MPK9_ARATH
ID MPK9_ARATH Reviewed; 510 AA.
AC Q9LV37; Q9MB22;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Mitogen-activated protein kinase 9;
DE Short=AtMPK9;
DE Short=MAP kinase 9;
DE EC=2.7.11.24;
GN Name=MPK9; OrderedLocusNames=At3g18040; ORFNames=MRC8.2, MRC8.4;
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;
RA Mizoguchi T., Ichimura K., Shinozaki K.;
RT "Arabidopsis thaliana mRNA for MAP kinase.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LV37-1; Sequence=Displayed;
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-185 and Tyr-187, 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=BAB02016.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB038694; BAA92223.1; -; mRNA.
DR EMBL; AB020749; BAB02016.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE76038.1; -; Genomic_DNA.
DR RefSeq; NP_001327298.1; NM_001338320.1.
DR RefSeq; NP_566595.1; NM_112686.4. [Q9LV37-1]
DR AlphaFoldDB; Q9LV37; -.
DR SMR; Q9LV37; -.
DR BioGRID; 6662; 2.
DR STRING; 3702.AT3G18040.1; -.
DR iPTMnet; Q9LV37; -.
DR PaxDb; Q9LV37; -.
DR PRIDE; Q9LV37; -.
DR ProteomicsDB; 250949; -. [Q9LV37-1]
DR EnsemblPlants; AT3G18040.1; AT3G18040.1; AT3G18040. [Q9LV37-1]
DR GeneID; 821329; -.
DR Gramene; AT3G18040.1; AT3G18040.1; AT3G18040. [Q9LV37-1]
DR KEGG; ath:AT3G18040; -.
DR Araport; AT3G18040; -.
DR TAIR; locus:2092717; AT3G18040.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_5_1; -.
DR InParanoid; Q9LV37; -.
DR PhylomeDB; Q9LV37; -.
DR PRO; PR:Q9LV37; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LV37; baseline and differential.
DR Genevisible; Q9LV37; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..510
FT /note="Mitogen-activated protein kinase 9"
FT /id="PRO_0000245809"
FT DOMAIN 23..314
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 393..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 185..187
FT /note="TXY"
FT COMPBIAS 412..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 187
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 190
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT CONFLICT 46
FT /note="G -> C (in Ref. 1; BAA92223)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="I -> S (in Ref. 1; BAA92223)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="E -> D (in Ref. 1; BAA92223)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="T -> N (in Ref. 1; BAA92223)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="I -> L (in Ref. 1; BAA92223)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="T -> Q (in Ref. 1; BAA92223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 58395 MW; 6E41FB646C3C7F12 CRC64;
MDPHKKVALE TEFFTEYGEA SRYQIQEVIG KGSYGVVASA IDTHSGEKVA IKKINDVFEH
VSDATRILRE IKLLRLLRHP DIVEIKHVML PPSRREFRDI YVVFELMESD LHQVIKANDD
LTPEHYQFFL YQLLRGLKFI HTANVFHRDL KPKNILANSD CKLKICDFGL ARVSFNDAPS
AIFWTDYVAT RWYRAPELCG SFFSKYTPAI DIWSIGCIFA EMLTGKPLFP GKNVVHQLDI
MTDLLGTPPP EAIARIRNEK ARRYLGNMRR KPPVPFTHKF PHVDPLALRL LHRLLAFDPK
DRPSAEEALA DPYFYGLANV DREPSTQPIP KLEFEFERRK ITKEDVRELI YREILEYHPQ
MLQEYLRGGE QTSFMYPSGV DRFKRQFAHL EENYGKGEKG SPLQRQHASL PRERVPAPKK
ENGSHNHDIE NRSIASLVTT LESPPTSQHE GSDYRNGTSQ TGYSARSLLK SASISASKCI
GMKPRNKSEY GESNNDTVDA LSQKVAALHT
