M3K17_ARATH
ID M3K17_ARATH Reviewed; 372 AA.
AC O80888;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 17 {ECO:0000303|PubMed:25720833};
DE EC=2.7.11.25 {ECO:0000250|UniProtKB:Q9ZVP5, ECO:0000255|PROSITE-ProRule:PRU00159};
GN Name=MAPKKK17 {ECO:0000303|PubMed:25720833};
GN OrderedLocusNames=At2g32510 {ECO:0000312|Araport:AT2G32510};
GN ORFNames=T26B15.7 {ECO:0000312|EMBL:AAC25933.1};
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=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 [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 ABSCISIC ACID AND OSMOTIC
RP STRESSES, AND INTERACTION WITH MKK3.
RC STRAIN=cv. Columbia;
RX PubMed=25720833; DOI=10.1111/tpj.12808;
RA Danquah A., de Zelicourt A., Boudsocq M., Neubauer J., Frei Dit Frey N.,
RA Leonhardt N., Pateyron S., Gwinner F., Tamby J.P., Ortiz-Masia D.,
RA Marcote M.J., Hirt H., Colcombet J.;
RT "Identification and characterization of an ABA-activated MAP kinase cascade
RT in Arabidopsis thaliana.";
RL Plant J. 82:232-244(2015).
CC -!- FUNCTION: Component of the abscisic acid (ABA) signaling pathway that
CC may act as ABA signal transducer in the context of abiotic stresses.
CC Triggers MPK7 activation in a MKK3-dependent manner. Mediates the ABA-
CC dependent activation of the MKK3-MPK7 module.
CC {ECO:0000269|PubMed:25720833}.
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:0000250|UniProtKB:Q9ZVP5, ECO:0000255|PROSITE-
CC ProRule:PRU00159};
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:0000250|UniProtKB:Q9ZVP5,
CC ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- SUBUNIT: Binds to MKK3. {ECO:0000269|PubMed:25720833}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ZVP5}.
CC -!- INDUCTION: Strongly induced by abscisic acid (ABA). Accumulates in
CC response to osmotic stresses (e.g. mannitol and NaCl).
CC {ECO:0000269|PubMed:25720833}.
CC -!- DISRUPTION PHENOTYPE: In the double mutant map3k17 map3k18, impaired
CC MPK7 activation mediated by abscisic acid (ABA).
CC {ECO:0000269|PubMed:25720833}.
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; AC004681; AAC25933.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08695.1; -; Genomic_DNA.
DR PIR; T02550; T02550.
DR RefSeq; NP_180810.1; NM_128810.2.
DR AlphaFoldDB; O80888; -.
DR SMR; O80888; -.
DR STRING; 3702.AT2G32510.1; -.
DR PaxDb; O80888; -.
DR PRIDE; O80888; -.
DR EnsemblPlants; AT2G32510.1; AT2G32510.1; AT2G32510.
DR GeneID; 817812; -.
DR Gramene; AT2G32510.1; AT2G32510.1; AT2G32510.
DR KEGG; ath:AT2G32510; -.
DR Araport; AT2G32510; -.
DR TAIR; locus:2060246; AT2G32510.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; O80888; -.
DR OMA; CYSERIG; -.
DR OrthoDB; 801642at2759; -.
DR PhylomeDB; O80888; -.
DR PRO; PR:O80888; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80888; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
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; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..372
FT /note="Mitogen-activated protein kinase kinase kinase 17"
FT /id="PRO_0000440622"
FT DOMAIN 3..259
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 9..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O23304"
SQ SEQUENCE 372 AA; 41235 MW; 849A872E40CDB650 CRC64;
MEWTRGRILG RGSTATVYAA AGHNSDEILA VKSSEVHRSE FLQREAKILS SLSSPYVIGY
RGSETKRESN GVVMYNLLME YAPYGTLTDA AAKDGGRVDE TRVVKYTRDI LKGLEYIHSK
GIVHCDVKGS NVVISEKGEA KIADFGCAKR VDPVFESPVM GTPAFMAPEV ARGEKQGKES
DIWAVGCTMI EMVTGSPPWT KADSREDPVS VLYRVGYSSE TPELPCLLAE EAKDFLEKCL
KREANERWTA TQLLNHPFLT TKPDIEPVLV PGLISNSPTS VTDQTFWRSV EEEEEEETEE
IQKDSRDLDR LSLWGCYSER IGRLKCVGGL DGTRCDMEGG DWIMVRARCE GTMISGSQKE
LIISENVLVG EL
