ID MPK6_ARATH Reviewed; 395 AA.
AC Q39026;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 13-JUL-2010, entry version 100.
DE RecName: Full=Mitogen-activated protein kinase 6;
DE Short=MAP kinase 6;
DE Short=AtMPK6;
DE EC=2.7.11.24;
GN Name=MPK6; OrderedLocusNames=At2g43790; ORFNames=F18O19.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; malvids; Brassicales; Brassicaceae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX MEDLINE=94109583; PubMed=8282107; DOI=10.1016/0014-5793(93)80852-L;
RA Mizoguchi T., Hayashida N., Yamaguchi-Shinozaki K., Kamada H.,
RA Shinozaki K.;
RT "ATMPKs: a gene family of plant MAP kinases in Arabidopsis thaliana.";
RL FEBS Lett. 336:440-444(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP ENZYME REGULATION, AND PHOSPHORYLATION.
RX PubMed=10713056; DOI=10.1074/jbc.275.11.7521;
RA Nuehse T.S., Peck S.C., Hirt H., Boller T.;
RT "Microbial elicitors induce activation and dual phosphorylation of the
RT Arabidopsis thaliana MAPK 6.";
RL J. Biol. Chem. 275:7521-7526(2000).
RN [5]
RP ENZYME REGULATION, AND PHOSPHORYLATION.
RX PubMed=11123804; DOI=10.1046/j.1365-313x.2000.00913.x;
RA Ichimura K., Mizoguchi T., Yoshida R., Yuasa T., Shinozaki K.;
RT "Various abiotic stresses rapidly activate Arabidopsis MAP kinases
RT ATMPK4 and ATMPK6.";
RL Plant J. 24:655-665(2000).
RN [6]
RP ENZYME REGULATION.
RX PubMed=10717008; DOI=10.1073/pnas.97.6.2940;
RA Kovtun Y., Chiu W.-L., Tena G., Sheen J.;
RT "Functional analysis of oxidative stress-activated mitogen-activated
RT protein kinase cascade in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2940-2945(2000).
RN [7]
RP ENZYME REGULATION.
RX PubMed=11577197; DOI=10.1093/pcp/pce123;
RA Yuasa T., Ichimura K., Mizoguchi T., Shinozaki K.;
RT "Oxidative stress activates ATMPK6, an Arabidopsis homologue of MAP
RT kinase.";
RL Plant Cell Physiol. 42:1012-1016(2001).
RN [8]
RP ENZYME REGULATION.
RX PubMed=11500556; DOI=10.1104/pp.126.4.1579;
RA Desikan R., Hancock J.T., Ichimura K., Shinozaki K., Neill S.J.;
RT "Harpin induces activation of the Arabidopsis mitogen-activated
RT protein kinases AtMPK4 and AtMPK6.";
RL Plant Physiol. 126:1579-1587(2001).
RN [9]
RP ENZYME REGULATION.
RX PubMed=12220631; DOI=10.1016/S0014-5793(02)03162-9;
RA Droillard M.-J., Boudsocq M., Barbier-Brygoo H., Lauriere C.;
RT "Different protein kinase families are activated by osmotic stresses
RT in Arabidopsis thaliana cell suspensions. Involvement of the MAP
RT kinases AtMPK3 and AtMPK6.";
RL FEBS Lett. 527:43-50(2002).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF LYS-92 AND LYS-93.
RX MEDLINE=21864699; PubMed=11875555; DOI=10.1038/415977a;
RA Asai T., Tena G., Plotnikova J., Willmann M.R., Chiu W.-L.,
RA Gomez-Gomez L., Boller T., Ausubel F.M., Sheen J.;
RT "MAP kinase signalling cascade in Arabidopsis innate immunity.";
RL Nature 415:977-983(2002).
RN [11]
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 [12]
RP ENZYME REGULATION.
RX PubMed=12628921; DOI=10.1093/emboj/cdg131;
RA Ouaked F., Rozhon W., Lecourieux D., Hirt H.;
RT "A MAPK pathway mediates ethylene signaling in plants.";
RL EMBO J. 22:1282-1288(2003).
RN [13]
RP INTERACTION WITH NDPK2.
RX PubMed=12506203; DOI=10.1073/pnas.252641899;
RA Moon H., Lee B., Choi G., Shin D., Prasad D.T., Lee O., Kwak S.-S.,
RA Kim D.H., Nam J., Bahk J., Hong J.C., Lee S.Y., Cho M.J., Lim C.O.,
RA Yun D.-J.;
RT "NDP kinase 2 interacts with two oxidative stress-activated MAPKs to
RT regulate cellular redox state and enhances multiple stress tolerance
RT in transgenic plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:358-363(2003).
RN [14]
RP FUNCTION, ENZYME REGULATION, AND INTERACTION WITH MKK2.
RX PubMed=15225555; DOI=10.1016/j.molcel.2004.06.023;
RA Teige M., Scheikl E., Eulgem T., Doczi R., Ichimura K., Shinozaki K.,
RA Dangl J.L., Hirt H.;
RT "The MKK2 pathway mediates cold and salt stress signaling in
RT Arabidopsis.";
RL Mol. Cell 15:141-152(2004).
RN [15]
RP FUNCTION.
RX PubMed=15020743; DOI=10.1105/tpc.015552;
RA Menke F.L.H., van Pelt J.A., Pieterse C.M.J., Klessig D.F.;
RT "Silencing of the mitogen-activated protein kinase MPK6 compromises
RT disease resistance in Arabidopsis.";
RL Plant Cell 16:897-907(2004).
RN [16]
RP FUNCTION.
RX PubMed=15539472; DOI=10.1105/tpc.104.026609;
RA Liu Y., Zhang S.;
RT "Phosphorylation of 1-aminocyclopropane-1-carboxylic acid synthase by
RT MPK6, a stress-responsive mitogen-activated protein kinase, induces
RT ethylene biosynthesis in Arabidopsis.";
RL Plant Cell 16:3386-3399(2004).
RN [17]
RP ENZYME REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=15500467; DOI=10.1111/j.1365-313X.2004.02229.x;
RA Ahlfors R., Macioszek V., Rudd J., Brosche M., Schlichting R.,
RA Scheel D., Kangasjarvi J.;
RT "Stress hormone-independent activation and nuclear translocation of
RT mitogen-activated protein kinases in Arabidopsis thaliana during ozone
RT exposure.";
RL Plant J. 40:512-522(2004).
RN [18]
RP ENZYME REGULATION.
RX PubMed=15084727; DOI=10.1104/pp.103.037275;
RA Miles G.P., Samuel M.A., Jones A.M., Ellis B.E.;
RT "Mastoparan rapidly activates plant MAP kinase signaling independent
RT of heterotrimeric G proteins.";
RL Plant Physiol. 134:1332-1336(2004).
RN [19]
RP FUNCTION.
RX PubMed=15964670; DOI=10.1016/j.envpol.2005.04.017;
RA Miles G.P., Samuel M.A., Zhang Y., Ellis B.E.;
RT "RNA interference-based (RNAi) suppression of AtMPK6, an Arabidopsis
RT mitogen-activated protein kinase, results in hypersensitivity to ozone
RT and misregulation of AtMPK3.";
RL Environ. Pollut. 138:230-237(2005).
RN [20]
RP ENZYME REGULATION, AND INTERACTION WITH AP2C1.
RX PubMed=17630279; DOI=10.1105/tpc.106.049585;
RA Schweighofer A., Kazanaviciute V., Scheikl E., Teige M., Doczi R.,
RA Hirt H., Schwanninger M., Kant M., Schuurink R., Mauch F., Buchala A.,
RA Cardinale F., Meskiene I.;
RT "The PP2C-type phosphatase AP2C1, which negatively regulates MPK4 and
RT MPK6, modulates innate immunity, jasmonic acid, and ethylene levels in
RT Arabidopsis.";
RL Plant Cell 19:2213-2224(2007).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, SUBCELLULAR
RP LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
RA Andreasson E., Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from
RT Arabidopsis thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: Involved in oxidative stress-mediated signaling cascade
CC (such as ozone). Involved in the innate immune MAP kinase
CC signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6) downstream of
CC bacterial flagellin receptor FLS2. May be involved in
CC hypersensitive response (HR)-mediated signaling cascade. May
CC phosphorylate regulators of WRKY transcription factors.
CC Phosphorylates 1-aminocyclopropane-1-carboxylic acid synthases
CC (ACS2 and ACS6) and may be involved in the regulation of bacterial
CC elicitor flagellin-induced ethylene production. Regulates locally
CC gene-mediated and basal resitance response to certain pathogens.
CC May be involved in the cold and salinity stress-mediated MAP
CC kinase signaling cascade (MEKK1, MEK1/MKK2 and MPK4/MPK6).
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- ENZYME REGULATION: Activated by threonine and tyrosine
CC phosphorylation. Activated by the MAP kinase kinases MKK2, MKK4
CC and MKK5. Activated in response to touch, wounding, low
CC temperature, low humidity, salt stress, hydrogen peroxide, ozone,
CC ACC (an ethylene precursor), mastoparan and UVC. Activated in
CC response to elicitors: oligogalacturonides, hexameric chitin
CC fragments, fungal xylanase, and the bacterial flagellin and
CC harpin. Repressed by the protein phosphatase 2C AP2C1.
CC -!- SUBUNIT: Interacts with MEKK1, MEK1 and MKK2. May form a ternary
CC complex with MEKK1 and MEK1 or MKK2. Interacts with NDPK2 and
CC AP2C1.
CC -!- INTERACTION:
CC Q9FX43:At1g73500/T9L24_8; NbExp=1; IntAct=EBI-349548, EBI-2128545;
CC Q9FKG1:ERF104; NbExp=3; IntAct=EBI-349548, EBI-2360943;
CC Q9S7U9:MKK2; NbExp=4; IntAct=EBI-349548, EBI-994350;
CC O22921:WRKY25; NbExp=1; IntAct=EBI-349548, EBI-1392386;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into
CC the nucleus in response to phosphorylation (Probable).
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-221 and Tyr-223, which activates
CC the enzyme.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC Ser/Thr protein kinase family. MAP kinase subfamily.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
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DR EMBL; D21842; BAA04869.1; -; mRNA.
DR EMBL; AC002333; AAB64027.1; -; Genomic_DNA.
DR EMBL; AY120737; AAM53295.1; -; mRNA.
DR EMBL; BT008855; AAP68294.1; -; mRNA.
DR IPI; IPI00530555; -.
DR PIR; S40472; S40472.
DR RefSeq; NP_181907.1; -.
DR UniGene; At.22266; -.
DR UniGene; At.53112; -.
DR UniGene; Rra.4023; -.
DR UniGene; Rra.9788; -.
DR UniGene; Rsa.2538; -.
DR SMR; Q39026; 52-395.
DR IntAct; Q39026; 8.
DR STRING; Q39026; -.
DR PRIDE; Q39026; -.
DR EnsemblPlants; AT2G43790.1-TAIR; AT2G43790.1-P; AT2G43790-TAIR-G.
DR GeneID; 818982; -.
DR GenomeReviews; CT485783_GR; AT2G43790.
DR KEGG; ath:AT2G43790; -.
DR NMPDR; fig|3702.1.peg.11540; -.
DR GeneFarm; 821; 89.
DR TAIR; At2g43790; -.
DR eggNOG; KOG0660; -.
DR HOGENOM; HBG755340; -.
DR InParanoid; Q39026; -.
DR OMA; NENARRY; -.
DR PhylomeDB; Q39026; -.
DR BRENDA; 2.7.11.24; 302.
DR ArrayExpress; Q39026; -.
DR Genevestigator; Q39026; -.
DR GermOnline; AT2G43790; Arabidopsis thaliana.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IDA:TAIR.
DR GO; GO:0005515; F:protein binding; IPI:IntAct.
DR GO; GO:0010120; P:camalexin biosynthetic process; IMP:TAIR.
DR GO; GO:0009864; P:induced systemic resistance, jasmonic acid ...; IMP:TAIR.
DR GO; GO:0048481; P:ovule development; IGI:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0080136; P:priming of cellular response to stress; IMP:TAIR.
DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
DR GO; GO:0009737; P:response to abscisic acid stimulus; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IDA:TAIR.
DR GO; GO:0009723; P:response to ethylene stimulus; IDA:TAIR.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:TAIR.
DR GO; GO:0009651; P:response to salt stress; IGI:TAIR.
DR InterPro; IPR008351; JNK_MAPK.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR000719; Prot_kinase_cat_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01772; JNKMAPKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Kinase_like; 1.
DR PROSITE; PS01351; MAPK; 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; Complete proteome; Cytoplasm; Hypersensitive response;
KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Plant defense;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1 395 Mitogen-activated protein kinase 6.
FT /FTId=PRO_0000186315.
FT DOMAIN 63 348 Protein kinase.
FT NP_BIND 69 77 ATP (By similarity).
FT MOTIF 221 223 TXY.
FT ACT_SITE 189 189 Proton acceptor (By similarity).
FT BINDING 92 92 ATP.
FT MOD_RES 221 221 Phosphothreonine.
FT MOD_RES 223 223 Phosphotyrosine.
FT MUTAGEN 92 92 K->M: Loss of kinase activity.
FT MUTAGEN 93 93 K->M: Loss of kinase activity.
SQ SEQUENCE 395 AA; 45058 MW; 296D2BD753C6DDA4 CRC64;
MDGGSGQPAA DTEMTEAPGG FPAAAPSPQM PGIENIPATL SHGGRFIQYN IFGNIFEVTA
KYKPPIMPIG KGAYGIVCSA MNSETNESVA IKKIANAFDN KIDAKRTLRE IKLLRHMDHE
NIVAIRDIIP PPLRNAFNDV YIAYELMDTD LHQIIRSNQA LSEEHCQYFL YQILRGLKYI
HSANVLHRDL KPSNLLLNAN CDLKICDFGL ARVTSESDFM TEYVVTRWYR APELLLNSSD
YTAAIDVWSV GCIFMELMDR KPLFPGRDHV HQLRLLMELI GTPSEEELEF LNENAKRYIR
QLPPYPRQSI TDKFPTVHPL AIDLIEKMLT FDPRRRITVL DALAHPYLNS LHDISDEPEC
TIPFNFDFEN HALSEEQMKE LIYREALAFN PEYQQ
//