ID MPK17_ORYSJ Reviewed; 582 AA. AC Q6L5F7; Q0DFQ5; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 2. DT 24-JAN-2024, entry version 123. DE RecName: Full=Mitogen-activated protein kinase 17; DE Short=MAP kinase 17; DE EC=2.7.11.24; GN Name=MPK17; OrderedLocusNames=Os05g0576800, LOC_Os05g50120; GN ORFNames=OJ1126_B10.5; 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=16261349; DOI=10.1007/s00438-005-0039-y; RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J., RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F., RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.; RT "A fine physical map of the rice chromosome 5."; RL Mol. Genet. Genomics 274:337-345(2005). RN [2] 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 [3] 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 [4] 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 [5] 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 [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 ethylene and infection with rice blast fungus (M.grisea). 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-267 and Tyr-269, 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=AAT39148.1; Type=Erroneous gene model prediction; 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; AC098571; AAT39148.1; ALT_SEQ; Genomic_DNA. DR EMBL; AP008211; BAF18318.1; -; Genomic_DNA. DR EMBL; AP014961; BAS95483.1; -; Genomic_DNA. DR EMBL; AK070644; BAG92074.1; -; mRNA. DR RefSeq; XP_015637399.1; XM_015781913.1. DR RefSeq; XP_015637400.1; XM_015781914.1. DR AlphaFoldDB; Q6L5F7; -. DR SMR; Q6L5F7; -. DR STRING; 39947.Q6L5F7; -. DR PaxDb; 39947-Q6L5F7; -. DR EnsemblPlants; Os05t0576800-01; Os05t0576800-01; Os05g0576800. DR GeneID; 4339697; -. DR Gramene; Os05t0576800-01; Os05t0576800-01; Os05g0576800. DR KEGG; osa:4339697; -. DR eggNOG; KOG0660; Eukaryota. DR HOGENOM; CLU_000288_181_5_1; -. DR InParanoid; Q6L5F7; -. DR OMA; YHAKLNV; -. DR OrthoDB; 1032011at2759; -. DR Proteomes; UP000000763; Chromosome 5. DR Proteomes; UP000059680; Chromosome 5. 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:SF218; MITOGEN-ACTIVATED PROTEIN KINASE 17; 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; Q6L5F7; OS. PE 2: Evidence at transcript level; KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..582 FT /note="Mitogen-activated protein kinase 17" FT /id="PRO_0000239760" FT DOMAIN 105..396 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 22..61 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 474..502 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 542..582 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 267..269 FT /note="TXY" FT COMPBIAS 32..55 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 231 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 111..119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 134 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 267 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" FT MOD_RES 269 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250" SQ SEQUENCE 582 AA; 66487 MW; 78DCBD1DEB835292 CRC64; MGGRARSILR WLRHHRSRRV SSSSFHLTTT GDDTVKDLHD PRREDAEGDG WEEVHEGPES DPEEYIALVS EDAGTHLPVR TEPRRMDPSK KEPDFFTEYG EANRYKVSEV IGKGSYGVVA AAVDTQTGER VAIKKINDVF DHVSDATRIL REIKLLRLLR HPDIVEIKHI MLPPSRREFR DIYVIFELME SDLHQVIKAN DDLTPEHHQF FLYQLLRGMK YIHAASVFHR DLKPKNILAN ADCKLKVCDF GLARVSFNDT PSAIFWTDYV ATRWYRAPEL CGSFFSKYTP AIDIWSVGCI FAELLTGKPL FPGKNVVHQL DLMTDLLGTP SAESLAKIRN EKARRYLSNM RKKPRVPFTK KFPGVDPMAL HLLERLLAFD PKDRPSAEEA LTDPYFNGLA NSEREPIAQP ISKLEFEFEK RKLAKDDVRE LIYREILEYH PHMLQEYLRG GDQMSFMYPS GVDRFKRQFA HLEEGVSKGE KSSPQLRQNA SLPRERAIGN KHGDDEYHAK LNVGEKPCHA SVTDGISKPL MSARSLLKSE SISASKCIGE KPKQDRDQED SLTESMDETA DEVSEKVAQL KT //