ID   MPK11_ARATH             Reviewed;         369 AA.
AC   Q9LMM5; B3H762;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Mitogen-activated protein kinase 11;
DE            Short=AtMPK11;
DE            Short=MAP kinase 11;
DE            EC=2.7.11.24;
GN   Name=MPK11; OrderedLocusNames=At1g01560; ORFNames=F22L4.10;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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] (ISOFORM 2).
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).
RN   [6]
RP   INTERACTION WITH MKK1; MKK2 AND MKK6.
RX   PubMed=19513235; DOI=10.4161/psb.3.12.6848;
RA   Lee J.S., Huh K.W., Bhargava A., Ellis B.E.;
RT   "Comprehensive analysis of protein-protein interactions between Arabidopsis
RT   MAPKs and MAPK kinases helps define potential MAPK signalling modules.";
RL   Plant Signal. Behav. 3:1037-1041(2008).
RN   [7]
RP   INTERACTION WITH MKK6.
RX   PubMed=21575092; DOI=10.1111/j.1365-313x.2011.04642.x;
RA   Zeng Q., Chen J.G., Ellis B.E.;
RT   "AtMPK4 is required for male-specific meiotic cytokinesis in Arabidopsis.";
RL   Plant J. 67:895-906(2011).
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   -!- SUBUNIT: Interacts with MKK1, MKK2 and MKK6.
CC       {ECO:0000269|PubMed:19513235, ECO:0000269|PubMed:21575092}.
CC   -!- INTERACTION:
CC       Q9LMM5; Q94A06: MKK1; NbExp=2; IntAct=EBI-2358699, EBI-994464;
CC       Q9LMM5; Q9S7U9: MKK2; NbExp=2; IntAct=EBI-2358699, EBI-994350;
CC       Q9LMM5; Q9M4B5: PFD4; NbExp=3; IntAct=EBI-2358699, EBI-2130809;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9LMM5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LMM5-2; Sequence=VSP_035539, VSP_035540;
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-198 and Tyr-200, which activates the
CC       enzyme. {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to introns retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR   EMBL; AC061957; AAF81314.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27305.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27306.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM59779.1; -; Genomic_DNA.
DR   EMBL; BX815051; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; C86146; C86146.
DR   RefSeq; NP_001117210.1; NM_001123738.2. [Q9LMM5-1]
DR   RefSeq; NP_001322113.1; NM_001331282.1. [Q9LMM5-2]
DR   RefSeq; NP_563631.2; NM_100038.4. [Q9LMM5-2]
DR   AlphaFoldDB; Q9LMM5; -.
DR   SMR; Q9LMM5; -.
DR   BioGRID; 24758; 3.
DR   IntAct; Q9LMM5; 4.
DR   STRING; 3702.Q9LMM5; -.
DR   iPTMnet; Q9LMM5; -.
DR   PaxDb; 3702-AT1G01560-2; -.
DR   ProteomicsDB; 250948; -. [Q9LMM5-1]
DR   EnsemblPlants; AT1G01560.1; AT1G01560.1; AT1G01560. [Q9LMM5-2]
DR   EnsemblPlants; AT1G01560.2; AT1G01560.2; AT1G01560. [Q9LMM5-1]
DR   EnsemblPlants; AT1G01560.4; AT1G01560.4; AT1G01560. [Q9LMM5-2]
DR   GeneID; 839523; -.
DR   Gramene; AT1G01560.1; AT1G01560.1; AT1G01560. [Q9LMM5-2]
DR   Gramene; AT1G01560.2; AT1G01560.2; AT1G01560. [Q9LMM5-1]
DR   Gramene; AT1G01560.4; AT1G01560.4; AT1G01560. [Q9LMM5-2]
DR   KEGG; ath:AT1G01560; -.
DR   Araport; AT1G01560; -.
DR   TAIR; AT1G01560; MPK11.
DR   eggNOG; KOG0660; Eukaryota.
DR   InParanoid; Q9LMM5; -.
DR   OMA; WKEELIY; -.
DR   OrthoDB; 5474493at2759; -.
DR   PhylomeDB; Q9LMM5; -.
DR   PRO; PR:Q9LMM5; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LMM5; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR   CDD; cd07858; STKc_TEY_MAPK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR   PANTHER; PTHR24055:SF439; MITOGEN-ACTIVATED PROTEIN KINASE 11-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; Q9LMM5; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..369
FT                   /note="Mitogen-activated protein kinase 11"
FT                   /id="PRO_0000245811"
FT   DOMAIN          40..326
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOTIF           198..200
FT                   /note="TXY"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         46..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         198
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q39026"
FT   MOD_RES         200
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q39026"
FT   MOD_RES         203
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q39026"
FT   VAR_SEQ         256..275
FT                   /note="LIGSPDDSSLGFLRSDNARR -> VNFSLFHLTILFRFNLKKEH (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14993207"
FT                   /id="VSP_035539"
FT   VAR_SEQ         276..369
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14993207"
FT                   /id="VSP_035540"
FT   CONFLICT        13
FT                   /note="N -> D (in Ref. 3; BX815051)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   369 AA;  42475 MW;  446673DB42C3DAA6 CRC64;
     MSIEKPFFGD DSNRGVSING GRYVQYNVYG NLFEVSKKYV PPLRPIGRGA SGIVCAAWNS
     ETGEEVAIKK IGNAFGNIID AKRTLREIKL LKHMDHDNVI AIIDIIRPPQ PDNFNDVHIV
     YELMDTDLHH IIRSNQPLTD DHSRFFLYQL LRGLKYVHSA NVLHRDLKPS NLLLNANCDL
     KIGDFGLART KSETDFMTEY VVTRWYRAPE LLLNCSEYTA AIDIWSVGCI LGEIMTREPL
     FPGRDYVQQL RLITELIGSP DDSSLGFLRS DNARRYVRQL PQYPRQNFAA RFPNMSVNAV
     DLLQKMLVFD PNRRITVDEA LCHPYLAPLH EYNEEPVCVR PFHFDFEQPS LTEENIKELI
     YRESVKFNP
//