(data stored in ACNUC8465 zone)

SWISSPROT: M2K3_ARATH

ID   M2K3_ARATH              Reviewed;         520 AA.
AC   O80396;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   11-DEC-2019, entry version 156.
DE   RecName: Full=Mitogen-activated protein kinase kinase 3;
DE            Short=AtMKK3;
DE            Short=MAP kinase kinase 3;
DE            EC=2.7.12.2;
GN   Name=MKK3; OrderedLocusNames=At5g40440; ORFNames=MPO12.19, MPO12_150;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA   Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT   features of the regions of 1,044,062 bp covered by thirteen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:291-300(1997).
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=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   [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   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, MUTAGENESIS OF SER-235 AND THR-241, AND PHOSPHORYLATION AT
RP   SER-235 AND THR-241.
RX   PubMed=17369371; DOI=10.1105/tpc.106.046581;
RA   Takahashi F., Yoshida R., Ichimura K., Mizoguchi T., Seo S., Yonezawa M.,
RA   Maruyama K., Yamaguchi-Shinozaki K., Shinozaki K.;
RT   "The mitogen-activated protein kinase cascade MKK3-MPK6 is an important
RT   part of the jasmonate signal transduction pathway in Arabidopsis.";
RL   Plant Cell 19:805-818(2007).
RN   [9]
RP   DISRUPTION PHENOTYPE, FUNCTION, INDUCTION BY PATHOGEN, MUTAGENESIS OF
RP   SER-235 AND THR-241, INTERACTION WITH MPK1; MPK2 AND MPK7, AND
RP   PHOSPHORYLATION AT SER-235 AND THR-241.
RX   PubMed=17933903; DOI=10.1105/tpc.106.050039;
RA   Doczi R., Brader G., Pettko-Szandtner A., Rajh I., Djamei A., Pitzschke A.,
RA   Teige M., Hirt H.;
RT   "The Arabidopsis mitogen-activated protein kinase kinase MKK3 is upstream
RT   of group C mitogen-activated protein kinases and participates in pathogen
RT   signaling.";
RL   Plant Cell 19:3266-3279(2007).
RN   [10]
RP   INTERACTION WITH MPK1; MPK2; MPK7 AND MPK14.
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   [11]
RP   INTERACTION WITH HOPF2.
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   [12]
RP   FUNCTION, MUTAGENESIS OF SER-235 AND THR-241, TISSUE SPECIFICITY, AND
RP   PHOSPHORYLATION AT SER-235 AND THR-241.
RX   PubMed=21419340; DOI=10.1016/j.molcel.2011.02.029;
RA   Takahashi F., Mizoguchi T., Yoshida R., Ichimura K., Shinozaki K.;
RT   "Calmodulin-dependent activation of MAP kinase for ROS homeostasis in
RT   Arabidopsis.";
RL   Mol. Cell 41:649-660(2011).
RN   [13]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH MAPKKK17 AND MAPKKK18.
RC   STRAIN=cv. Columbia;
RX   PubMed=25720833; DOI=10.1111/tpj.12808;
RA   Danquah A., de Zelicourt A., Boudsocq M., Neubauer J., Frei Dit Frey N.,
RA   Leonhardt N., Pateyron S., Gwinner F., Tamby J.P., Ortiz-Masia D.,
RA   Marcote M.J., Hirt H., Colcombet J.;
RT   "Identification and characterization of an ABA-activated MAP kinase cascade
RT   in Arabidopsis thaliana.";
RL   Plant J. 82:232-244(2015).
RN   [14]
RP   INTERACTION WITH MAPKKK17; MPK1; MPK2 AND MPK7.
RC   STRAIN=cv. Columbia;
RX   PubMed=25680457; DOI=10.1007/s11103-015-0295-0;
RA   Matsuoka D., Yasufuku T., Furuya T., Nanmori T.;
RT   "An abscisic acid inducible Arabidopsis MAPKKK, MAPKKK18 regulates leaf
RT   senescence via its kinase activity.";
RL   Plant Mol. Biol. 87:565-575(2015).
CC   -!- FUNCTION: MKK3-MPK6 module plays an important role in the jasmonate
CC       signal transduction pathway through the negative regulation of
CC       MYC2/JIN1 expression. Activates by phosphorylation the downstream MPK6,
CC       MPK7 and MPK8. MKK3-MPK7 module acts as a positive regulator of PR1
CC       gene expression. MKK3-MPK8 module negatively regulates ROS accumulation
CC       through controlling expression of the RBOHD gene. Component of the
CC       abscisic acid (ABA) signaling pathway that may act as ABA signal
CC       transducer in the context of abiotic stresses. Activator of the C group
CC       MAP kinases. Activates MPK7 in response to ABA (PubMed:25720833).
CC       {ECO:0000269|PubMed:17369371, ECO:0000269|PubMed:17933903,
CC       ECO:0000269|PubMed:21419340, ECO:0000269|PubMed:25720833}.
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 MPK1, MPK2 and MPK7 (PubMed:17933903,
CC       PubMed:19513235, PubMed:25680457). Interacts with P.syringae type III
CC       effector HopF2 (PubMed:20571112). Interacts with MPK14
CC       (PubMed:19513235). Binds to MAPKKK17 and MAPKKK18 (PubMed:25720833,
CC       PubMed:25680457). {ECO:0000269|PubMed:17933903,
CC       ECO:0000269|PubMed:19513235, ECO:0000269|PubMed:20571112,
CC       ECO:0000269|PubMed:25680457, ECO:0000269|PubMed:25720833}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10048483,
CC       ECO:0000269|PubMed:21419340}.
CC   -!- INDUCTION: By Pseudomonas syringae pv tomato strain DC3000 infection.
CC       {ECO:0000269|PubMed:17933903}.
CC   -!- PTM: Phosphorylation at Ser-235 and Thr-241 by MAP kinase kinase
CC       kinases positively regulates kinase activity.
CC       {ECO:0000305|PubMed:17369371, ECO:0000305|PubMed:17933903,
CC       ECO:0000305|PubMed:21419340}.
CC   -!- DISRUPTION PHENOTYPE: More sensitive to Pseudomonas syringae pv. tomato
CC       DC3000 infection. Hypersensitivity to abscisic acid (ABA) in
CC       germination and root elongation (PubMed:25720833).
CC       {ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:25720833}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
DR   EMBL; AB015314; BAA28829.1; -; mRNA.
DR   EMBL; AB006702; BAB11601.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94548.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70658.1; -; Genomic_DNA.
DR   EMBL; AK117136; BAC41814.1; -; mRNA.
DR   EMBL; BT006481; AAP21289.1; -; mRNA.
DR   PIR; T51338; T51338.
DR   RefSeq; NP_001318713.1; NM_001344328.1.
DR   RefSeq; NP_198860.1; NM_123408.3.
DR   SMR; O80396; -.
DR   BioGrid; 19293; 7.
DR   IntAct; O80396; 5.
DR   STRING; 3702.AT5G40440.1; -.
DR   iPTMnet; O80396; -.
DR   PaxDb; O80396; -.
DR   PRIDE; O80396; -.
DR   EnsemblPlants; AT5G40440.1; AT5G40440.1; AT5G40440.
DR   EnsemblPlants; AT5G40440.4; AT5G40440.4; AT5G40440.
DR   GeneID; 834042; -.
DR   Gramene; AT5G40440.1; AT5G40440.1; AT5G40440.
DR   Gramene; AT5G40440.4; AT5G40440.4; AT5G40440.
DR   KEGG; ath:AT5G40440; -.
DR   Araport; AT5G40440; -.
DR   TAIR; locus:2170578; AT5G40440.
DR   eggNOG; KOG0581; Eukaryota.
DR   eggNOG; ENOG410XQ5A; LUCA.
DR   HOGENOM; HOG000234206; -.
DR   InParanoid; O80396; -.
DR   KO; K20607; -.
DR   OrthoDB; 688282at2759; -.
DR   PhylomeDB; O80396; -.
DR   PRO; PR:O80396; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; O80396; baseline and differential.
DR   Genevisible; O80396; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IDA:TAIR.
DR   GO; GO:0004708; F:MAP kinase kinase activity; IDA:TAIR.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0000187; P:activation of MAPK activity; IBA:GO_Central.
DR   GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR   GO; GO:0009814; P:defense response, incompatible interaction; IMP:TAIR.
DR   GO; GO:0009866; P:induced systemic resistance, ethylene mediated signaling pathway; IEP:TAIR.
DR   GO; GO:0009864; P:induced systemic resistance, jasmonic acid mediated signaling pathway; IEP:TAIR.
DR   GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR   GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
DR   CDD; cd00780; NTF2; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR018222; Nuclear_transport_factor_2_euk.
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; SSF54427; SSF54427; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50177; NTF2_DOMAIN; 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;
DR   PRODOM; O80396.
DR   SWISS-2DPAGE; O80396.
KW   Abscisic acid signaling pathway; ATP-binding; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Plant defense; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..520
FT                   /note="Mitogen-activated protein kinase kinase 3"
FT                   /id="PRO_0000428622"
FT   DOMAIN          83..339
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          366..516
FT                   /note="NTF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT   NP_BIND         89..97
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   COMPBIAS        22..26
FT                   /note="Poly-Ser"
FT   ACT_SITE        207
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         112
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9S7U9"
FT   MOD_RES         235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:17369371,
FT                   ECO:0000305|PubMed:17933903, ECO:0000305|PubMed:21419340"
FT   MOD_RES         241
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000305|PubMed:17369371,
FT                   ECO:0000305|PubMed:17933903, ECO:0000305|PubMed:21419340"
FT   MOD_RES         245
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O80397"
FT   MUTAGEN         235
FT                   /note="S->D: Constitutively active; when associated with D-
FT                   241."
FT                   /evidence="ECO:0000269|PubMed:17369371,
FT                   ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:21419340"
FT   MUTAGEN         235
FT                   /note="S->E: Constitutively active; when associated with E-
FT                   241."
FT                   /evidence="ECO:0000269|PubMed:17369371,
FT                   ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:21419340"
FT   MUTAGEN         241
FT                   /note="T->D: Constitutively active; when associated with D-
FT                   235."
FT                   /evidence="ECO:0000269|PubMed:17369371,
FT                   ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:21419340"
FT   MUTAGEN         241
FT                   /note="T->E: Constitutively active; when associated with E-
FT                   235."
FT                   /evidence="ECO:0000269|PubMed:17369371,
FT                   ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:21419340"
SQ   SEQUENCE   520 AA;  57529 MW;  9CD63397CCF38AA2 CRC64;
     MAALEELKKK LSPLFDAEKG FSSSSSLDPN DSYLLSDGGT VNLLSRSYGV YNFNELGLQK
     CTSSHVDESE SSETTYQCAS HEMRVFGAIG SGASSVVQRA IHIPNHRILA LKKINIFERE
     KRQQLLTEIR TLCEAPCHEG LVDFHGAFYS PDSGQISIAL EYMNGGSLAD ILKVTKKIPE
     PVLSSLFHKL LQGLSYLHGV RHLVHRDIKP ANLLINLKGE PKITDFGISA GLENSMAMCA
     TFVGTVTYMS PERIRNDSYS YPADIWSLGL ALFECGTGEF PYIANEGPVN LMLQILDDPS
     PTPPKQEFSP EFCSFIDACL QKDPDARPTA DQLLSHPFIT KHEKERVDLA TFVQSIFDPT
     QRLKDLADML TIHYYSLFDG FDDLWHHAKS LYTETSVFSF SGKHNTGSTE IFSALSDIRN
     TLTGDLPSEK LVHVVEKLHC KPCGSGGVII RAVGSFIVGN QFLICGDGVQ AEGLPSFKDL
     GFDVASRRVG RFQEQFVVES GDLIGKYFLA KQELYITNLD
//

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