MPK4_ORYSJ
ID MPK4_ORYSJ Reviewed; 369 AA.
AC Q5Z859; Q0D9T8; Q8H0P1; Q9FQM2; Q9SMA9;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Mitogen-activated protein kinase 4;
DE Short=MAP kinase 4;
DE EC=2.7.11.24;
DE AltName: Full=Multiple stress-responsive MAP kinase 3;
DE AltName: Full=OsMAP2;
DE AltName: Full=OsMSRMK3;
GN Name=MPK4; Synonyms=MAP2, MSRMK3;
GN OrderedLocusNames=Os06g0699400, LOC_Os06g48590;
GN ORFNames=OsJ_22520 {ECO:0000312|EMBL:EAZ38166.1}, P0468G03.11;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12177502; DOI=10.1104/pp.006072;
RA Wen J.-Q., Oono K., Imai R.;
RT "Two novel mitogen-activated protein signaling components, OsMEK1 and
RT OsMAP1, are involved in a moderate low-temperature signaling pathway in
RT rice.";
RL Plant Physiol. 129:1880-1891(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Nipponbare; TISSUE=Leaf;
RX PubMed=12507518; DOI=10.1016/s0006-291x(02)02868-1;
RA Agrawal G.K., Agrawal S.K., Shibato J., Iwahashi H., Rakwal R.;
RT "Novel rice MAP kinases OsMSRMK3 and OsWJUMK1 involved in encountering
RT diverse environmental stresses and developmental regulation.";
RL Biochem. Biophys. Res. Commun. 300:775-783(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang H.-J., Fu S.-F., Tai Y.-H., Huang D.-D., Kuo T.T.;
RT "Molecular cloning and expression of a MAP kinase homologue from rice.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [9]
RP INDUCTION, AND NOMENCLATURE.
RX PubMed=16673940; DOI=10.1094/mpmi-19-0530;
RA Reyna N.S., Yang Y.;
RT "Molecular analysis of the rice MAP kinase gene family in relation to
RT Magnaporthe grisea infection.";
RL Mol. Plant Microbe Interact. 19:530-540(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 -!- TISSUE SPECIFICITY: Expressed in leaves and panicles.
CC {ECO:0000269|PubMed:12507518}.
CC -!- INDUCTION: By stresses, hormones, heavy metals, phosphatase inhibitors
CC and infection with rice blast fungus (M.grisea). Down-regulated by
CC drought, high/low temperature and UV-C. {ECO:0000269|PubMed:12507518,
CC ECO:0000269|PubMed:16673940}.
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}.
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DR EMBL; AF216316; AAG40580.1; -; mRNA.
DR EMBL; AJ512642; CAD54741.1; -; mRNA.
DR EMBL; AJ251330; CAB61889.1; -; mRNA.
DR EMBL; AP004278; BAD53997.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF20385.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS99326.1; -; Genomic_DNA.
DR EMBL; CM000143; EAZ38166.1; -; Genomic_DNA.
DR EMBL; AK071376; BAG92461.1; -; mRNA.
DR RefSeq; XP_015643564.1; XM_015788078.1.
DR RefSeq; XP_015643565.1; XM_015788079.1.
DR RefSeq; XP_015643566.1; XM_015788080.1.
DR AlphaFoldDB; Q5Z859; -.
DR SMR; Q5Z859; -.
DR STRING; 4530.OS06T0699400-01; -.
DR PaxDb; Q5Z859; -.
DR PRIDE; Q5Z859; -.
DR EnsemblPlants; Os06t0699400-01; Os06t0699400-01; Os06g0699400.
DR GeneID; 4341956; -.
DR Gramene; Os06t0699400-01; Os06t0699400-01; Os06g0699400.
DR KEGG; osa:4341956; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q5Z859; -.
DR OMA; QGHAFES; -.
DR OrthoDB; 741207at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q5Z859; OS.
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; IBA:GO_Central.
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 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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transferase.
FT CHAIN 1..369
FT /note="Mitogen-activated protein kinase 4"
FT /id="PRO_0000239747"
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"
FT MOD_RES 193
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="A -> V (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="Y -> V (in Ref. 3; CAB61889)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="A -> V (in Ref. 3; CAB61889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 42244 MW; D21EBE45865CE08B CRC64;
MAMMVDPPNG MGNQGKHYYT MWQTLFEIDT KYVPIKPIGR GAYGIVCSSI NRATNEKVAI
KKINNVFDNR VDALRTLREL KLLRHLRHEN VIALKDIMMP VHRRSFKDVY LVYELMDTDL
HQIIKSSQPL SNDHCQYFLF QLLRGLKYLH SAGILHRDLK PGNLLVNANC DLKICDFGLA
RTNNTKGQFM TEYVVTRWYR APELLLCCDN YGTSIDVWSV GCIFAELLGR KPIFPGTECL
NQLKLIVNVL GTMSEADIEF IDNPKARKYI KTLPYTPGIP LTSMYPQAHP LAIDLLQKML
VFDPSKRISV TEALEHPYMS PLYDPSANPP AQVPIDLDID ENLGVDMIRE MMWQEMLHYH
PEVVAGVNM
