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 27-MAR-2024, entry version 203. DE RecName: Full=Mitogen-activated protein kinase 6 {ECO:0000303|PubMed:8282107}; DE Short=AtMPK6 {ECO:0000303|PubMed:8282107}; DE Short=MAP kinase 6 {ECO:0000303|PubMed:8282107}; DE EC=2.7.11.24 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:10713056, ECO:0000269|PubMed:10717008, ECO:0000269|PubMed:11123804}; GN Name=MPK6 {ECO:0000303|PubMed:8282107}; GN OrderedLocusNames=At2g43790 {ECO:0000312|Araport:AT2G43790}; GN ORFNames=F18O19.10 {ECO:0000312|EMBL:AAB64027.1}; 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]. RC STRAIN=cv. Columbia; RX 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 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., Moffat K.S., RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; RL Nature 402:761-768(1999). 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=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 ACTIVITY REGULATION, PHOSPHORYLATION AT THR-221 AND TYR-223, AND CATALYTIC RP ACTIVITY. 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 [6] RP ACTIVITY REGULATION, PHOSPHORYLATION, AND CATALYTIC ACTIVITY. 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 ATMPK4 RT and ATMPK6."; RL Plant J. 24:655-665(2000). RN [7] RP ACTIVITY REGULATION, AND CATALYTIC ACTIVITY. 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 [8] RP ACTIVITY REGULATION, AND CATALYTIC ACTIVITY. 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 [9] RP ACTIVITY REGULATION, AND CATALYTIC ACTIVITY. 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 protein RT kinases AtMPK4 and AtMPK6."; RL Plant Physiol. 126:1579-1587(2001). RN [10] RP ACTIVITY REGULATION, AND CATALYTIC ACTIVITY. 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 in RT Arabidopsis thaliana cell suspensions. Involvement of the MAP kinases RT AtMPK3 and AtMPK6."; RL FEBS Lett. 527:43-50(2002). RN [11] RP FUNCTION, AND MUTAGENESIS OF LYS-92 AND LYS-93. RX PubMed=11875555; DOI=10.1038/415977a; RA Asai T., Tena G., Plotnikova J., Willmann M.R., Chiu W.-L., Gomez-Gomez L., RA Boller T., Ausubel F.M., Sheen J.; RT "MAP kinase signalling cascade in Arabidopsis innate immunity."; RL Nature 415:977-983(2002). RN [12] 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 [13] RP ACTIVITY REGULATION, AND CATALYTIC ACTIVITY. 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 [14] 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 in RT transgenic plants."; RL Proc. Natl. Acad. Sci. U.S.A. 100:358-363(2003). RN [15] RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH MKK2, AND CATALYTIC RP ACTIVITY. 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 Arabidopsis."; RL Mol. Cell 15:141-152(2004). RN [16] 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 disease RT resistance in Arabidopsis."; RL Plant Cell 16:897-907(2004). RN [17] 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 MPK6, RT a stress-responsive mitogen-activated protein kinase, induces ethylene RT biosynthesis in Arabidopsis."; RL Plant Cell 16:3386-3399(2004). RN [18] RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY. RX PubMed=15500467; DOI=10.1111/j.1365-313x.2004.02229.x; RA Ahlfors R., Macioszek V., Rudd J., Brosche M., Schlichting R., Scheel D., RA 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 [19] RP ACTIVITY 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 of RT heterotrimeric G proteins."; RL Plant Physiol. 134:1332-1336(2004). RN [20] 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 and RT misregulation of AtMPK3."; RL Environ. Pollut. 138:230-237(2005). RN [21] 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 [22] RP ACTIVITY REGULATION, AND DEPHOSPHORYLATION. RX PubMed=17586809; DOI=10.1074/jbc.m701888200; RA Lee J.S., Ellis B.E.; RT "Arabidopsis MAPK phosphatase 2 (MKP2) positively regulates oxidative RT stress tolerance and inactivates the MPK3 and MPK6 MAPKs."; RL J. Biol. Chem. 282:25020-25029(2007). RN [23] RP ACTIVITY REGULATION. RX PubMed=17506336; DOI=10.1094/mpmi-20-5-0589; RA Brader G., Djamei A., Teige M., Palva E.T., Hirt H.; RT "The MAP kinase kinase MKK2 affects disease resistance in Arabidopsis."; RL Mol. Plant Microbe Interact. 20:589-596(2007). RN [24] RP FUNCTION. RX PubMed=17259259; DOI=10.1105/tpc.106.048298; RA Wang H., Ngwenyama N., Liu Y., Walker J.C., Zhang S.; RT "Stomatal development and patterning are regulated by environmentally RT responsive mitogen-activated protein kinases in Arabidopsis."; RL Plant Cell 19:63-73(2007). RN [25] RP ACTIVITY REGULATION, AND FUNCTION. 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 [26] RP ACTIVITY 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., Hirt H., RA Schwanninger M., Kant M., Schuurink R., Mauch F., Buchala A., Cardinale F., RA Meskiene I.; RT "The PP2C-type phosphatase AP2C1, which negatively regulates MPK4 and MPK6, RT modulates innate immunity, jasmonic acid, and ethylene levels in RT Arabidopsis."; RL Plant Cell 19:2213-2224(2007). RN [27] RP ACTIVITY REGULATION. 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 [28] RP FUNCTION, ACTIVITY REGULATION, 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 [29] RP FUNCTION. RX PubMed=18248592; DOI=10.1111/j.1365-313x.2008.03433.x; RA Xing Y., Jia W., Zhang J.; RT "AtMKK1 mediates ABA-induced CAT1 expression and H2O2 production via RT AtMPK6-coupled signaling in Arabidopsis."; RL Plant J. 54:440-451(2008). RN [30] RP INTERACTION WITH MKK2; MKK4; MKK5 AND MKK6. 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 [31] RP FUNCTION. RX PubMed=18378893; DOI=10.1073/pnas.0711301105; RA Ren D., Liu Y., Yang K.Y., Han L., Mao G., Glazebrook J., Zhang S.; RT "A fungal-responsive MAPK cascade regulates phytoalexin biosynthesis in RT Arabidopsis."; RL Proc. Natl. Acad. Sci. U.S.A. 105:5638-5643(2008). RN [32] RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-226, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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., Andreasson E., RA Rathjen J.P., Peck S.C.; RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis RT thaliana."; RL J. Proteomics 72:439-451(2009). RN [33] RP ACTIVITY REGULATION, DEPHOSPHORYLATION, AND INTERACTION WITH MKP1 AND PTP1. RX PubMed=19789277; DOI=10.1105/tpc.109.067678; RA Bartels S., Anderson J.C., Gonzalez Besteiro M.A., Carreri A., Hirt H., RA Buchala A., Metraux J.P., Peck S.C., Ulm R.; RT "MAP kinase phosphatase1 and protein tyrosine phosphatase1 are repressors RT of salicylic acid synthesis and SNC1-mediated responses in Arabidopsis."; RL Plant Cell 21:2884-2897(2009). RN [34] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=19484493; DOI=10.1007/s11103-009-9503-0; RA Xing Y., Jia W., Zhang J.; RT "AtMKK1 and AtMPK6 are involved in abscisic acid and sugar signaling in RT Arabidopsis seed germination."; RL Plant Mol. Biol. 70:725-736(2009). RN [35] RP FUNCTION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE. 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 [36] RP INTERACTION WITH DSPTP1B/MKP2. RX PubMed=20626661; DOI=10.1111/j.1365-313x.2010.04297.x; RA Lumbreras V., Vilela B., Irar S., Sole M., Capellades M., Valls M., RA Coca M., Pages M.; RT "MAPK phosphatase MKP2 mediates disease responses in Arabidopsis and RT functionally interacts with MPK3 and MPK6."; RL Plant J. 63:1017-1030(2010). RN [37] RP INTERACTION WITH DSPTP1B/MKP2. RX PubMed=21057191; DOI=10.4161/psb.5.11.13645; RA Vilela B., Pages M., Lumbreras V.; RT "Regulation of MAPK signaling and cell death by MAPK phosphatase MKP2."; RL Plant Signal. Behav. 5:1497-1500(2010). RN [38] RP INTERACTION WITH MKK6. RX PubMed=21575092; DOI=10.1111/j.1365-313x.2011.04642.x; RA Zeng Q., Chen J.G., Ellis B.E.; RT "AtMPK4 is required for male-specific meiotic cytokinesis in Arabidopsis."; RL Plant J. 67:895-906(2011). RN [39] 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). RN [40] RP FUNCTION. RX PubMed=23263767; DOI=10.1105/tpc.112.104695; RA Meng X., Wang H., He Y., Liu Y., Walker J.C., Torii K.U., Zhang S.; RT "A MAPK cascade downstream of ERECTA receptor-like protein kinase regulates RT Arabidopsis inflorescence architecture by promoting localized cell RT proliferation."; RL Plant Cell 24:4948-4960(2012). RN [41] RP ACTIVITY REGULATION. RC STRAIN=cv. Columbia; RX PubMed=21969089; DOI=10.1007/s00299-011-1157-0; RA Kim J.-M., Woo D.-H., Kim S.-H., Lee S.-Y., Park H.-Y., Seok H.-Y., RA Chung W.S., Moon Y.-H.; RT "Arabidopsis MKKK20 is involved in osmotic stress response via regulation RT of MPK6 activity."; RL Plant Cell Rep. 31:217-224(2012). RN [42] RP INTERACTION WITH VQ4 AND IKU1/VQ14. RX PubMed=24750137; DOI=10.1111/nph.12817; RA Pecher P., Eschen-Lippold L., Herklotz S., Kuhle K., Naumann K., Bethke G., RA Uhrig J., Weyhe M., Scheel D., Lee J.; RT "The Arabidopsis thaliana mitogen-activated protein kinases MPK3 and MPK6 RT target a subclass of 'VQ-motif'-containing proteins to regulate immune RT responses."; RL New Phytol. 203:592-606(2014). RN [43] RP FUNCTION, AND INTERACTION WITH LIP5. RC STRAIN=cv. Columbia; RX PubMed=25010425; DOI=10.1371/journal.ppat.1004243; RA Wang F., Shang Y., Fan B., Yu J.-Q., Chen Z.; RT "Arabidopsis LIP5, a positive regulator of multivesicular body biogenesis, RT is a critical target of pathogen-responsive MAPK cascade in plant basal RT defense."; RL PLoS Pathog. 10:E1004243-E1004243(2014). RN [44] RP FUNCTION, INTERACTION WITH BASL AND YDA, AND SUBCELLULAR LOCATION. RC STRAIN=cv. Columbia; RX PubMed=25843888; DOI=10.1016/j.devcel.2015.02.022; RA Zhang Y., Wang P., Shao W., Zhu J.-K., Dong J.; RT "The BASL polarity protein controls a MAPK signaling feedback loop in RT asymmetric cell division."; RL Dev. Cell 33:136-149(2015). RN [45] RP INTERACTION WITH RACK1A; RACK1B AND RACK1C. RX PubMed=25731164; DOI=10.1038/nature14243; RA Cheng Z., Li J.F., Niu Y., Zhang X.C., Woody O.Z., Xiong Y., Djonovic S., RA Millet Y., Bush J., McConkey B.J., Sheen J., Ausubel F.M.; RT "Pathogen-secreted proteases activate a novel plant immune pathway."; RL Nature 521:213-216(2015). RN [46] RP DEVELOPMENTAL STAGE, MUTAGENESIS OF 221-THR--TYR-223, SUBCELLULAR LOCATION, RP AND ACTIVITY REGULATION. RC STRAIN=cv. Columbia; RX PubMed=27746029; DOI=10.1016/j.cub.2016.08.066; RA Zhang Y., Guo X., Dong J.; RT "Phosphorylation of the polarity protein BASL differentiates asymmetric RT cell fate through MAPKs and SPCH."; RL Curr. Biol. 26:2957-2965(2016). RN [47] RP INTERACTION WITH PTP1. RX PubMed=27029354; DOI=10.1093/jxb/erw107; RA Cho H.Y., Wen T.N., Wang Y.T., Shih M.C.; RT "Quantitative phosphoproteomics of protein kinase SnRK1 regulated protein RT phosphorylation in Arabidopsis under submergence."; RL J. Exp. Bot. 67:2745-2760(2016). RN [48] RP INTERACTION WITH FLZ9. RX DOI=10.1016/j.cpb.2015.10.004; RA Nietzsche M., Landgraf R., Tohge T., Boernke F.; RT "A protein-protein interaction network linking the energy-sensor kinase RT SnRK1 to multiple signaling pathways in Arabidopsis thaliana."; RL Curr. Plant Biol. 5:36-44(2016). RN [49] RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MKK5, AND ACTIVITY RP REGULATION. RC STRAIN=cv. Columbia; RX PubMed=27913741; DOI=10.1104/pp.16.01386; RA Li K., Yang F., Zhang G., Song S., Li Y., Ren D., Miao Y., Song C.-P.; RT "AIK1, a mitogen-activated protein kinase, modulates abscisic acid RT responses through the MKK5-MPK6 kinase cascade."; RL Plant Physiol. 173:1391-1408(2017). RN [50] RP REVIEW ON MITOGEN-ACTIVATED PROTEIN KINASE CASCADES. RX PubMed=30349547; DOI=10.3389/fpls.2018.01387; RA Jagodzik P., Tajdel-Zielinska M., Ciesla A., Marczak M., Ludwikow A.; RT "Mitogen-activated protein kinase cascades in plant hormone signaling."; RL Front. Plant Sci. 9:1387-1387(2018). RN [51] RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 29-395, AND MUTAGENESIS OF RP GLU-289; PHE-364; PHE-366 AND PHE-368. RX PubMed=27160427; DOI=10.1038/srep25646; RA Wang B., Qin X., Wu J., Deng H., Li Y., Yang H., Chen Z., Liu G., Ren D.; RT "Analysis of crystal structure of Arabidopsis MPK6 and generation of its RT mutants with higher activity."; RL Sci. Rep. 6:25646-25646(2016). RN [52] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 32-395, AND SUBCELLULAR LOCATION. RX PubMed=31235876; DOI=10.1038/s41477-019-0440-x; RA Putarjunan A., Ruble J., Srivastava A., Zhao C., Rychel A.L., RA Hofstetter A.K., Tang X., Zhu J.K., Tama F., Zheng N., Torii K.U.; RT "Bipartite anchoring of SCREAM enforces stomatal initiation by coupling MAP RT kinases to SPEECHLESS."; RL Nat. Plants 5:742-754(2019). CC -!- FUNCTION: Mitogen-activated protein kinase (MAPK) which regulates CC abscisic acid (ABA) responses in a MAPKKK20-MKK5-MPK6 cascade involved CC in root growth (e.g. root cell division and elongation) and stomatal CC response (PubMed:27913741). Involved in oxidative stress-mediated CC signaling cascade (such as ozone). Involved in the innate immune MAP CC kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6) downstream of CC bacterial flagellin receptor FLS2. May be involved in hypersensitive CC response (HR)-mediated signaling cascade by modulating LIP5 CC phosphorylation and subsequent multivesicular bodies (MVBs) CC trafficking. May phosphorylate regulators of WRKY transcription CC factors. 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 gene- CC mediated and basal resistance response to certain pathogens. May be CC involved in the cold and salinity stress-mediated MAP kinase signaling CC cascade (MEKK1, MKK1/MKK2 and MPK4/MPK6). MKK1-MPK6 module mediates CC abscisic acid (ABA)-dependent CAT1 expression with H(2)O(2) production CC and response to drought and salt stress. MKK1-MPK6 module is also CC involved in sugar signaling during the process of seed germination. CC MKK3-MPK6 module plays an important role in the jasmonate signal CC transduction pathway through the negative regulation of MYC2/JIN1 CC expression. MKK9-MPK3/MPK6 module phosphorylates and activates EIN3, CC leading to the promotion of EIN3-mediated transcription in ethylene CC signaling. MPK3/MPK6 cascade regulates camalexin synthesis through CC transcriptional regulation of the biosynthetic genes after pathogen CC infection. MKK9-MPK6 module positively regulates leaf senescence. YDA- CC MKK4/MKK5-MPK3/MPK6 module regulates stomatal cell fate before the CC guard mother cell (GMC) is specified. When activated, reinforces the CC feedback loop by phosphorylating BASL, and inhibits stomatal fate by CC phosphorylating SPCH (PubMed:25843888). This MAPK cascade also CC functions downstream of the ER receptor in regulating coordinated local CC cell proliferation, which shapes the morphology of plant organs. CC {ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:15020743, CC ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:15539472, CC ECO:0000269|PubMed:15964670, ECO:0000269|PubMed:17259259, CC ECO:0000269|PubMed:17369371, ECO:0000269|PubMed:18248592, CC ECO:0000269|PubMed:18273012, ECO:0000269|PubMed:18378893, CC ECO:0000269|PubMed:19251906, ECO:0000269|PubMed:19484493, CC ECO:0000269|PubMed:23263767, ECO:0000269|PubMed:25010425, CC ECO:0000269|PubMed:25843888, ECO:0000269|PubMed:27913741}. 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=2.7.11.24; CC Evidence={ECO:0000269|PubMed:10713056, ECO:0000269|PubMed:10717008, CC ECO:0000269|PubMed:11123804, ECO:0000269|PubMed:11500556, CC ECO:0000269|PubMed:11577197, ECO:0000269|PubMed:12220631, CC ECO:0000269|PubMed:12628921, ECO:0000269|PubMed:15225555, CC ECO:0000269|PubMed:15500467}; 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=2.7.11.24; Evidence={ECO:0000269|PubMed:10713056, CC ECO:0000269|PubMed:10717008, ECO:0000269|PubMed:11123804, CC ECO:0000269|PubMed:11500556, ECO:0000269|PubMed:11577197, CC ECO:0000269|PubMed:12220631, ECO:0000269|PubMed:12628921, CC ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:15500467}; CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine CC phosphorylation. Activated by the MAP kinase kinases MKK2, MKK3, MKK4, CC MKK5, MKK7 and MKK9. Activated in response to touch, wounding, low CC temperature, low humidity, salt stress, hydrogen peroxide, ozone, ACC CC (an ethylene precursor), jasmonic acid (JA), mastoparan and UVC. CC Activated in response to elicitors: oligogalacturonides, hexameric CC chitin fragments, fungal xylanase, and the bacterial flagellin and CC harpin. Activated upon Pseudomonas syringae pv. tomato DC3000 CC infection. Repressed by the protein phosphatase 2C AP2C1 and the CC protein-tyrosine-phosphatases MKP1 and PTP1. Repressed by DSPTP1B/MKP2- CC mediated dephosphorylation. Activated by polarized BASL CC (PubMed:27746029). Triggered by MKKK20 in response to various abiotic CC stresses, including osmotic stress, cold and reactive oxygen species CC (ROS) (PubMed:21969089). Activated by MKK5 in response to abscisic acid CC (ABA) (PubMed:27913741). {ECO:0000269|PubMed:10713056, CC ECO:0000269|PubMed:10717008, ECO:0000269|PubMed:11123804, CC ECO:0000269|PubMed:11500556, ECO:0000269|PubMed:11577197, CC ECO:0000269|PubMed:12220631, ECO:0000269|PubMed:12628921, CC ECO:0000269|PubMed:15084727, ECO:0000269|PubMed:15225555, CC ECO:0000269|PubMed:15500467, ECO:0000269|PubMed:17369371, CC ECO:0000269|PubMed:17506336, ECO:0000269|PubMed:17586809, CC ECO:0000269|PubMed:17630279, ECO:0000269|PubMed:17933903, CC ECO:0000269|PubMed:18273012, ECO:0000269|PubMed:19251906, CC ECO:0000269|PubMed:19789277, ECO:0000269|PubMed:21969089, CC ECO:0000269|PubMed:27746029, ECO:0000269|PubMed:27913741}. CC -!- SUBUNIT: Interacts with MEKK1, MKK1 and MKK2. May form a ternary CC complex with MEKK1 and MKK1 or MKK2. Interacts with NDPK2, AP2C1, MKP1 CC and PTP1. Interacts with DSPTP1B/MKP2, especially during HR-like CC responses triggered by fungal elicitors. Interacts with MKK4, MKK5 and CC MKK6 (PubMed:12506203, PubMed:15225555, PubMed:17630279, CC PubMed:19513235, PubMed:19789277, PubMed:20626661, PubMed:21057191, CC PubMed:21575092, PubMed:27913741). Binds to LIP5 (PubMed:25010425). CC Interacts with VQ4 and IKU1/VQ14 (PubMed:24750137). Interacts with CC RACK1A, RACK1B and RACK1C (PubMed:25731164). Interacts with PTP1 CC (PubMed:27029354). Interacts with FLZ9 (Ref.48). Binds to BASL and YDA CC (PubMed:25843888). {ECO:0000269|PubMed:12506203, CC ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:17630279, CC ECO:0000269|PubMed:19513235, ECO:0000269|PubMed:19789277, CC ECO:0000269|PubMed:20626661, ECO:0000269|PubMed:21057191, CC ECO:0000269|PubMed:21575092, ECO:0000269|PubMed:24750137, CC ECO:0000269|PubMed:25010425, ECO:0000269|PubMed:25731164, CC ECO:0000269|PubMed:25843888, ECO:0000269|PubMed:27029354, CC ECO:0000269|PubMed:27913741, ECO:0000269|Ref.48}. CC -!- INTERACTION: CC Q39026; O80871: At2g30020; NbExp=3; IntAct=EBI-349548, EBI-16897073; CC Q39026; O80719: At2g47060; NbExp=3; IntAct=EBI-349548, EBI-4436376; CC Q39026; Q84JD1: At5g07260; NbExp=4; IntAct=EBI-349548, EBI-25510874; CC Q39026; Q8VZG1: DGK3; NbExp=4; IntAct=EBI-349548, EBI-4441630; CC Q39026; Q9FKG1: ERF104; NbExp=3; IntAct=EBI-349548, EBI-2360943; CC Q39026; Q9S7U9: MKK2; NbExp=8; IntAct=EBI-349548, EBI-994350; CC Q39026; O80397: MKK4; NbExp=7; IntAct=EBI-349548, EBI-2358409; CC Q39026; Q8RXG3: MKK5; NbExp=4; IntAct=EBI-349548, EBI-2358458; CC Q39026; Q9FJV0: MKK6; NbExp=5; IntAct=EBI-349548, EBI-1238868; CC Q39026; Q9M0J5: MYB41; NbExp=2; IntAct=EBI-349548, EBI-4474106; CC Q39026; Q9LPW3: SCRM2; NbExp=4; IntAct=EBI-349548, EBI-4451593; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000269|PubMed:31235876}. CC Cytoplasm, cell cortex {ECO:0000269|PubMed:25843888}. Note=Translocated CC into the nucleus in response to phosphorylation (Probable). Recruited CC by BASL at the cell cortex in a polarized manner (PubMed:25843888). CC Mobility in stomatal lineage ground cells (SLGCs) is triggered by BASL, CC increased in response to hydrogen peroxide H(2)O(2), but repressed by CC U0126 (PubMed:27746029). {ECO:0000269|PubMed:25843888, CC ECO:0000269|PubMed:27746029, ECO:0000305}. CC -!- DEVELOPMENTAL STAGE: Copolarizes with BASL, YDA and MPK3 in stomatal CC asymmetric cell division (ACD) cells. {ECO:0000269|PubMed:27746029}. CC -!- INDUCTION: By Alternaria brassicae pathogen infection. CC {ECO:0000269|PubMed:21947882}. 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 the CC enzyme. Dephosphorylated by DSPTP1B/MKP2. {ECO:0000269|PubMed:10713056, CC ECO:0000269|PubMed:11123804}. CC -!- DISRUPTION PHENOTYPE: Reduced sensitivity to abscisic acid (ABA) during CC germination. Insensitivity to ABA in terms of root growth inhibition CC (e.g. root cell division and elongation) and stomatal response leading CC to increased water loss under dehydrated conditions (PubMed:27913741). CC Delayed senescence phenotype. {ECO:0000269|PubMed:19251906, CC ECO:0000269|PubMed:19484493, ECO:0000269|PubMed:27913741}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. MAP kinase subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00159, 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; D21842; BAA04869.1; -; mRNA. DR EMBL; AC002333; AAB64027.1; -; Genomic_DNA. DR EMBL; CP002685; AEC10325.1; -; Genomic_DNA. DR EMBL; AY120737; AAM53295.1; -; mRNA. DR EMBL; BT008855; AAP68294.1; -; mRNA. DR PIR; S40472; S40472. DR RefSeq; NP_181907.1; NM_129941.4. DR PDB; 5CI6; X-ray; 3.00 A; A/B=29-395. DR PDB; 6DTL; X-ray; 2.75 A; A/B=32-395. DR PDBsum; 5CI6; -. DR PDBsum; 6DTL; -. DR AlphaFoldDB; Q39026; -. DR SMR; Q39026; -. DR BioGRID; 4318; 218. DR DIP; DIP-31825N; -. DR ELM; Q39026; -. DR IntAct; Q39026; 17. DR MINT; Q39026; -. DR STRING; 3702.Q39026; -. DR iPTMnet; Q39026; -. DR PaxDb; 3702-AT2G43790-1; -. DR ProteomicsDB; 238273; -. DR EnsemblPlants; AT2G43790.1; AT2G43790.1; AT2G43790. DR GeneID; 818982; -. DR Gramene; AT2G43790.1; AT2G43790.1; AT2G43790. DR KEGG; ath:AT2G43790; -. DR Araport; AT2G43790; -. DR TAIR; AT2G43790; MPK6. DR eggNOG; KOG0660; Eukaryota. DR HOGENOM; CLU_000288_181_1_1; -. DR InParanoid; Q39026; -. DR OMA; MDIPRPE; -. DR OrthoDB; 5474493at2759; -. DR PhylomeDB; Q39026; -. DR BRENDA; 2.7.11.24; 399. DR PRO; PR:Q39026; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; Q39026; baseline and differential. DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0009524; C:phragmoplast; IDA:TAIR. DR GO; GO:0009574; C:preprophase band; IDA:TAIR. DR GO; GO:0005802; C:trans-Golgi network; 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:0019902; F:phosphatase binding; IPI:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB. DR GO; GO:0010120; P:camalexin biosynthetic process; IMP:TAIR. DR GO; GO:0051301; P:cell division; IMP:UniProtKB. DR GO; GO:0042742; P:defense response to bacterium; IEP:TAIR. DR GO; GO:0009864; P:induced systemic resistance, jasmonic acid mediated signaling pathway; IMP:TAIR. DR GO; GO:0010229; P:inflorescence development; IMP:TAIR. DR GO; GO:0010150; P:leaf senescence; IMP:UniProtKB. DR GO; GO:0048481; P:plant ovule development; IGI:TAIR. DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW. DR GO; GO:0009555; P:pollen development; IGI:TAIR. DR GO; GO:0010183; P:pollen tube guidance; IGI:TAIR. DR GO; GO:0080136; P:priming of cellular response to stress; IMP:TAIR. DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR. DR GO; GO:0010082; P:regulation of root meristem growth; IMP:UniProtKB. DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB. DR GO; GO:0051510; P:regulation of unidimensional cell growth; IMP:UniProtKB. DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR. DR GO; GO:0009409; P:response to cold; IDA:TAIR. DR GO; GO:0009723; P:response to ethylene; IDA:TAIR. DR GO; GO:0050826; P:response to freezing; IMP:TAIR. DR GO; GO:0009620; P:response to fungus; IEP:UniProtKB. DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:TAIR. DR GO; GO:1902065; P:response to L-glutamate; IDA:TAIR. DR GO; GO:0006970; P:response to osmotic stress; IDA:TAIR. DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR. DR GO; GO:0000302; P:response to reactive oxygen species; IEP:TAIR. DR GO; GO:0009651; P:response to salt stress; IGI:TAIR. DR GO; GO:0010224; P:response to UV-B; IMP:TAIR. DR GO; GO:0048364; P:root development; IMP:TAIR. DR CDD; cd07858; STKc_TEY_MAPK; 1. DR DisProt; DP02631; -. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR003527; MAP_kinase_CS. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF573; MITOGEN-ACTIVATED PROTEIN KINASE 6; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-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. DR Genevisible; Q39026; AT. PE 1: Evidence at protein level; KW 3D-structure; Abscisic acid signaling pathway; ATP-binding; Cytoplasm; KW Hypersensitive response; Kinase; Nucleotide-binding; Nucleus; KW Phosphoprotein; Plant defense; Reference proteome; KW Serine/threonine-protein kinase; Stress response; Transferase. FT CHAIN 1..395 FT /note="Mitogen-activated protein kinase 6" FT /id="PRO_0000186315" FT DOMAIN 63..348 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..35 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 221..223 FT /note="TXY" FT ACT_SITE 189 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 69..77 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 92 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 221 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:10713056" FT MOD_RES 223 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:10713056" FT MOD_RES 226 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19245862" FT MUTAGEN 92 FT /note="K->M: Loss of kinase activity." FT /evidence="ECO:0000269|PubMed:11875555" FT MUTAGEN 93 FT /note="K->M: Loss of kinase activity." FT /evidence="ECO:0000269|PubMed:11875555" FT MUTAGEN 221..223 FT /note="TEY->AEF: In MPK6_AEF; reduced mobility, impaired FT BASL-triggered mobility increase, and clustered stomata." FT /evidence="ECO:0000269|PubMed:27746029" FT MUTAGEN 289 FT /note="E->G: Reduced kinase activity." FT /evidence="ECO:0000269|PubMed:27160427" FT MUTAGEN 364 FT /note="F->L: Increased kinase activity, and confers the FT ability to induce ethylene and leaf senescence." FT /evidence="ECO:0000269|PubMed:27160427" FT MUTAGEN 366 FT /note="F->L: Increased kinase activity." FT /evidence="ECO:0000269|PubMed:27160427" FT MUTAGEN 368 FT /note="F->L: Increased kinase activity, and confers the FT ability to induce ethylene and leaf senescence." FT /evidence="ECO:0000269|PubMed:27160427" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:5CI6" FT STRAND 38..41 FT /evidence="ECO:0007829|PDB:6DTL" FT TURN 42..45 FT /evidence="ECO:0007829|PDB:6DTL" FT STRAND 46..51 FT /evidence="ECO:0007829|PDB:6DTL" FT STRAND 54..59 FT /evidence="ECO:0007829|PDB:6DTL" FT STRAND 67..82 FT /evidence="ECO:0007829|PDB:6DTL" FT TURN 83..86 FT /evidence="ECO:0007829|PDB:6DTL" FT STRAND 87..94 FT /evidence="ECO:0007829|PDB:6DTL" FT TURN 95..98 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 101..116 FT /evidence="ECO:0007829|PDB:6DTL" FT STRAND 125..128 FT /evidence="ECO:0007829|PDB:6DTL" FT STRAND 132..136 FT /evidence="ECO:0007829|PDB:6DTL" FT STRAND 140..145 FT /evidence="ECO:0007829|PDB:6DTL" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 151..156 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 163..182 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:6DTL" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:6DTL" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 219..223 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 232..235 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 244..259 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 269..280 FT /evidence="ECO:0007829|PDB:6DTL" FT STRAND 285..291 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 293..300 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 310..313 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 319..328 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 333..335 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 339..344 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 346..348 FT /evidence="ECO:0007829|PDB:6DTL" FT TURN 349..351 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 354..356 FT /evidence="ECO:0007829|PDB:6DTL" FT STRAND 368..372 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 375..389 FT /evidence="ECO:0007829|PDB:6DTL" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:6DTL" 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 //