ID   MPK12_ORYSJ             Reviewed;         580 AA.
AC   Q5Z9J0; Q0D9M9; Q5Z9J1; Q9SE23; Q9SPF0;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Mitogen-activated protein kinase 12;
DE            Short=MAP kinase 12;
DE            EC=2.7.11.24;
DE   AltName: Full=Blast- and wound-induced MAP kinase 1;
DE   AltName: Full=MAP kinase 1;
DE   AltName: Full=OsBWMK1;
DE   AltName: Full=OsMAPK1;
GN   Name=MPK12; Synonyms=BWMK1, MAPK1;
GN   OrderedLocusNames=Os06g0708000, LOC_Os06g49430;
GN   ORFNames=P0621D05.40-1, P0621D05.40-2;
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 [MRNA] (ISOFORM 1), ACTIVITY REGULATION, INDUCTION, AND
RP   PHOSPHORYLATION AT THR-249 AND TYR-251.
RX   PubMed=10624015; DOI=10.1094/mpmi.1999.12.12.1064;
RA   He C., Fong S.H.T., Yang D., Wang G.-L.;
RT   "BWMK1, a novel MAP kinase induced by fungal infection and mechanical
RT   wounding in rice.";
RL   Mol. Plant Microbe Interact. 12:1064-1073(1999).
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] (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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 37-580 (ISOFORM 1), FUNCTION, ACTIVITY
RP   REGULATION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH EREBP1.
RX   PubMed=12913152; DOI=10.1104/pp.103.023176;
RA   Cheong Y.H., Moon B.C., Kim J.K., Kim C.Y., Kim M.C., Kim I.H., Park C.Y.,
RA   Kim J.C., Park B.O., Koo S.C., Yoon H.W., Chung W.S., Lim C.O., Lee S.Y.,
RA   Cho M.J.;
RT   "BWMK1, a rice mitogen-activated protein kinase, locates in the nucleus and
RT   mediates pathogenesis-related gene expression by activation of a
RT   transcription factor.";
RL   Plant Physiol. 132:1961-1972(2003).
RN   [7]
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   -!- FUNCTION: May be involved in defense signaling pathway. Phosphorylates
CC       EREBP1 transcriptional activator in vitro. Enhances DNA-binding
CC       activity of EREBP1 to the GCC box element of pathogenesis-related (PR)
CC       gene promoters. {ECO:0000269|PubMed:12913152}.
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 (By similarity). Activated in response to hydrogen
CC       peroxide, salicylic acid, jasmonic acid, ethylene, fungal elicitor and
CC       infection with rice blast fungus (M.grisea). {ECO:0000250,
CC       ECO:0000269|PubMed:10624015, ECO:0000269|PubMed:12913152}.
CC   -!- SUBUNIT: Interacts with EREBP1. {ECO:0000269|PubMed:12913152}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12913152}. Nucleus
CC       {ECO:0000269|PubMed:12913152}. Note=Translocated into the nucleus in
CC       response to phosphorylation. {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5Z9J0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5Z9J0-2; Sequence=VSP_019264;
CC   -!- INDUCTION: By hydrogen peroxide, salicylic acid (SA), jasmonic acid
CC       (JA), ethylene, abscisic acid (ABA), fungal elicitor, infection with
CC       rice blast fungus (M.grisea) and wounding.
CC       {ECO:0000269|PubMed:10624015, ECO:0000269|PubMed:12913152,
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-249 and Tyr-251, which activates the
CC       enzyme (By similarity). Phosphorylated on tyrosine residue.
CC       {ECO:0000250, ECO:0000269|PubMed:10624015}.
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=AAF23902.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF177392; AAD52659.1; -; mRNA.
DR   EMBL; AP003621; BAD53616.1; -; Genomic_DNA.
DR   EMBL; AP003621; BAD53617.1; -; Genomic_DNA.
DR   EMBL; AP008212; BAF20444.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS99425.1; -; Genomic_DNA.
DR   EMBL; AK066531; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK067925; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF194415; AAF23902.1; ALT_INIT; mRNA.
DR   RefSeq; XP_015643068.1; XM_015787582.1.
DR   AlphaFoldDB; Q5Z9J0; -.
DR   SMR; Q5Z9J0; -.
DR   BioGRID; 811054; 2.
DR   STRING; 39947.Q5Z9J0; -.
DR   iPTMnet; Q5Z9J0; -.
DR   PaxDb; 39947-Q5Z9J0; -.
DR   EnsemblPlants; Os06t0708000-01; Os06t0708000-01; Os06g0708000. [Q5Z9J0-1]
DR   EnsemblPlants; Os06t0708000-02; Os06t0708000-02; Os06g0708000. [Q5Z9J0-2]
DR   EnsemblPlants; Os06t0708000-03; Os06t0708000-03; Os06g0708000. [Q5Z9J0-2]
DR   GeneID; 4342017; -.
DR   Gramene; Os06t0708000-01; Os06t0708000-01; Os06g0708000. [Q5Z9J0-1]
DR   Gramene; Os06t0708000-02; Os06t0708000-02; Os06g0708000. [Q5Z9J0-2]
DR   Gramene; Os06t0708000-03; Os06t0708000-03; Os06g0708000. [Q5Z9J0-2]
DR   KEGG; osa:4342017; -.
DR   eggNOG; KOG0660; Eukaryota.
DR   InParanoid; Q5Z9J0; -.
DR   OMA; HHKKGAP; -.
DR   OrthoDB; 1032011at2759; -.
DR   PRO; PR:Q5Z9J0; -.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
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:0006952; P:defense response; IEA:UniProtKB-KW.
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.
DR   Genevisible; Q5Z9J0; OS.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Plant defense; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..580
FT                   /note="Mitogen-activated protein kinase 12"
FT                   /id="PRO_0000239755"
FT   DOMAIN          87..378
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          18..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..506
FT                   /note="Required for kinase activity and nuclear
FT                   localization"
FT   REGION          458..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           249..251
FT                   /note="TXY"
FT   COMPBIAS        18..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..541
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        213
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         93..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         249
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000305|PubMed:10624015"
FT   MOD_RES         251
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000305|PubMed:10624015"
FT   VAR_SEQ         1..74
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12869764"
FT                   /id="VSP_019264"
FT   CONFLICT        196
FT                   /note="Q -> R (in Ref. 5; AK066531)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        367
FT                   /note="S -> P (in Ref. 1; AAD52659)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   580 AA;  65945 MW;  793AA85445857EF6 CRC64;
     MGGGGTLVDG FRRLFHRRTA SGSNQSSNAG EEAASSDLEV ADDPDLVALR SIRIRVPKRK
     MPLPVESHKK NTVEMEFFTE YGEASQYQIQ EVIGKGSYGV VAAAVDTRTG ERVAIKKIND
     VFEHVSDATR ILREIKLLRL LRHPDIVEIK HIMLPPSRRE FQDIYVVFEL MESDLHQVIR
     ANDDLTPEHY QFFLYQLLRA LKYIHAANVF HRDLKPKNIL ANSDCKLKIC DFGLARASFN
     DAPSAIFWTD YVATRWYRAP ELCGSFFSKY TPAIDIWSIG CIFAELLTGR PLFPGKNVVH
     QLDIITDLLG TPSSETLSRI RNEKARRYLS TMRKKHAVPF SQKFRNTDPL ALRLLERLLA
     FDPKDRSSAE EALADPYFAS LANVEREPSR HPISKLEFEF ERRKLTKDDV RELIYREILE
     YHPQMLQEYM KGGEQISFLY PSGVDRFKRQ FAHLEENYSK GERGSPLQRK HASLPRERVG
     VSKDGYNQQN TNDQERSADS VARTTVSPPM SQDAQQHGSA GQNGVTSTDL SSRSYLKSAS
     ISASKCVAVK DNKEPEDDYI SEEMEGSVDG LSEQVSRMHS
//