MPK19_ARATH
ID MPK19_ARATH Reviewed; 598 AA.
AC Q9LUC3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Mitogen-activated protein kinase 19;
DE Short=AtMPK19;
DE Short=MAP kinase 19;
DE EC=2.7.11.24;
GN Name=MPK19; OrderedLocusNames=At3g14720; ORFNames=MIE1.22;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 518-598.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
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 [5]
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).
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 -!- 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;
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9LUC3; O80931: AS1; NbExp=3; IntAct=EBI-25512843, EBI-763232;
CC Q9LUC3; O23160: MYB73; NbExp=3; IntAct=EBI-25512843, EBI-25506855;
CC Q9LUC3; Q9SLH3: RGA; NbExp=3; IntAct=EBI-25512843, EBI-963624;
CC Q9LUC3; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-25512843, EBI-15192297;
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-187 and Tyr-189, which activates the
CC enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02403.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB023038; BAB02403.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75559.1; -; Genomic_DNA.
DR EMBL; BX824157; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_188090.2; NM_112333.3.
DR AlphaFoldDB; Q9LUC3; -.
DR SMR; Q9LUC3; -.
DR BioGRID; 6034; 4.
DR IntAct; Q9LUC3; 4.
DR STRING; 3702.AT3G14720.1; -.
DR PaxDb; Q9LUC3; -.
DR PRIDE; Q9LUC3; -.
DR ProteomicsDB; 239072; -.
DR EnsemblPlants; AT3G14720.1; AT3G14720.1; AT3G14720.
DR GeneID; 820700; -.
DR Gramene; AT3G14720.1; AT3G14720.1; AT3G14720.
DR KEGG; ath:AT3G14720; -.
DR Araport; AT3G14720; -.
DR TAIR; locus:2089576; AT3G14720.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_13_1; -.
DR InParanoid; Q9LUC3; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; Q9LUC3; -.
DR PRO; PR:Q9LUC3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUC3; baseline and differential.
DR Genevisible; Q9LUC3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; ISS: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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 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.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..598
FT /note="Mitogen-activated protein kinase 19"
FT /id="PRO_0000245819"
FT DOMAIN 25..316
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 396..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 187..189
FT /note="TXY"
FT COMPBIAS 415..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 189
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 192
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
SQ SEQUENCE 598 AA; 67408 MW; 32C11D790A966F85 CRC64;
MQKTQEKKNM KEMEFFTEYG DANRYRILEV IGKGSYGVVC AAIDTQTGEK VAIKKINDVF
EHVSDALRIL REVKLLRLLR HPDIVEIKSI MLPPSKREFK DIYVVFELME SDLHQVIKAN
DDLTREHHQF FLYQMLRALK YMHTANVYHR DLKPKNILAN ANCKLKVCDF GLARVSFNDT
PTTVFWTDYV ATRWYRAPEL CGSFCSKYTP AIDIWSIGCI FAEVLTGKPL FPGKSVVHQL
DLITDLLGTP KSETIAGVRN EKARKYLNEM RKKNLVPFSQ KFPNADPLAL RLLQRLLAFD
PKDRPTAAEA LADPYFKCLA KVEREPSCQP ISKMEFEFER RRLTKDDIRE LIYREILEYH
PQLLKDYMNS EGSSFLYPSA IGHLRKQFAY LEENSGKSGP VIPPDRKHAS LPRSAVHSSA
VNSNAQPSLN ASDSRRVSIE PSRNGVVPST SAYSTKPLGP PPRVPSGKPG RVVESSVTYE
NDRNLKESSY DARTSYYRST VLPPQTVSPN CYFLPNTMNQ EKRSGTEAAS QPKPQFVPTQ
CNSAKPAELN PNPYVQSQHK VGIDAKLLHA QSQYGPAGAA AVAVAAHRNI GAVGYGMS
