M2K7_ARATH
ID M2K7_ARATH Reviewed; 307 AA.
AC Q9LPQ3; A0ME75;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Mitogen-activated protein kinase kinase 7;
DE Short=AtMKK7;
DE Short=MAP kinase kinase 7;
DE EC=2.7.12.2;
DE AltName: Full=Protein BUSHY AND DWARF 1;
GN Name=MKK7; Synonyms=BUD1; OrderedLocusNames=At1g18350; ORFNames=F15H18.14;
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], FUNCTION, MUTANT BUD1, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF LYS-74.
RX PubMed=16377756; DOI=10.1105/tpc.105.037846;
RA Dai Y., Wang H., Li B., Huang J., Liu X., Zhou Y., Mou Z., Li J.;
RT "Increased expression of MAP KINASE KINASE7 causes deficiency in polar
RT auxin transport and leads to plant architectural abnormality in
RT Arabidopsis.";
RL Plant Cell 18:308-320(2006).
RN [2]
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 [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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
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 [6]
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 [7]
RP FUNCTION, AND INDUCTION BY PATHOGEN.
RX PubMed=17908155; DOI=10.1111/j.1365-313x.2007.03294.x;
RA Zhang X., Dai Y., Xiong Y., DeFraia C., Li J., Dong X., Mou Z.;
RT "Overexpression of Arabidopsis MAP kinase kinase 7 leads to activation of
RT plant basal and systemic acquired resistance.";
RL Plant J. 52:1066-1079(2007).
RN [8]
RP FUNCTION.
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 [9]
RP REVIEW.
RX PubMed=19704652; DOI=10.4161/psb.3.4.5230;
RA Zhang X., Xiong Y., Defraia C., Schmelz E., Mou Z.;
RT "The Arabidopsis MAP kinase kinase 7: A crosstalk point between auxin
RT signaling and defense responses?";
RL Plant Signal. Behav. 3:272-274(2008).
RN [10]
RP INTERACTION WITH MPK15.
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).
CC -!- FUNCTION: May function as a negative regulator of polar auxin
CC transport. Positively regulates plant basal and systemic acquired
CC resistance (SAR). Activates MPK3 and MPK6 in vitro.
CC {ECO:0000269|PubMed:16377756, ECO:0000269|PubMed:17908155,
CC ECO:0000269|PubMed:18273012}.
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 -!- SUBUNIT: Interacts with MPK15. {ECO:0000269|PubMed:19513235}.
CC -!- INTERACTION:
CC Q9LPQ3; Q9FYK5: ESR2; NbExp=3; IntAct=EBI-2128593, EBI-1536925;
CC Q9LPQ3; O64682: PID; NbExp=3; IntAct=EBI-2128593, EBI-1393382;
CC Q9LPQ3; Q9LNV3: STP2; NbExp=3; IntAct=EBI-2128593, EBI-25512884;
CC Q9LPQ3; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-2128593, EBI-15192297;
CC Q9LPQ3; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-2128593, EBI-4426557;
CC Q9LPQ3; Q5CCK4: VAL2; NbExp=5; IntAct=EBI-2128593, EBI-15193683;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues, with a relatively higher
CC level in leaves and lower level in roots and flowers.
CC {ECO:0000269|PubMed:16377756}.
CC -!- INDUCTION: By Pseudomonas syringae pv. tomato (Pst) DC3000/avrRpt2
CC infection. {ECO:0000269|PubMed:17908155}.
CC -!- PTM: Phosphorylation at Ser-193 and Ser-199 by MAP kinase kinase
CC kinases positively regulates kinase activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: Overexpression of MKK5 (mutant bud1) causes deficiency
CC in polar auxin transport and leads to plant architectural abnormality
CC (PubMed:16377756). The bud1 mutant accumulates elevated levels of SA,
CC and exhibits constitutive PR gene expression and enhanced resistance to
CC both bacterial and oomycete pathogens (PubMed:17908155).
CC {ECO:0000305|PubMed:16377756, ECO:0000305|PubMed:17908155}.
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=ABK28402.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ185389; ABA70752.1; -; mRNA.
DR EMBL; AC013354; AAF25995.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29706.1; -; Genomic_DNA.
DR EMBL; DQ446261; ABE65631.1; -; mRNA.
DR EMBL; DQ652843; ABK28402.1; ALT_SEQ; mRNA.
DR RefSeq; NP_173271.1; NM_101693.3.
DR AlphaFoldDB; Q9LPQ3; -.
DR SMR; Q9LPQ3; -.
DR BioGRID; 23655; 6.
DR DIP; DIP-52434N; -.
DR IntAct; Q9LPQ3; 9.
DR STRING; 3702.AT1G18350.1; -.
DR PaxDb; Q9LPQ3; -.
DR PRIDE; Q9LPQ3; -.
DR EnsemblPlants; AT1G18350.1; AT1G18350.1; AT1G18350.
DR GeneID; 838416; -.
DR Gramene; AT1G18350.1; AT1G18350.1; AT1G18350.
DR KEGG; ath:AT1G18350; -.
DR Araport; AT1G18350; -.
DR TAIR; locus:2014099; AT1G18350.
DR eggNOG; KOG0581; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q9LPQ3; -.
DR OMA; REVHIMT; -.
DR OrthoDB; 688282at2759; -.
DR PhylomeDB; Q9LPQ3; -.
DR PRO; PR:Q9LPQ3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPQ3; baseline and differential.
DR Genevisible; Q9LPQ3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0004708; F:MAP kinase kinase activity; TAS: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:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:TAIR.
DR GO; GO:0009875; P:pollen-pistil interaction; IGI:TAIR.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00109; TYRKINASE.
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; Kinase; Nucleotide-binding; Phosphoprotein; Plant defense;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..307
FT /note="Mitogen-activated protein kinase kinase 7"
FT /id="PRO_0000428623"
FT DOMAIN 45..303
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 51..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O80396"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O80397"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O80397"
FT MUTAGEN 74
FT /note="K->R: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:16377756"
SQ SEQUENCE 307 AA; 34272 MW; 7F831976745C4FEA CRC64;
MALVRKRRQI NLRLPVPPLS VHLPWFSFAS STAPVINNGI SASDVEKLHV LGRGSSGIVY
KVHHKTTGEI YALKSVNGDM SPAFTRQLAR EMEILRRTDS PYVVRCQGIF EKPIVGEVSI
LMEYMDGGNL ESLRGAVTEK QLAGFSRQIL KGLSYLHSLK IVHRDIKPAN LLLNSRNEVK
IADFGVSKII TRSLDYCNSY VGTCAYMSPE RFDSAAGENS DVYAGDIWSF GVMILELFVG
HFPLLPQGQR PDWATLMCVV CFGEPPRAPE GCSDEFRSFV DCCLRKESSE RWTASQLLGH
PFLRESL
