147"
FT MUTAGEN 99
FT /note="K->R: Loss of kinase activity. Phosphorylated by
FT MAPKKK5 and MAPKKK20."
FT /evidence="ECO:0000269|PubMed:11687590,
FT ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:24019147,
FT ECO:0000269|PubMed:27679653, ECO:0000269|PubMed:27913741"
FT MUTAGEN 215
FT /note="T->A: Impaired phosphorylation by MAPKKK5; when
FT associated with A-221."
FT /evidence="ECO:0000269|PubMed:27679653"
FT MUTAGEN 215
FT /note="T->D: Constitutively active; when associated with D-
FT 221."
FT /evidence="ECO:0000269|PubMed:11687590,
FT ECO:0000269|PubMed:11875555"
FT MUTAGEN 215
FT /note="T->E: Constitutively active; when associated with E-
FT 221."
FT /evidence="ECO:0000269|PubMed:11687590,
FT ECO:0000269|PubMed:11875555"
FT MUTAGEN 221
FT /note="S->A: Impaired phosphorylation by MAPKKK5; when
FT associated with A-215."
FT /evidence="ECO:0000269|PubMed:27679653"
FT MUTAGEN 221
FT /note="S->D: Constitutively active; when associated with D-
FT 215."
FT /evidence="ECO:0000269|PubMed:11687590,
FT ECO:0000269|PubMed:11875555"
FT MUTAGEN 221
FT /note="S->E: Constitutively active; when associated with E-
FT 215."
FT /evidence="ECO:0000269|PubMed:11687590,
FT ECO:0000269|PubMed:11875555"
FT MUTAGEN 313
FT /note="R->A,K: Loss of ADP-ribosylation."
FT /evidence="ECO:0000269|PubMed:20571112"
FT CONFLICT 192
FT /note="N -> D (in Ref. 1; BAA28831)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 38329 MW; 216C96728F34B5B5 CRC64;
MKPIQSPSGV ASPMKNRLRK RPDLSLPLPH RDVALAVPLP LPPPSSSSSA PASSSAISTN
ISAAKSLSEL ERVNRIGSGA GGTVYKVIHT PTSRPFALKV IYGNHEDTVR RQICREIEIL
RSVDHPNVVK CHDMFDHNGE IQVLLEFMDQ GSLEGAHIWQ EQELADLSRQ ILSGLAYLHR
RHIVHRDIKP SNLLINSAKN VKIADFGVSR ILAQTMDPCN SSVGTIAYMS PERINTDLNH
GRYDGYAGDV WSLGVSILEF YLGRFPFAVS RQGDWASLMC AICMSQPPEA PATASQEFRH
FVSCCLQSDP PKRWSAQQLL QHPFILKATG GPNLRQMLPP PRPLPSAS
