M3K20_ARATH
ID M3K20_ARATH Reviewed; 342 AA.
AC Q9SND6; A0A178VGW0;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 20 {ECO:0000303|PubMed:21969089};
DE Short=MAPKK kinase 20 {ECO:0000303|PubMed:21969089};
DE EC=2.7.11.25 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:27913741, ECO:0000269|PubMed:28848569};
DE AltName: Full=Protein ABA-INSENSITIVE PROTEIN KINASE 1 {ECO:0000303|PubMed:27913741};
GN Name=MAPKKK20 {ECO:0000303|PubMed:21969089};
GN Synonyms=AIK1 {ECO:0000303|PubMed:27913741},
GN MKKK20 {ECO:0000303|PubMed:21969089};
GN OrderedLocusNames=At3g50310 {ECO:0000312|Araport:AT3G50310};
GN ORFNames=F11C1.150 {ECO:0000312|EMBL:CAB62310.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY SALT; MANNITOL; METHYL
RP VIOLOGEN; SORBITOL AND COLD, AND DEVELOPMENTAL STAGE.
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 [4]
RP REVIEW ON SIGNALING.
RX PubMed=24795738; DOI=10.3389/fpls.2014.00151;
RA Golldack D., Li C., Mohan H., Probst N.;
RT "Tolerance to drought and salt stress in plants: Unraveling the signaling
RT networks.";
RL Front. Plant Sci. 5:151-151(2014).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION WITH MKK3 AND MPK18,
RP AUTOPHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION
RP AT SER-18; THR-19; TYR-41; TYR-66; SER-93 AND SER-114, AND ACTIVITY
RP REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=28848569; DOI=10.3389/fpls.2017.01352;
RA Benhamman R., Bai F., Drory S.B., Loubert-Hudon A., Ellis B., Matton D.P.;
RT "The Arabidopsis mitogen-activated protein kinase kinase kinase 20 (MKKK20)
RT acts upstream of MKK3 and MPK18 in two separate signaling pathways involved
RT in root microtubule functions.";
RL Front. Plant Sci. 8:1352-1352(2017).
RN [6]
RP FUNCTION, MUTAGENESIS OF LYS-36, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY ABSCISIC ACID,
RP ACTIVITY REGULATION, INTERACTION WITH MKK5, AND SUBCELLULAR LOCATION.
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 [7]
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 [8]
RP INTERACTION WITH MKK3, AND SUBCELLULAR LOCATION.
RX PubMed=30081740; DOI=10.1080/15592324.2018.1503498;
RA Bai F., Matton D.P.;
RT "The Arabidopsis mitogen-activated protein kinase kinase kinase 20 (MKKK20)
RT C-terminal domain interacts with MKK3 and harbors a typical DEF mammalian
RT MAP kinase docking site.";
RL Plant Signal. Behav. 13:E1503498-E1503498(2018).
CC -!- FUNCTION: Mitogen-activated protein kinase kinase (MAPKK) that
CC phosphorylates both MKK3 and MPK18 and regulate two separate signaling
CC pathways involved in root microtubule functions (PubMed:28848569).
CC MAPKK which regulates abscisic acid (ABA) responses in a MAPKKK20-MKK5-
CC MPK6 cascade involved in root growth (e.g. root cell division and
CC elongation) and stomatal response, probably via MKK5 activation by
CC protein phosphorylation and subsequent activation of MAPK6 by MKK5
CC (PubMed:27913741). Involved in various abiotic stresses (e.g. osmotic
CC stress, cold and hydrogen peroxide) responses by phosphorylating and
CC thus regulating MPK6 activity, in an ABA-independent manner
CC (PubMed:21969089). {ECO:0000269|PubMed:21969089,
CC ECO:0000269|PubMed:27913741, ECO:0000269|PubMed:28848569}.
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=2.7.11.25;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00159,
CC ECO:0000269|PubMed:27913741, ECO:0000269|PubMed:28848569};
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=2.7.11.25; Evidence={ECO:0000255|PROSITE-ProRule:PRU00159,
CC ECO:0000269|PubMed:27913741, ECO:0000269|PubMed:28848569};
CC -!- ACTIVITY REGULATION: Activated through serine, threonine and tyrosine
CC phosphorylation, especially upon abscisic acid (ABA) treatment
CC (PubMed:28848569, PubMed:27913741). Restricted activity by ABI1-
CC mediated dephosphorylation (PubMed:27913741).
CC {ECO:0000269|PubMed:27913741, ECO:0000269|PubMed:28848569}.
CC -!- SUBUNIT: Interacts with MKK3 and MPK18 via its C-terminal domain
CC (PubMed:28848569, PubMed:30081740). Binds to MKK5 (PubMed:27913741).
CC {ECO:0000269|PubMed:27913741, ECO:0000269|PubMed:28848569,
CC ECO:0000269|PubMed:30081740}.
CC -!- INTERACTION:
CC Q9SND6; P25854: CAM4; NbExp=2; IntAct=EBI-1235872, EBI-1235664;
CC Q9SND6; Q03509: CAM6; NbExp=2; IntAct=EBI-1235872, EBI-1236097;
CC Q9SND6; Q9S744: CML9; NbExp=2; IntAct=EBI-1235872, EBI-1236048;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28848569}. Cytoplasm
CC {ECO:0000269|PubMed:27913741, ECO:0000269|PubMed:28848569,
CC ECO:0000269|PubMed:30081740}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, seedlings, leaves, flower buds,
CC flowers and siliques. {ECO:0000269|PubMed:21969089,
CC ECO:0000269|PubMed:27913741, ECO:0000269|PubMed:28848569}.
CC -!- DEVELOPMENTAL STAGE: During flower development, strongly expressed in
CC pollen grains with a progressive increase from young buds to later
CC stages of maturation (PubMed:28848569). To a lesser extent, present in
CC the gynoecium, particularly in the style and carpel (PubMed:28848569).
CC Also expressed in nectaries, petals, sepals and pollen tubes
CC (PubMed:28848569). Accumulates progressively during seedlings
CC development (PubMed:21969089). In mature plants, confined to floral
CC clusters (PubMed:21969089). In roots, present in meristematic and
CC elongation zones (PubMed:27913741). {ECO:0000269|PubMed:21969089,
CC ECO:0000269|PubMed:27913741, ECO:0000269|PubMed:28848569}.
CC -!- INDUCTION: Induced by salt (NaCl), mannitol, methyl viologen (MV),
CC sorbitol and cold (PubMed:21969089). Triggered by abscisic acid (ABA)
CC (PubMed:27913741). {ECO:0000269|PubMed:21969089,
CC ECO:0000269|PubMed:27913741}.
CC -!- PTM: Autophosphorylates; active in phosphorylated state
CC (PubMed:28848569). Dephosphorylated by ABI1 (PubMed:27913741).
CC {ECO:0000269|PubMed:27913741, ECO:0000269|PubMed:28848569}.
CC -!- DISRUPTION PHENOTYPE: Short roots with abnormal twisting (e.g. leftward
CC skewing) in media containing microtubule-disrupting drugs (e.g.
CC oryzalin) (PubMed:28848569). Stronger sensitivity to high salt
CC concentration and higher water loss rates under dehydration conditions
CC (PubMed:21969089). Increased accumulation of superoxide under high salt
CC condition (PubMed:21969089). All these phenotypes are associated with
CC reduced MPK6 activity (PubMed:21969089). Insensitivity to abscisic acid
CC (ABA) in terms of root growth inhibition (e.g. root cell division and
CC elongation) and stomatal response leading to increased water loss under
CC dehydrated conditions (PubMed:27913741). Impaired ABA-mediated
CC increased activity of MPK6 (PubMed:27913741).
CC {ECO:0000269|PubMed:21969089, ECO:0000269|PubMed:27913741,
CC ECO:0000269|PubMed:28848569}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AL132976; CAB62310.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78651.1; -; Genomic_DNA.
DR PIR; T45577; T45577.
DR RefSeq; NP_190600.1; NM_114891.2.
DR AlphaFoldDB; Q9SND6; -.
DR IntAct; Q9SND6; 7.
DR STRING; 3702.AT3G50310.1; -.
DR PaxDb; Q9SND6; -.
DR PRIDE; Q9SND6; -.
DR EnsemblPlants; AT3G50310.1; AT3G50310.1; AT3G50310.
DR GeneID; 824193; -.
DR Gramene; AT3G50310.1; AT3G50310.1; AT3G50310.
DR KEGG; ath:AT3G50310; -.
DR Araport; AT3G50310; -.
DR TAIR; locus:2074835; AT3G50310.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q9SND6; -.
DR OMA; KDSKKRW; -.
DR OrthoDB; 841529at2759; -.
DR PhylomeDB; Q9SND6; -.
DR BRENDA; 2.7.11.25; 399.
DR PRO; PR:Q9SND6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SND6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IDA:TAIR.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0019901; F:protein kinase binding; IPI: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:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0048235; P:pollen sperm cell differentiation; IEP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0010082; P:regulation of root meristem growth; IMP:TAIR.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:TAIR.
DR GO; GO:0051510; P:regulation of unidimensional cell growth; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0000302; P:response to reactive oxygen species; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; 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 Abscisic acid signaling pathway; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Stress response; Transferase.
FT CHAIN 1..342
FT /note="Mitogen-activated protein kinase kinase kinase 20"
FT /id="PRO_0000449278"
FT DOMAIN 3..268
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 285..342
FT /note="Required for MKK3 binding"
FT /evidence="ECO:0000269|PubMed:30081740"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 9..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28848569"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:28848569"
FT MOD_RES 41
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:28848569"
FT MOD_RES 66
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:28848569"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28848569"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:28848569"
FT MUTAGEN 36
FT /note="K->M: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:27913741"
SQ SEQUENCE 342 AA; 37553 MW; 1DCDE1978DD920D4 CRC64;
MEWVRGETIG FGTFSTVSTA TKSRNSGDFP ALIAVKSTDA YGAASLSNEK SVLDSLGDCP
EIIRCYGEDS TVENGEEMHN LLLEYASRGS LASYMKKLGG EGLPESTVRR HTGSVLRGLR
HIHAKGFAHC DIKLANILLF NDGSVKIADF GLAMRVDGDL TALRKSVEIR GTPLYMAPEC
VNDNEYGSAA DVWALGCAVV EMFSGKTAWS VKEGSHFMSL LIRIGVGDEL PKIPEMLSEE
GKDFLSKCFV KDPAKRWTAE MLLNHSFVTI DLEDDHRENF VVKVKDEDKV LMSPKCPFEF
DDWDSFTLDS NPSFDSPVER LGSLVSGSIP DWSVGGSWLT VR
