MPK17_ORYSJ
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 03-AUG-2022, entry version 117.
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};
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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; 4530.OS05T0576800-01; -.
DR PaxDb; Q6L5F7; -.
DR PRIDE; 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; NDLTHEH; -.
DR OrthoDB; 741207at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q6L5F7; 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 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.
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
