MPK5_ORYSJ
ID MPK5_ORYSJ Reviewed; 369 AA.
AC Q10N20; B7EDC7; Q7FNE2; Q8GZZ3; Q8S3T6; Q9AXF2; Q9FQM3; Q9FSE6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Mitogen-activated protein kinase 5;
DE Short=MAP kinase 5;
DE EC=2.7.11.24;
DE AltName: Full=Benzothiadiazole-induced MAP kinase 1;
DE AltName: Full=MAP kinase 2;
DE AltName: Full=Multiple stress-responsive MAP kinase 2;
DE AltName: Full=OsBIMK1;
DE AltName: Full=OsMAP1;
DE AltName: Full=OsMAPK2;
DE AltName: Full=OsMAPK5;
DE AltName: Full=OsMPK3;
DE AltName: Full=OsMSRMK2;
GN Name=MPK5; Synonyms=BIMK1, MAPK2, MAPK5, MPK3, MSRMK2;
GN OrderedLocusNames=Os03g0285800, LOC_Os03g17700;
GN ORFNames=OsJ_10412 {ECO:0000312|EMBL:EEE58837.1}, OSJNBa0013D02.9;
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] (ISOFORM MAPK5A), AND INDUCTION.
RC STRAIN=cv. Nipponbare; TISSUE=Leaf;
RX PubMed=12074577; DOI=10.1016/s0006-291x(02)00571-5;
RA Agrawal G.K., Rakwal R., Iwahashi H.;
RT "Isolation of novel rice (Oryza sativa L.) multiple stress responsive MAP
RT kinase gene, OsMSRMK2, whose mRNA accumulates rapidly in response to
RT environmental cues.";
RL Biochem. Biophys. Res. Commun. 294:1009-1016(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MAPK5A), ACTIVITY REGULATION,
RP INTERACTION WITH MKK1, AND INDUCTION.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MAPK5A), TISSUE SPECIFICITY, INDUCTION,
RP AND PHOSPHORYLATION.
RX PubMed=11975731; DOI=10.1034/j.1399-3054.2002.1140410.x;
RA Huang H.-J., Fu S.-F., Tai Y.-H., Chou W.-C., Huang D.-D.;
RT "Expression of Oryza sativa MAP kinase gene is developmentally regulated
RT and stress-responsive.";
RL Physiol. Plantarum 114:572-580(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MAPK5A AND MAPK5B), FUNCTION, ACTIVITY
RP REGULATION, INDUCTION, AND ALTERNATIVE SPLICING.
RX PubMed=12615946; DOI=10.1105/tpc.008714;
RA Xiong L., Yang Y.;
RT "Disease resistance and abiotic stress tolerance in rice are inversely
RT modulated by an abscisic acid-inducible mitogen-activated protein kinase.";
RL Plant Cell 15:745-759(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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).
RN [12]
RP FUNCTION, INTERACTION WITH CPK18, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-14 AND THR-32, AND MUTAGENESIS OF THR-14; THR-32 AND LYS-65.
RX PubMed=25035404; DOI=10.1105/tpc.114.126441;
RA Xie K., Chen J., Wang Q., Yang Y.;
RT "Direct phosphorylation and activation of a mitogen-activated protein
RT kinase by a calcium-dependent protein kinase in rice.";
RL Plant Cell 26:3077-3089(2014).
CC -!- FUNCTION: Involved in disease resistance and abiotic stress tolerance
CC signaling pathways. Acts as a positive regulator of drought, salt and
CC cold tolerance. Negatively modulates pathogenesis-related (PR) gene
CC expression and broad-spectrum disease resistance (PubMed:12615946).
CC Functions downstream of CPK18 in a signaling pathway that represses
CC defense gene expression and negatively regulates resistance to rice
CC blast fungus. Phosphorylated by CPK18 at Thr-14 and Thr-32 and
CC activated independently of MAP kinase kinase (MKK) phosphorylation
CC (PubMed:25035404). {ECO:0000269|PubMed:12615946,
CC ECO:0000269|PubMed:25035404}.
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 (By similarity). Activated in response to low
CC temperature (12 degrees Celsius) treatment (PubMed:12177502,
CC PubMed:12615946). Activated by phosphorylation at Thr-14 and Thr-32 by
CC CPK18 (PubMed:25035404). {ECO:0000250, ECO:0000269|PubMed:12177502,
CC ECO:0000269|PubMed:12615946, ECO:0000269|PubMed:25035404}.
CC -!- SUBUNIT: Interacts with MKK1 (PubMed:12177502). Interacts with CPK18
CC (PubMed:25035404). {ECO:0000269|PubMed:12177502,
CC ECO:0000269|PubMed:25035404}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25035404}. Cytoplasm
CC {ECO:0000269|PubMed:25035404}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=MAPK5a;
CC IsoId=Q10N20-1, Q7FNE2-1;
CC Sequence=Displayed;
CC Name=MAPK5b;
CC IsoId=Q10N20-2, Q7FNE2-2;
CC Sequence=VSP_019261;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and panicles, and at
CC lower levels in leaves. {ECO:0000269|PubMed:11975731}.
CC -!- INDUCTION: By benzothiadiazole (BTH), dichloroisonicotinic acid,
CC probenazole, jasmonic acid, wounding and infection with P.syringae and
CC M.grisea, by stresses, hormones, heavy metals, high/low temperature,
CC UV-C and phosphatase inhibitors. {ECO:0000269|PubMed:11975731,
CC ECO:0000269|PubMed:12074577, ECO:0000269|PubMed:12177502,
CC ECO:0000269|PubMed:12615946, 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 at Thr-194 and Tyr-196, which activates the
CC enzyme (By similarity). Autophosphorylated. Phosphorylated by CPK18 at
CC Thr-14 and Thr-32, which activates the enzyme (PubMed:25035404).
CC {ECO:0000250, ECO:0000269|PubMed:25035404}.
CC -!- MISCELLANEOUS: [Isoform MAPK5b]: Does not possess kinase activity.
CC {ECO:0000305}.
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=AAO16999.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ486975; CAD31224.1; -; mRNA.
DR EMBL; AF216315; AAG40579.1; -; mRNA.
DR EMBL; AJ250311; CAC13967.1; -; mRNA.
DR EMBL; AF479883; AAL87689.1; -; mRNA.
DR EMBL; AF479884; AAL87690.1; -; mRNA.
DR EMBL; AC134232; AAO16999.1; ALT_INIT; Genomic_DNA.
DR EMBL; DP000009; ABF95354.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11684.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83624.1; -; Genomic_DNA.
DR EMBL; CM000140; EEE58837.1; -; Genomic_DNA.
DR EMBL; AK067339; BAG90374.1; -; mRNA.
DR EMBL; AK104834; BAG96983.1; -; mRNA.
DR RefSeq; XP_015630496.1; XM_015775010.1. [Q10N20-1]
DR AlphaFoldDB; Q10N20; -.
DR SMR; Q10N20; -.
DR IntAct; Q10N20; 2.
DR MINT; Q10N20; -.
DR STRING; 4530.OS03T0285800-01; -.
DR iPTMnet; Q10N20; -.
DR PaxDb; Q10N20; -.
DR PRIDE; Q10N20; -.
DR EnsemblPlants; Os03t0285800-01; Os03t0285800-01; Os03g0285800. [Q10N20-1]
DR EnsemblPlants; Os03t0285800-02; Os03t0285800-02; Os03g0285800. [Q10N20-1]
DR GeneID; 4332475; -.
DR Gramene; Os03t0285800-01; Os03t0285800-01; Os03g0285800. [Q10N20-1]
DR Gramene; Os03t0285800-02; Os03t0285800-02; Os03g0285800. [Q10N20-1]
DR KEGG; osa:4332475; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q10N20; -.
DR OMA; MDIPRPE; -.
DR OrthoDB; 741207at2759; -.
DR PlantReactome; R-OSA-9675508; Root elongation.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q10N20; OS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:1901002; P:positive regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR008351; MAPK_JNK.
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 PRINTS; PR01772; JNKMAPKINASE.
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 Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..369
FT /note="Mitogen-activated protein kinase 5"
FT /id="PRO_0000239748"
FT DOMAIN 36..322
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 194..196
FT /note="TXY"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 42..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:25035404"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:25035404"
FT MOD_RES 194
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 196
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 70..173
FT /note="Missing (in isoform MAPK5b)"
FT /evidence="ECO:0000303|PubMed:12615946"
FT /id="VSP_019261"
FT MUTAGEN 14
FT /note="T->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:25035404"
FT MUTAGEN 32
FT /note="T->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:25035404"
FT MUTAGEN 65
FT /note="K->R: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:25035404"
FT CONFLICT 46
FT /note="A -> G (in Ref. 3; CAC13967)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="H -> L (in Ref. 3; CAC13967)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 42995 MW; 417D81732635F2D3 CRC64;
MDGAPVAEFR PTMTHGGRYL LYDIFGNKFE VTNKYQPPIM PIGRGAYGIV CSVMNFETRE
MVAIKKIANA FNNDMDAKRT LREIKLLRHL DHENIIGIRD VIPPPIPQAF NDVYIATELM
DTDLHHIIRS NQELSEEHCQ YFLYQILRGL KYIHSANVIH RDLKPSNLLL NANCDLKICD
FGLARPSSES DMMTEYVVTR WYRAPELLLN STDYSAAIDV WSVGCIFMEL INRQPLFPGR
DHMHQMRLIT EVIGTPTDDE LGFIRNEDAR KYMRHLPQYP RRTFASMFPR VQPAALDLIE
RMLTFNPLQR ITVEEALDHP YLERLHDIAD EPICLEPFSF DFEQKALNED QMKQLIFNEA
IEMNPNIRY
