M2K9_ARATH
ID M2K9_ARATH Reviewed; 310 AA.
AC Q9FX43;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Mitogen-activated protein kinase kinase 9;
DE Short=AtMKK9;
DE Short=MAP kinase kinase 9;
DE EC=2.7.12.2;
GN Name=MKK9; Synonyms=MAP2K9; OrderedLocusNames=At1g73500; ORFNames=T9L24.32;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 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 [6]
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 [7]
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-76; SER-201 AND THR-205,
RP AND PHOSPHORYLATION AT SER-201 AND THR-205.
RX PubMed=18693252; DOI=10.1074/jbc.m801392200;
RA Xu J., Li Y., Wang Y., Liu H., Lei L., Yang H., Liu G., Ren D.;
RT "Activation of MAPK kinase 9 induces ethylene and camalexin biosynthesis
RT and enhances sensitivity to salt stress in Arabidopsis.";
RL J. Biol. Chem. 283:26996-27006(2008).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
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 [10]
RP REVIEW.
RX PubMed=19704518; DOI=10.4161/psb.3.10.5995;
RA Yoo S.D., Sheen J.;
RT "MAPK signaling in plant hormone ethylene signal transduction.";
RL Plant Signal. Behav. 3:848-849(2008).
RN [11]
RP FUNCTION, INDUCTION, MUTAGENESIS OF LYS-76; SER-195 AND SER-201, DISRUPTION
RP PHENOTYPE, AND PHOSPHORYLATION AT SER-195 AND SER-201.
RX PubMed=19251906; DOI=10.1104/pp.108.133439;
RA Zhou C., Cai Z., Guo Y., Gan S.;
RT "An arabidopsis mitogen-activated protein kinase cascade, MKK9-MPK6, plays
RT a role in leaf senescence.";
RL Plant Physiol. 150:167-177(2009).
RN [12]
RP INDUCTION BY PATHOGEN.
RX PubMed=21947882; DOI=10.1007/s11033-011-1232-1;
RA Kannan P., Pandey D., Gupta A.K., Punetha H., Taj G., Kumar A.;
RT "Expression analysis of MAP2K9 and MAPK6 during pathogenesis of Alternaria
RT blight in Arabidopsis thaliana ecotype Columbia.";
RL Mol. Biol. Rep. 39:4439-4444(2012).
CC -!- FUNCTION: MKK9-MPK3/MPK6 module phosphorylates and activates EIN3,
CC leading to the promotion of EIN3-mediated transcription in ethylene
CC signaling. Autophosphorylates and also phosphorylates MPK3 and MPK6.
CC Plays an important role in ethylene and camalexin biosynthesis and in
CC salt stress response. MKK9-MPK6 module positively regulates leaf
CC senescence. {ECO:0000269|PubMed:18273012, ECO:0000269|PubMed:18693252,
CC ECO:0000269|PubMed:19251906}.
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 -!- 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;
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 -!- INTERACTION:
CC Q9FX43; Q9M1Z5: MPK10; NbExp=2; IntAct=EBI-2128545, EBI-2358527;
CC Q9FX43; Q8GYQ5: MPK12; NbExp=2; IntAct=EBI-2128545, EBI-2128461;
CC Q9FX43; Q9SJG9: MPK20; NbExp=2; IntAct=EBI-2128545, EBI-2358896;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18273012}. Nucleus
CC {ECO:0000269|PubMed:18273012}. Note=Translocated into the nucleus by
CC ACC treatment.
CC -!- INDUCTION: Up-regulated during leaf senescence. By Alternaria brassicae
CC pathogen infection. {ECO:0000269|PubMed:19251906,
CC ECO:0000269|PubMed:21947882}.
CC -!- PTM: Phosphorylation at Ser-195 and Ser-201 by MAP kinase kinase
CC kinases positively regulates kinase activity. Autophosphorylated
CC (Probable). {ECO:0000305|PubMed:18693252, ECO:0000305|PubMed:19251906}.
CC -!- DISRUPTION PHENOTYPE: Broad spectrum of moderate ethylene-insensitive
CC phenotypes. Reduced salt sensitivity. Delayed senescence phenotype.
CC {ECO:0000269|PubMed:18273012, ECO:0000269|PubMed:18693252,
CC ECO:0000269|PubMed:19251906}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; AC012396; AAG30984.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35470.1; -; Genomic_DNA.
DR EMBL; AK118530; BAC43133.1; -; mRNA.
DR EMBL; BT005300; AAO63364.1; -; mRNA.
DR EMBL; AY084571; AAM61137.1; -; mRNA.
DR PIR; G96761; G96761.
DR RefSeq; NP_177492.1; NM_106009.3.
DR AlphaFoldDB; Q9FX43; -.
DR SMR; Q9FX43; -.
DR BioGRID; 28904; 6.
DR IntAct; Q9FX43; 9.
DR STRING; 3702.AT1G73500.1; -.
DR iPTMnet; Q9FX43; -.
DR PaxDb; Q9FX43; -.
DR PRIDE; Q9FX43; -.
DR EnsemblPlants; AT1G73500.1; AT1G73500.1; AT1G73500.
DR GeneID; 843685; -.
DR Gramene; AT1G73500.1; AT1G73500.1; AT1G73500.
DR KEGG; ath:AT1G73500; -.
DR Araport; AT1G73500; -.
DR TAIR; locus:2206885; AT1G73500.
DR eggNOG; KOG0581; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q9FX43; -.
DR OMA; RITCVSK; -.
DR OrthoDB; 688282at2759; -.
DR PhylomeDB; Q9FX43; -.
DR BRENDA; 2.7.12.2; 399.
DR PRO; PR:Q9FX43; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FX43; baseline and differential.
DR Genevisible; Q9FX43; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IDA:TAIR.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; HDA:TAIR.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0010120; P:camalexin biosynthetic process; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009693; P:ethylene biosynthetic process; IDA:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:UniProtKB.
DR GO; GO:0009875; P:pollen-pistil interaction; IGI:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0009620; P:response to fungus; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
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 ATP-binding; Cytoplasm; Ethylene biosynthesis; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Stress response; Transferase.
FT CHAIN 1..310
FT /note="Mitogen-activated protein kinase kinase 9"
FT /id="PRO_0000428625"
FT DOMAIN 47..306
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 53..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:19251906"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:18693252,
FT ECO:0000305|PubMed:19251906"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:18693252"
FT MUTAGEN 76
FT /note="K->R: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:18693252,
FT ECO:0000269|PubMed:19251906"
FT MUTAGEN 195
FT /note="S->E: Constitutively active; when associated with E-
FT 201."
FT /evidence="ECO:0000269|PubMed:19251906"
FT MUTAGEN 201
FT /note="S->D: Constitutively active; when associated with D-
FT 205."
FT /evidence="ECO:0000269|PubMed:18693252,
FT ECO:0000269|PubMed:19251906"
FT MUTAGEN 201
FT /note="S->E: Constitutively active; when associated with E-
FT 195."
FT /evidence="ECO:0000269|PubMed:18693252,
FT ECO:0000269|PubMed:19251906"
FT MUTAGEN 205
FT /note="T->D: Constitutively active; when associated with D-
FT 201."
FT /evidence="ECO:0000269|PubMed:18693252"
SQ SEQUENCE 310 AA; 34347 MW; CF855943643D9261 CRC64;
MALVRERRQL NLRLPLPPIS DRRFSTSSSS ATTTTVAGCN GISACDLEKL NVLGCGNGGI
VYKVRHKTTS EIYALKTVNG DMDPIFTRQL MREMEILRRT DSPYVVKCHG IFEKPVVGEV
SILMEYMDGG TLESLRGGVT EQKLAGFAKQ ILKGLSYLHA LKIVHRDIKP ANLLLNSKNE
VKIADFGVSK ILVRSLDSCN SYVGTCAYMS PERFDSESSG GSSDIYAGDI WSFGLMMLEL
LVGHFPLLPP GQRPDWATLM CAVCFGEPPR APEGCSEEFR SFVECCLRKD SSKRWTAPQL
LAHPFLREDL
