ID MPK13_ORYSJ Reviewed; 506 AA. AC Q0E459; Q6QUV9; Q6Z831; Q9SE22; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 101. DE RecName: Full=Mitogen-activated protein kinase 13; DE Short=MAP kinase 13; DE EC=2.7.11.24; DE AltName: Full=Benzothiadiazole-induced MAP kinase 2; DE AltName: Full=MAP kinase 2; DE AltName: Full=OsBIMK2; DE AltName: Full=OsBWMK2; DE AltName: Full=OsMAPK2; DE AltName: Full=OsMPK17-2; DE AltName: Full=Wound- and blast-induced MAPK 2; GN Name=MPK13; Synonyms=BIMK2, BWMK2, MAPK2, MPK17-2; GN OrderedLocusNames=Os02g0135200, LOC_Os02g04230; ORFNames=P0585B01.25; 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]. RA Cheong Y.H., Moon B.C., Kim J.K., Cho M.J.; RT "Novel plant MAP kinases phosphorylate defense-related transcription RT factors."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Aichi asahi; RA Wang D.-P., Zhao W.-S., Wang M., Meng X.-B., Lin R.-M., Zhang S.-H., RA Peng Y.-L.; RT "Oryza sativa (japonica cultivar-group) wound and blast induced MAPK RT (BWMK2) mRNA."; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [3] 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 [4] 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 [5] 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 [6] 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 -!- INDUCTION: By salicylic acid (SA), ethylene and infection with rice CC blast fungus (M.grisea). {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-175 and Tyr-177, 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=AAF23903.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF194416; AAF23903.1; ALT_FRAME; mRNA. DR EMBL; AY588939; AAT00625.1; -; mRNA. DR EMBL; AP004799; BAD10093.1; -; Genomic_DNA. DR EMBL; AP008208; BAF07729.1; -; Genomic_DNA. DR EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_015626451.1; XM_015770965.1. DR RefSeq; XP_015626452.1; XM_015770966.1. DR RefSeq; XP_015626453.1; XM_015770967.1. DR RefSeq; XP_015626454.1; XM_015770968.1. DR AlphaFoldDB; Q0E459; -. DR SMR; Q0E459; -. DR STRING; 39947.Q0E459; -. DR PaxDb; 39947-Q0E459; -. DR EnsemblPlants; Os02t0135200-01; Os02t0135200-01; Os02g0135200. DR GeneID; 4328223; -. DR Gramene; Os02t0135200-01; Os02t0135200-01; Os02g0135200. DR KEGG; osa:4328223; -. DR eggNOG; KOG0660; Eukaryota. DR InParanoid; Q0E459; -. DR OrthoDB; 1032011at2759; -. DR Proteomes; UP000000763; Chromosome 2. DR Proteomes; UP000059680; Chromosome 2. 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:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd07859; STKc_TDY_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 PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1. DR PANTHER; PTHR24055:SF429; MITOGEN-ACTIVATED PROTEIN KINASE 13; 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. PE 2: Evidence at transcript level; KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..506 FT /note="Mitogen-activated protein kinase 13" FT /id="PRO_0000239756" FT DOMAIN 13..304 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 384..421 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 175..177 FT /note="TXY" FT COMPBIAS 384..401 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 139 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 19..27 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 42 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 175 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" FT MOD_RES 177 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250" SQ SEQUENCE 506 AA; 58281 MW; 7EBCBA768079F972 CRC64; MEFFTEYGEA SQYQIQEVVG KGSYGVVAAA VDTHTGERVA IKKINDVFEH VSDAIRILRE IKVLRLLRHP DIVVIKHIML PPTRREFRDI YVVFELMESD LHQVIEANHD LSPEHHRFFL YQLLCALKYI HSANVFHRDL KPKNILANSD CKLKICDFGL ARVAFNDSPS TIFWTDYVAT RWYRAPELCG SFFSKYTPAI DIWSIGCIFA EILTGRPLFP GRNVVHQLDL ITDLLGTPSS ETLSRIRNEN ARGYLTGMQR KHPIPFSHKF HNADPLALRL LERLLAFDPK DRPTAEEALA DPYFRGISKL SREPSRLPVS KFEFEFERRK LTKDDVREMI YREILEYHPQ MLQEYIRGGE QISFLYPSGV DRFKRQFAHL EENYSRGERS TPLRRQHASL PRERVCSSVD SNNQDSDNEE RRAISSIART MISPPRSQEK GKNRASAYPN GIINLNSNPK IYLKSASISA STCIIRGNKG PKENGISEDM EEVVYELSDN VTRMLS //