MP3K2_ARATH
ID MP3K2_ARATH Reviewed; 773 AA.
AC O81472;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 9 {ECO:0000303|PubMed:22643122};
DE Short=MAP kinase kinase kinase 9 {ECO:0000303|PubMed:22643122};
DE EC=2.7.11.24 {ECO:0000250|UniProtKB:P53778};
DE AltName: Full=MAPK/ERK kinase kinase 2 {ECO:0000303|PubMed:12119167};
DE Short=AtMEKK2 {ECO:0000303|PubMed:12119167};
DE AltName: Full=Protein SUPPRESSOR OF MKK1 MKK2 1 {ECO:0000303|PubMed:22643122};
GN Name=MEKK2 {ECO:0000303|PubMed:12119167};
GN Synonyms=MAPKKK9 {ECO:0000303|PubMed:22643122},
GN SUMM1 {ECO:0000303|PubMed:22643122};
GN OrderedLocusNames=At4g08480 {ECO:0000312|EMBL:AEE82649.1};
GN ORFNames=T15F16.3 {ECO:0000312|EMBL:AAC28188.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
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 [2]
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 [3]
RP 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 [4]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF VAL-492; ALA-527; SER-538 AND
RP LEU-557.
RX PubMed=20668060; DOI=10.1104/pp.110.159897;
RA Bush S.M., Krysan P.J.;
RT "iTILLING: a personalized approach to the identification of induced
RT mutations in Arabidopsis.";
RL Plant Physiol. 154:25-35(2010).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-53; GLY-177; ASP-183;
RP GLY-523; GLU-530; SER-602; GLY-611; ALA-628; GLY-644; ALA-665; GLU-667;
RP GLY-687; GLY-715; PRO-740 AND ALA-746, INTERACTION WITH MPK4, AND
RP PHOSPHORYLATION AT SER-79; SER-150; SER-365 AND SER-768 BY MAPK4.
RC STRAIN=cv. Columbia;
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, REGULATION BY MPK4, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=23695980; DOI=10.1105/tpc.113.112102;
RA Su S.-H., Bush S.M., Zaman N., Stecker K., Sussman M.R., Krysan P.;
RT "Deletion of a tandem gene family in Arabidopsis: increased MEKK2 abundance
RT triggers autoimmunity when the MEKK1-MKK1/2-MPK4 signaling cascade is
RT disrupted.";
RL Plant Cell 25:1895-1910(2013).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23574009; DOI=10.1111/tpj.12201;
RA Forde B.G., Cutler S.R., Zaman N., Krysan P.J.;
RT "Glutamate signalling via a MEKK1 kinase-dependent pathway induces changes
RT in Arabidopsis root architecture.";
RL Plant J. 75:1-10(2013).
CC -!- FUNCTION: Triggers SUMM2-mediated immune responses, including cell
CC death and defense responses. Probably inhibited by the MEKK1-MKK1/
CC MKK2-MPK4 kinase cascade to adjust plant defense (PubMed:22643122,
CC PubMed:23695980). Seems to contribute in transducing external glutamate
CC (L-Glu) signal that elicits large-scale changes in root architecture
CC (PubMed:23574009). {ECO:0000269|PubMed:22643122,
CC ECO:0000269|PubMed:23574009, ECO:0000269|PubMed:23695980}.
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:0000250|UniProtKB:P53778};
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:0000250|UniProtKB:P53778};
CC -!- SUBUNIT: Interacts with MPK4. {ECO:0000269|PubMed:22643122}.
CC -!- INTERACTION:
CC O81472; Q39024: MPK4; NbExp=3; IntAct=EBI-6271434, EBI-994375;
CC -!- TISSUE SPECIFICITY: Expressed at least in rosette leaves (at protein
CC level). {ECO:0000269|PubMed:23695980}.
CC -!- INDUCTION: Down-regulated by MPK4. {ECO:0000269|PubMed:23695980}.
CC -!- PTM: Phosphorylated by MPK4 upon treatment with flg22.
CC {ECO:0000269|PubMed:22643122}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:20668060,
CC PubMed:23695980). Suppresses the cell death and defense responses not
CC only in mkk1 mkk2 but also in mekk1 and mpk4 mutants (PubMed:22643122,
CC PubMed:23695980). In the triple mutant mekk1 mekk2 mekk3, no apparent
CC phenotype, but meek1-like dwarf phenotype when complemented by MEKK2
CC (PubMed:23695980). The triple mutant mekk1 mekk2 mekk3 is almost
CC insensitive to external glutamate (L-Glu) on root growth
CC (PubMed:23574009). {ECO:0000269|PubMed:20668060,
CC ECO:0000269|PubMed:22643122, ECO:0000269|PubMed:23574009,
CC ECO:0000269|PubMed:23695980}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; AF076275; AAC28188.1; -; Genomic_DNA.
DR EMBL; AL161511; CAB77973.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82649.1; -; Genomic_DNA.
DR PIR; T01835; T01835.
DR RefSeq; NP_192588.1; NM_116917.4.
DR AlphaFoldDB; O81472; -.
DR SMR; O81472; -.
DR IntAct; O81472; 1.
DR STRING; 3702.AT4G08480.1; -.
DR iPTMnet; O81472; -.
DR PaxDb; O81472; -.
DR PRIDE; O81472; -.
DR ProteomicsDB; 239066; -.
DR EnsemblPlants; AT4G08480.1; AT4G08480.1; AT4G08480.
DR GeneID; 826407; -.
DR Gramene; AT4G08480.1; AT4G08480.1; AT4G08480.
DR KEGG; ath:AT4G08480; -.
DR Araport; AT4G08480; -.
DR TAIR; locus:2133539; AT4G08480.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_000288_2_6_1; -.
DR InParanoid; O81472; -.
DR OMA; HIDYEAS; -.
DR OrthoDB; 630495at2759; -.
DR PhylomeDB; O81472; -.
DR BRENDA; 2.7.11.25; 399.
DR PRO; PR:O81472; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81472; baseline and differential.
DR Genevisible; O81472; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0031347; P:regulation of defense response; IMP:UniProtKB.
DR GO; GO:1902065; P:response to L-glutamate; IMP:UniProtKB.
DR GO; GO:0022622; P:root system development; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Immunity; Innate immunity; Kinase; Nucleotide-binding;
KW Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..773
FT /note="Mitogen-activated protein kinase kinase kinase 9"
FT /id="PRO_0000434763"
FT DOMAIN 501..755
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..493
FT /note="Regulatory region"
FT /evidence="ECO:0000250|UniProtKB:Q39008"
FT REGION 426..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 624
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 507..515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22643122"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22643122"
FT MOD_RES 365
FT /note="Phosphoserine; by MAPK4"
FT /evidence="ECO:0000269|PubMed:22643122"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 53
FT /note="R->W: In summ1-13; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 177
FT /note="G->D: In summ1-9; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 183
FT /note="D->N: In summ1-4; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 492
FT /note="V->I: No obvious abnormal phenotype."
FT /evidence="ECO:0000269|PubMed:20668060"
FT MUTAGEN 523
FT /note="G->E: In summ1-3; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 527
FT /note="A->T: No obvious abnormal phenotype."
FT /evidence="ECO:0000269|PubMed:20668060"
FT MUTAGEN 530
FT /note="E->K: In summ1-19; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 538
FT /note="S->N: No obvious abnormal phenotype."
FT /evidence="ECO:0000269|PubMed:20668060"
FT MUTAGEN 557
FT /note="L->F: No obvious abnormal phenotype."
FT /evidence="ECO:0000269|PubMed:20668060"
FT MUTAGEN 602
FT /note="S->F: In summ1-7; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 611
FT /note="G->S: In summ1-17; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 628
FT /note="A->T: In summ1-16; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 644
FT /note="G->E: In summ1-8; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 665
FT /note="A->T: In summ1-18; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 667
FT /note="E->K: In summ1-5; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 687
FT /note="G->R: In summ1-12; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 715
FT /note="G->S: In summ1-11; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 740
FT /note="P->L: In summ1-2; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
FT MUTAGEN 746
FT /note="A->T: In summ1-6; suppression of impaired plant
FT defense responses in mkk1 mkk2, mekk1 and mpk4 mutants."
FT /evidence="ECO:0000269|PubMed:22643122"
SQ SEQUENCE 773 AA; 84974 MW; 1813278CE0B31BBB CRC64;
MKKSSDKSPV RQHDTATQIN SDAVSSSTSF TDSDSTCSFL TPSMEFPDRI SFRRIDFSEA
APTGVVLPST SSELTRSNSS ENKIPNEDIS VSTSSRYLVF DKILALMKKS PGRRGDKTSP
ARRLDRSDAV RRNIDYDAGE DSSSLLITRS LDFPNRTSFR VDGVDDGEID RIYQYIGVSG
PEDFAISSDA WKARMEHERS SSDVVNKLKS LDLDSREAGP SGGVVASSSM NHKFQGHDLS
EAGSIGVVVA SNFTLSESNK IENLNSLRDK EIVDGDMVEN RCGIERKPTI LVKSRGYLVH
NDDVGVGGGI KGVRPPVLNV PRADKEVVDG GTVESKSGIE WKPTILVKSK GYLVSNDGGI
KGVTSPVLNL RPTDKEVVDS GTVENRRGIK GVRPSVLKPP PVMKLPPVDL PGSSWDILTH
FAPDSEIVRR PSSSSSSENG CDEEEAEDDK VEKEETGDMF IQLEDTTDEA CSFTTNEGDS
SSTVSNTSPI CVSGGSINTS WQKGQLLRQG SFGSVYEAIS EDGDFFAVKE VSLLDQGSQA
QECIQQLEGE IALLSQLEHQ NILRYRGTDK DGSNLYIFLE LVTQGSLLEL YRRYQIRDSL
ISLYTKQILD GLKYLHHKGF IHRDIKCATI LVDANGTVKL ADFGLAKVSK LNDIKSRKET
LFWMAPEVIN RKDNDGYRSP ADIWSLGCTV LEMCTGQIPY SDLEPVEALF RIRRGTLPEV
PDTLSLDARH FILKCLKLNP EERPTATELL NHPFVRRPLP SSGSGSTSPL IRR
