MPK6_ARATH
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 03-AUG-2022, entry version 196.
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.AT2G43790.1; -.
DR iPTMnet; Q39026; -.
DR PaxDb; Q39026; -.
DR PRIDE; Q39026; -.
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; locus:2043904; AT2G43790.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q39026; -.
DR OMA; YTDLNPV; -.
DR OrthoDB; 741207at2759; -.
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 Genevisible; Q39026; AT.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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: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:0035556; P:intracellular signal transduction; IBA:GO_Central.
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 DisProt; DP02631; -.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 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
