MPK7_ARATH
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 03-AUG-2022, entry version 172.
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; 2.
DR STRING; 3702.AT2G18170.1; -.
DR iPTMnet; Q39027; -.
DR PaxDb; Q39027; -.
DR PRIDE; Q39027; -.
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; locus:2053119; AT2G18170.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q39027; -.
DR OMA; AEPMIRE; -.
DR OrthoDB; 741207at2759; -.
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 Genevisible; Q39027; 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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:TAIR.
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 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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
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
