ID MPK11_ORYSJ Reviewed; 570 AA. AC Q5VN19; Q0DC96; Q5VN20; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 2. DT 24-JAN-2024, entry version 117. DE RecName: Full=Mitogen-activated protein kinase 11; DE Short=MAP kinase 11; DE EC=2.7.11.24; GN Name=MPK11; OrderedLocusNames=Os06g0367900, LOC_Os06g26340; GN ORFNames=OSJNBa0015G09.36-1, OSJNBa0015G09.36-2; 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 [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 [2] 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). 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 [5] RP 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5VN19-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5VN19-2; Sequence=VSP_019262, VSP_019263; CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues CC whose phosphorylation activates the MAP kinases. CC -!- PTM: Dually phosphorylated on Thr-188 and Tyr-190, 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 --------------------------------------------------------------------------- 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; AP005763; BAD69155.1; -; Genomic_DNA. DR EMBL; AP005763; BAD69156.1; -; Genomic_DNA. DR EMBL; AP008212; BAF19527.1; -; Genomic_DNA. DR EMBL; AP014962; BAS97726.1; -; Genomic_DNA. DR EMBL; AP014962; BAS97727.1; -; Genomic_DNA. DR EMBL; AK065641; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK066968; BAG90204.1; -; mRNA. DR EMBL; AK100081; BAG94435.1; -; mRNA. DR RefSeq; XP_015643951.1; XM_015788465.1. DR RefSeq; XP_015643953.1; XM_015788467.1. DR AlphaFoldDB; Q5VN19; -. DR SMR; Q5VN19; -. DR STRING; 39947.Q5VN19; -. DR PaxDb; 39947-Q5VN19; -. DR EnsemblPlants; Os06t0367900-01; Os06t0367900-01; Os06g0367900. [Q5VN19-1] DR EnsemblPlants; Os06t0367900-02; Os06t0367900-02; Os06g0367900. [Q5VN19-2] DR GeneID; 4341010; -. DR Gramene; Os06t0367900-01; Os06t0367900-01; Os06g0367900. [Q5VN19-1] DR Gramene; Os06t0367900-02; Os06t0367900-02; Os06g0367900. [Q5VN19-2] DR KEGG; osa:4341010; -. DR eggNOG; KOG0660; Eukaryota. DR HOGENOM; CLU_000288_181_5_1; -. DR InParanoid; Q5VN19; -. DR OMA; QIQGVHA; -. DR OrthoDB; 1032011at2759; -. DR Proteomes; UP000000763; Chromosome 6. DR Proteomes; UP000059680; Chromosome 6. DR ExpressionAtlas; Q5VN19; baseline and differential. 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:SF456; MITOGEN-ACTIVATED PROTEIN KINASE 11; 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 Genevisible; Q5VN19; OS. PE 2: Evidence at transcript level; KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; KW Transferase. FT CHAIN 1..570 FT /note="Mitogen-activated protein kinase 11" FT /id="PRO_0000239754" FT DOMAIN 26..317 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOTIF 188..190 FT /note="TXY" FT ACT_SITE 152 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 32..40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 55 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 188 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" FT MOD_RES 190 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250" FT VAR_SEQ 416..421 FT /note="STIVHS -> RAFNYR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12869764" FT /id="VSP_019262" FT VAR_SEQ 422..570 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12869764" FT /id="VSP_019263" SQ SEQUENCE 570 AA; 64524 MW; 56B9FDFF251177ED CRC64; MQTSNFRKKN AAEVDFFMGY GDVNRYEVLE VIGKGSYGLV CSANDIHTGE KVAIKKIHNI FEHISDAARI LREIKLLRLL RHPDIVEIKH IMLPPSKMDF RDIYVVFELM ESDLHQVIKA NDDLTREHYQ FFLYQMLRAL KYIHTANVYH RDLKPKNILA NANCKLKICD FGLARVAFTD APTTVFWTDY VATRWYRAPE LCGSFYSKYT PAIDIWSIGC IFAEVLIGKP LFPGKNVVHQ LDLITDLLGT PSLDAISQVR NDKARKYLTC MRKKQPASFS HKFLKADPLA LQLLRKLLAF DPKDRPSAQE ALADPYFNGL AKVEREPSCQ PIPKMEFEFE RRRATKEDIK ELIFQEILEY HPQLLKEHIS GTERPNFHHL SVVDQFRKQF TQVEENLNGS GAAVSLQRKH SSLPRSTIVH SAAIPAKDYK HVASSSTKLA VDGSWNAQIQ GVHANIAGEP STIVRPAVSS ERSLAPTLQW QPNMTHFLNH ALCYQNTVFS GSLLDATGPA QAIPRTTPYV DYRSGNLDLY QHHVSREDVQ SDTATAQAHA ASHGPVPAVS YSLPGTYRIT //