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 12-APR-2017, entry version 133.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC 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.,
RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA 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.,
RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Portal (Araport);
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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
RT 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;
RP ASP-183; GLY-523; GLU-530; SER-602; GLY-611; ALA-628; GLY-644;
RP ALA-665; GLU-667; GLY-687; GLY-715; PRO-740 AND ALA-746, INTERACTION
RP WITH MPK4, AND PHOSPHORYLATION AT SER-79; SER-150; SER-365 AND SER-768
RP 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
RP MASS 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
RT abundance triggers autoimmunity when the MEKK1-MKK1/2-MPK4 signaling
RT cascade is 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
RT changes 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
CC glutamate (L-Glu) signal that elicits large-scale changes in root
CC architecture (PubMed:23574009). {ECO:0000269|PubMed:22643122,
CC ECO:0000269|PubMed:23574009, ECO:0000269|PubMed:23695980}.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC {ECO:0000250|UniProtKB:P53778}.
CC -!- SUBUNIT: Interacts with MPK4. {ECO:0000269|PubMed:22643122}.
CC -!- INTERACTION:
CC Q39024:MPK4; NbExp=3; IntAct=EBI-6271434, EBI-994375;
CC -!- TISSUE SPECIFICITY: Expressed at least in rosette leaves (at
CC protein 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
CC not only in mkk1 mkk2 but also in mekk1 and mpk4 mutants
CC (PubMed:22643122, PubMed:23695980). In the triple mutant mekk1
CC mekk2 mekk3, no appearent phenotype, but meek1-like dwarf
CC phenotype when complemented by MEKK2 (PubMed:23695980). The triple
CC mutant mekk1 mekk2 mekk3 is almost insensitive to external
CC glutamate (L-Glu) on root growth (PubMed:23574009).
CC {ECO:0000269|PubMed:20668060, ECO:0000269|PubMed:22643122,
CC ECO:0000269|PubMed:23574009, 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 UniGene; At.33748; -.
DR ProteinModelPortal; O81472; -.
DR SMR; O81472; -.
DR IntAct; O81472; 1.
DR STRING; 3702.AT4G08480.1; -.
DR iPTMnet; O81472; -.
DR PaxDb; O81472; -.
DR PRIDE; O81472; -.
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 eggNOG; ENOG410XQGS; LUCA.
DR HOGENOM; HOG000239933; -.
DR KO; K20605; -.
DR OMA; IERKPTI; -.
DR OrthoDB; EOG0936083X; -.
DR PhylomeDB; O81472; -.
DR PRO; PR:O81472; -.
DR Proteomes; UP000006548; Chromosome 4.
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:0004702; F:signal transducer, downstream of receptor, with serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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.
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; Complete proteome; Immunity; Innate immunity; Kinase;
KW Nucleotide-binding; Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1 773 Mitogen-activated protein kinase kinase
FT kinase 9.
FT /FTId=PRO_0000434763.
FT DOMAIN 501 755 Protein kinase. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT NP_BIND 507 515 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT REGION 100 493 Regulatory region.
FT {ECO:0000250|UniProtKB:Q39008}.
FT ACT_SITE 624 624 Proton acceptor. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT BINDING 529 529 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT MOD_RES 79 79 Phosphoserine.
FT {ECO:0000269|PubMed:22643122}.
FT MOD_RES 150 150 Phosphoserine.
FT {ECO:0000269|PubMed:22643122}.
FT MOD_RES 365 365 Phosphoserine; by MAPK4.
FT {ECO:0000269|PubMed:22643122}.
FT MOD_RES 768 768 Phosphoserine.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 53 53 R->W: In summ1-13; suppression of
FT impaired plant defense responses in mkk1
FT mkk2, mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 177 177 G->D: In summ1-9; suppression of impaired
FT plant defense responses in mkk1 mkk2,
FT mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 183 183 D->N: In summ1-4; suppression of impaired
FT plant defense responses in mkk1 mkk2,
FT mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 492 492 V->I: No obvious abnormal phenotype.
FT {ECO:0000269|PubMed:20668060}.
FT MUTAGEN 523 523 G->E: In summ1-3; suppression of impaired
FT plant defense responses in mkk1 mkk2,
FT mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 527 527 A->T: No obvious abnormal phenotype.
FT {ECO:0000269|PubMed:20668060}.
FT MUTAGEN 530 530 E->K: In summ1-19; suppression of
FT impaired plant defense responses in mkk1
FT mkk2, mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 538 538 S->N: No obvious abnormal phenotype.
FT {ECO:0000269|PubMed:20668060}.
FT MUTAGEN 557 557 L->F: No obvious abnormal phenotype.
FT {ECO:0000269|PubMed:20668060}.
FT MUTAGEN 602 602 S->F: In summ1-7; suppression of impaired
FT plant defense responses in mkk1 mkk2,
FT mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 611 611 G->S: In summ1-17; suppression of
FT impaired plant defense responses in mkk1
FT mkk2, mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 628 628 A->T: In summ1-16; suppression of
FT impaired plant defense responses in mkk1
FT mkk2, mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 644 644 G->E: In summ1-8; suppression of impaired
FT plant defense responses in mkk1 mkk2,
FT mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 665 665 A->T: In summ1-18; suppression of
FT impaired plant defense responses in mkk1
FT mkk2, mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 667 667 E->K: In summ1-5; suppression of impaired
FT plant defense responses in mkk1 mkk2,
FT mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 687 687 G->R: In summ1-12; suppression of
FT impaired plant defense responses in mkk1
FT mkk2, mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 715 715 G->S: In summ1-11; suppression of
FT impaired plant defense responses in mkk1
FT mkk2, mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 740 740 P->L: In summ1-2; suppression of impaired
FT plant defense responses in mkk1 mkk2,
FT mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
FT MUTAGEN 746 746 A->T: In summ1-6; suppression of impaired
FT plant defense responses in mkk1 mkk2,
FT mekk1 and mpk4 mutants.
FT {ECO:0000269|PubMed:22643122}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 501 755 iprf:PROTEIN_KINASE_DOM [T]
FT MYHIT 502 755 ipfam:Pkinase [T]
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
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