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Mitogen-activated protein kinase kinase kinase 1 (ARAKIN) (AtMEKK1) (MAP kinase kinase kinase 1) (EC 2.7.11.25)

 M3K1_ARATH              Reviewed;         608 AA.
Q39008; O81470; Q39020; Q8W4N5;
11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
11-JUL-2006, sequence version 2.
25-APR-2018, entry version 130.
RecName: Full=Mitogen-activated protein kinase kinase kinase 1;
Short=ARAKIN;
Short=AtMEKK1;
Short=MAP kinase kinase kinase 1;
EC=2.7.11.25 {ECO:0000269|PubMed:23857079};
Name=MEKK1; OrderedLocusNames=At4g08500; ORFNames=T15F16.5;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
STRAIN=cv. Columbia;
PubMed=8570631; DOI=10.1073/pnas.93.2.765;
Mizoguchi T., Irie K., Hirayama T., Hayashida N.,
Yamaguchi-Shinozaki K., Matsumoto K., Shinozaki K.;
"A gene encoding a mitogen-activated protein kinase kinase kinase is
induced simultaneously with genes for a mitogen-activated protein
kinase and an S6 ribosomal protein kinase by touch, cold, and water
stress in Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 93:765-769(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 115-608.
PubMed=8597596; DOI=10.1016/0167-4781(95)00233-2;
Covic L., Lew R.R.;
"Arabidopsis thaliana cDNA isolated by functional complementation
shows homology to serine/threonine protein kinases.";
Biochim. Biophys. Acta 1305:125-129(1996).
[6]
INDUCTION.
PubMed=10556579; DOI=10.1016/S0167-4889(99)00096-8;
Covic L., Silva N.F., Lew R.R.;
"Functional characterization of ARAKIN (ATMEKK1): a possible mediator
in an osmotic stress response pathway in higher plants.";
Biochim. Biophys. Acta 1451:242-254(1999).
[7]
SUBUNIT, AND INTERACTION WITH MKK1; MMK2 AND MPK4.
PubMed=9878570; DOI=10.1006/bbrc.1998.9796;
Ichimura K., Mizoguchi T., Irie K., Morris P.C., Giraudat J.,
Matsumoto K., Shinozaki K.;
"Isolation of ATMEKK1 (a MAP kinase kinase kinase)-interacting
proteins and analysis of a MAP kinase cascade in Arabidopsis.";
Biochem. Biophys. Res. Commun. 253:532-543(1998).
[8]
FUNCTION.
PubMed=11875555; DOI=10.1038/415977a;
Asai T., Tena G., Plotnikova J., Willmann M.R., Chiu W.-L.,
Gomez-Gomez L., Boller T., Ausubel F.M., Sheen J.;
"MAP kinase signalling cascade in Arabidopsis innate immunity.";
Nature 415:977-983(2002).
[9]
NOMENCLATURE.
PubMed=12119167; DOI=10.1016/S1360-1385(02)02302-6;
MAPK group;
"Mitogen-activated protein kinase cascades in plants: a new
nomenclature.";
Trends Plant Sci. 7:301-308(2002).
[10]
FUNCTION.
PubMed=15225555; DOI=10.1016/j.molcel.2004.06.023;
Teige M., Scheikl E., Eulgem T., Doczi R., Ichimura K., Shinozaki K.,
Dangl J.L., Hirt H.;
"The MKK2 pathway mediates cold and salt stress signaling in
Arabidopsis.";
Mol. Cell 15:141-152(2004).
[11]
FUNCTION, AND INTERACTION WITH MKK1; MKK2 AND MPK4.
PubMed=18982020; DOI=10.1038/cr.2008.300;
Gao M., Liu J., Bi D., Zhang Z., Cheng F., Chen S., Zhang Y.;
"MEKK1, MKK1/MKK2 and MPK4 function together in a mitogen-activated
protein kinase cascade to regulate innate immunity in plants.";
Cell Res. 18:1190-1198(2008).
[12]
INTERACTION WITH CRLK1, AND SUBCELLULAR LOCATION.
PubMed=20724845; DOI=10.4161/psb.5.8.12225;
Yang T., Shad Ali G., Yang L., Du L., Reddy A.S., Poovaiah B.W.;
"Calcium/calmodulin-regulated receptor-like kinase CRLK1 interacts
with MEKK1 in plants.";
Plant Signal. Behav. 5:991-994(2010).
[13]
CATALYTIC ACTIVITY, ENZYME REGULATION, AND PHOSPHORYLATION.
STRAIN=cv. Columbia;
PubMed=23857079; DOI=10.1007/s10265-013-0576-0;
Furuya T., Matsuoka D., Nanmori T.;
"Phosphorylation of Arabidopsis thaliana MEKK1 via Ca(2+) signaling as
a part of the cold stress response.";
J. Plant Res. 126:833-840(2013).
[14]
INTERACTION WITH RACK1A; RACK1B AND RACK1C.
PubMed=25731164; DOI=10.1038/nature14243;
Cheng Z., Li J.F., Niu Y., Zhang X.C., Woody O.Z., Xiong Y.,
Djonovic S., Millet Y., Bush J., McConkey B.J., Sheen J.,
Ausubel F.M.;
"Pathogen-secreted proteases activate a novel plant immune pathway.";
Nature 521:213-216(2015).
-!- FUNCTION: The MEKK1, MKK1/MKK2 and MPK4 function in a signaling
pathway that modulates the expression of genes responding to
biotic and abiotic stresses and also plays an important role in
pathogen defense by negatively regulating innate immunity.
Involved in the innate immune MAP kinase signaling cascade (MEKK1,
MKK4/MKK5 and MPK3/MPK6) downstream of bacterial flagellin
receptor FLS2. May be involved in the cold and salinity stress-
mediated MAP kinase signaling cascade (MEKK1, MKK1/MKK2 and
MPK4/MPK6). Activates by phosphorylation the downstream MKK2, MKK4
and MKK5 in a calcium-dependent manner.
{ECO:0000269|PubMed:11875555, ECO:0000269|PubMed:15225555,
ECO:0000269|PubMed:18982020, ECO:0000269|PubMed:23857079}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:23857079}.
-!- ENZYME REGULATION: Activated by cold via CRLK1-mediated
phosphorylation and leading to elevated kinase activity towards
MKK2. {ECO:0000269|PubMed:23857079}.
-!- SUBUNIT: Interacts with MKK1, MMK2 and MPK4. May form a ternary
complex composed of MEKK1 and MKK1/MKK2 and MPK4 (PubMed:18982020,
PubMed:9878570). Interacts with RACK1A, RACK1B and RACK1C
(PubMed:25731164). Binds to CRLK1 (PubMed:20724845).
{ECO:0000269|PubMed:18982020, ECO:0000269|PubMed:20724845,
ECO:0000269|PubMed:25731164, ECO:0000269|PubMed:9878570}.
-!- INTERACTION:
Q94A06:MKK1; NbExp=4; IntAct=EBI-994439, EBI-994464;
Q9SUP6:WRKY53; NbExp=5; IntAct=EBI-994439, EBI-1235980;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20724845}.
Endosome {ECO:0000269|PubMed:20724845}.
-!- INDUCTION: By touch, cold and salinity stress.
{ECO:0000269|PubMed:10556579, ECO:0000269|PubMed:8570631}.
-!- PTM: Phosphorylated by CRLK1 in response to cold.
{ECO:0000269|PubMed:23857079}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase kinase subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA99196.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=AAA99196.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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EMBL; D50468; BAA09057.1; -; mRNA.
EMBL; AF076275; AAC28196.1; -; Genomic_DNA.
EMBL; AL161511; CAB77975.1; -; Genomic_DNA.
EMBL; CP002687; AEE82651.1; -; Genomic_DNA.
EMBL; AY062459; AAL32537.1; -; mRNA.
EMBL; BT000116; AAN15435.1; -; mRNA.
EMBL; L43125; AAA99196.1; ALT_SEQ; Genomic_DNA.
PIR; T01833; T01833.
RefSeq; NP_192590.1; NM_116919.4.
UniGene; At.21066; -.
ProteinModelPortal; Q39008; -.
SMR; Q39008; -.
BioGrid; 11709; 9.
IntAct; Q39008; 3.
STRING; 3702.AT4G08500.1; -.
iPTMnet; Q39008; -.
PaxDb; Q39008; -.
EnsemblPlants; AT4G08500.1; AT4G08500.1; AT4G08500.
GeneID; 826409; -.
Gramene; AT4G08500.1; AT4G08500.1; AT4G08500.
KEGG; ath:AT4G08500; -.
Araport; AT4G08500; -.
TAIR; locus:2133559; AT4G08500.
eggNOG; KOG0198; Eukaryota.
eggNOG; ENOG410XQGS; LUCA.
HOGENOM; HOG000239933; -.
InParanoid; Q39008; -.
KO; K13414; -.
OMA; ARNINYD; -.
OrthoDB; EOG0936083X; -.
PhylomeDB; Q39008; -.
BRENDA; 2.7.11.25; 399.
PRO; PR:Q39008; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q39008; baseline and differential.
Genevisible; Q39008; AT.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IDA:TAIR.
GO; GO:0019900; F:kinase binding; IPI:TAIR.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0009631; P:cold acclimation; IDA:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0000165; P:MAPK cascade; IMP:TAIR.
GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0009409; P:response to cold; IDA:UniProtKB.
GO; GO:1902065; P:response to L-glutamate; IMP:TAIR.
GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0009611; P:response to wounding; IDA:TAIR.
GO; GO:0010449; P:root meristem growth; IGI:TAIR.
GO; GO:0022622; P:root system development; IMP:TAIR.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Endosome; Immunity;
Innate immunity; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Plant defense; Reference proteome; Serine/threonine-protein kinase;
Stress response; Transferase.
CHAIN 1 608 Mitogen-activated protein kinase kinase
kinase 1.
/FTId=PRO_0000245826.
DOMAIN 333 587 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 339 347 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 325 Regulatory region.
{ECO:0000269|PubMed:9878570}.
REGION 192 234 Binding with MPK4.
{ECO:0000269|PubMed:9878570}.
ACT_SITE 456 456 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 361 361 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000250|UniProtKB:O81472}.
MOD_RES 603 603 Phosphoserine.
{ECO:0000250|UniProtKB:O81472}.
CONFLICT 39 39 D -> A (in Ref. 1; AAC28196).
{ECO:0000305}.
CONFLICT 341 341 R -> L (in Ref. 4; AAL32537/AAN15435).
{ECO:0000305}.
SEQUENCE 608 AA; 66024 MW; 70C1A1C314E2DFDD CRC64;
MDRILARMKK STGRRGGDKN ITPVRRLERR DAARNINYDA ASCSSSSAED LSVSTSSLMT
RSLEFPEPTS FRIGGGVGEM DRIYRSLGVS GPDDLAISFD AWEACKKRSS SDVVNRFKSF
DLDKVRDQDL SEEGPSGVVV GSDSMNHKVQ GQDLSEAGPS GGIVTELSEI GNLITPVDRL
VADGVVENRR VMERTPTIVK SKGYLVPNNV VAVGVGVGGG IKGLRPPVLK PPPAMKRPPI
DHRGSSWDFL THFAPSETVK RPSSSSSSSE DGCDEEEGKE EEAEAEEMGA RFIQLGDTAD
ETCSFTTNEG DSSSTVSNTS PIYPDGGAII TSWQKGQLLG RGSFGSVYEG ISGDGDFFAV
KEVSLLDQGS QAQECIQQLE GEIKLLSQLQ HQNIVRYRGT AKDGSNLYIF LELVTQGSLL
KLYQRYQLRD SVVSLYTRQI LDGLKYLHDK GFIHRDIKCA NILVDANGAV KLADFGLAKV
SKFNDIKSCK GTPFWMAPEV INRKDSDGYG SPADIWSLGC TVLEMCTGQI PYSDLEPVQA
LFRIGRGTLP EVPDTLSLDA RLFILKCLKV NPEERPTAAE LLNHPFVRRP LPSVGSGGSG
SASPLLRR


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