ID   MPK7_ARATH              Reviewed;         368 AA.
AC   Q39027; Q56W33; Q9SI14;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=Mitogen-activated protein kinase 7;
DE            Short=AtMPK7;
DE            Short=MAP kinase 7;
DE            EC=2.7.11.24;
GN   Name=MPK7; OrderedLocusNames=At2g18170; ORFNames=F8D23;
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;
RX   PubMed=8282107; DOI=10.1016/0014-5793(93)80852-l;
RA   Mizoguchi T., Hayashida N., Yamaguchi-Shinozaki K., Kamada H.,
RA   Shinozaki K.;
RT   "ATMPKs: a gene family of plant MAP kinases in Arabidopsis thaliana.";
RL   FEBS Lett. 336:440-444(1993).
RN   [2]
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   [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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
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   [7]
RP   INTERACTION WITH MKK3, ACTIVITY REGULATION, AND FUNCTION.
RX   PubMed=17933903; DOI=10.1105/tpc.106.050039;
RA   Doczi R., Brader G., Pettko-Szandtner A., Rajh I., Djamei A., Pitzschke A.,
RA   Teige M., Hirt H.;
RT   "The Arabidopsis mitogen-activated protein kinase kinase MKK3 is upstream
RT   of group C mitogen-activated protein kinases and participates in pathogen
RT   signaling.";
RL   Plant Cell 19:3266-3279(2007).
RN   [8]
RP   INTERACTION WITH MKK3.
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   [9]
RP   ACTIVITY REGULATION.
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).
RN   [10]
RP   INTERACTION WITH MKK3.
RC   STRAIN=cv. Columbia;
RX   PubMed=25680457; DOI=10.1007/s11103-015-0295-0;
RA   Matsuoka D., Yasufuku T., Furuya T., Nanmori T.;
RT   "An abscisic acid inducible Arabidopsis MAPKKK, MAPKKK18 regulates leaf
RT   senescence via its kinase activity.";
RL   Plant Mol. Biol. 87:565-575(2015).
CC   -!- FUNCTION: MKK3-MPK7 module acts as a positive regulator of PR1 gene
CC       expression. {ECO:0000269|PubMed:17933903}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC       phosphorylation (By similarity). Activated in response to hydrogen
CC       peroxide. Activation is triggered by MAPKKK17 and MAPKKK18 in a MKK3-
CC       dependent manner (PubMed:25720833). {ECO:0000250,
CC       ECO:0000269|PubMed:17933903, ECO:0000269|PubMed:25720833}.
CC   -!- SUBUNIT: Interacts with MKK3. {ECO:0000269|PubMed:17933903,
CC       ECO:0000269|PubMed:19513235, ECO:0000269|PubMed:25680457}.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-191 and Tyr-193, 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=BAD95376.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D21843; BAA04870.1; -; mRNA.
DR   EMBL; AC007212; AAD31349.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06734.1; -; Genomic_DNA.
DR   EMBL; AK222214; BAD95376.1; ALT_FRAME; mRNA.
DR   PIR; B84561; B84561.
DR   PIR; S40473; S40473.
DR   RefSeq; NP_179409.1; NM_127374.4.
DR   AlphaFoldDB; Q39027; -.
DR   SMR; Q39027; -.
DR   BioGRID; 1687; 100.
DR   IntAct; Q39027; 3.
DR   STRING; 3702.Q39027; -.
DR   iPTMnet; Q39027; -.
DR   PaxDb; 3702-AT2G18170-1; -.
DR   ProteomicsDB; 238274; -.
DR   EnsemblPlants; AT2G18170.1; AT2G18170.1; AT2G18170.
DR   GeneID; 816330; -.
DR   Gramene; AT2G18170.1; AT2G18170.1; AT2G18170.
DR   KEGG; ath:AT2G18170; -.
DR   Araport; AT2G18170; -.
DR   TAIR; AT2G18170; MPK7.
DR   eggNOG; KOG0660; Eukaryota.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; Q39027; -.
DR   OMA; GCRNILR; -.
DR   OrthoDB; 5474493at2759; -.
DR   PhylomeDB; Q39027; -.
DR   BRENDA; 2.7.11.24; 399.
DR   PRO; PR:Q39027; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q39027; baseline and differential.
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:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IDA: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:SF401; MITOGEN-ACTIVATED PROTEIN KINASE 7; 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; Q39027; AT.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Plant defense;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..368
FT                   /note="Mitogen-activated protein kinase 7"
FT                   /id="PRO_0000186316"
FT   DOMAIN          32..319
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOTIF           191..193
FT                   /note="TXY"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         38..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         191
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q39026"
FT   MOD_RES         193
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q39026"
FT   MOD_RES         196
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q39026"
FT   CONFLICT        104
FT                   /note="S -> T (in Ref. 1; BAA04870)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303
FT                   /note="D -> E (in Ref. 1; BAA04870)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        324
FT                   /note="D -> E (in Ref. 1; BAA04870)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="S -> T (in Ref. 1; BAA04870)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        366
FT                   /note="S -> L (in Ref. 1; BAA04870)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   368 AA;  42299 MW;  64587E4CA40C1418 CRC64;
     MAMLVEPPNG IKQQGKHYYS MWQTLFEIDT KYVPIKPIGR GAYGVVCSSI NRETNERVAI
     KKIHNVFENR VDALRTLREL KLLRHVRHEN VIALKDVMLP ANRSSFKDVY LVYELMDTDL
     HQIIKSSQSL SDDHCKYFLF QLLRGLKYLH SANILHRDLK PGNLLVNANC DLKICDFGLA
     RTSQGNEQFM TEYVVTRWYR APELLLCCDN YGTSIDVWSV GCIFAEILGR KPIFPGTECL
     NQLKLIINVV GSQQESDIRF IDNPKARRFI KSLPYSRGTH LSNLYPQANP LAIDLLQRML
     VFDPTKRISV TDALLHPYMA GLFDPGSNPP AHVPISLDID ENMEEPVIRE MMWNEMLYYH
     PEAEISNA
//