ID   MPK15_ORYSJ             Reviewed;         498 AA.
AC   Q53N72; B7EFP8;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Mitogen-activated protein kinase 15;
DE            Short=MAP kinase 15;
DE            EC=2.7.11.24;
GN   Name=MPK15; OrderedLocusNames=Os11g0271100, LOC_Os11g17080;
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=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(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=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].
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   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 jasmonic acid (JA) and infection with rice blast fungus
CC       (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}.
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DR   EMBL; AC135497; AAX94956.1; -; Genomic_DNA.
DR   EMBL; DP000010; ABA92667.1; -; Genomic_DNA.
DR   EMBL; AP014967; BAT13563.1; -; Genomic_DNA.
DR   EMBL; AK068981; BAG91195.1; -; mRNA.
DR   RefSeq; XP_015615372.1; XM_015759886.1.
DR   AlphaFoldDB; Q53N72; -.
DR   SMR; Q53N72; -.
DR   STRING; 39947.Q53N72; -.
DR   PaxDb; 39947-Q53N72; -.
DR   EnsemblPlants; Os11t0271100-01; Os11t0271100-01; Os11g0271100.
DR   GeneID; 4350264; -.
DR   Gramene; Os11t0271100-01; Os11t0271100-01; Os11g0271100.
DR   KEGG; osa:4350264; -.
DR   eggNOG; KOG0660; Eukaryota.
DR   HOGENOM; CLU_000288_181_5_1; -.
DR   InParanoid; Q53N72; -.
DR   OMA; QPKPEQY; -.
DR   OrthoDB; 1032011at2759; -.
DR   Proteomes; UP000000763; Chromosome 11.
DR   Proteomes; UP000059680; Chromosome 11.
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:SF158; MITOGEN-ACTIVATED PROTEIN KINASE P38A-RELATED; 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; Q53N72; 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..498
FT                   /note="Mitogen-activated protein kinase 15"
FT                   /id="PRO_0000239758"
FT   DOMAIN          13..304
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          388..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           175..177
FT                   /note="TXY"
FT   COMPBIAS        484..498
FT                   /note="Polar 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   498 AA;  56967 MW;  EBC9F67E62DF299D CRC64;
     MDFFTEYGEG NRYKIEEVIG KGSYGVVCSA LDTHTGEKVA IKKINDIFEH VSDATRILRE
     IKLLRLLRHP DIVEIKHILL PPSRREFKDI YVVFELMESD LHQVIKANDD LTPEHYQFFL
     YQLLRGLKYI HTANVFHRDL KPKNILANAD CKLKICDFGL ARVAFSDTPT AIFWTDYVAT
     RWYRAPELCG SFFSKYTPAI DIWSIGCIFA ELLTGKPLFP GKNVVHQLDI ITDLLGTPST
     EAISRIRNEK ARRYLSSMRR KKPIPFTQKF PNADPLALRL LERMLSFEPK DRPNAEEALA
     DPYFRNIANV DREPSAQPVT KLEFEFERRR ITKEDIRELI YRDILEYHPN MLREYLEGTE
     SAGFMYPSAV DHFKKQFAYL EEHYAKGSTA APPERQHNSL PRPSVLYSDD RPQNTANIAE
     DLSKCVLGDN TQKMHQGSAS VCANRVPQGG AARPGKVVGS ALRYGNCSTS TAEQYEHRRT
     DRNPALATNT VSPRGSYP
//