MPK12_ORYSJ
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 03-AUG-2022, entry version 124.
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. [Q5Z9J0-1]
DR AlphaFoldDB; Q5Z9J0; -.
DR SMR; Q5Z9J0; -.
DR BioGRID; 811054; 2.
DR STRING; 4530.OS06T0708000-01; -.
DR iPTMnet; Q5Z9J0; -.
DR PaxDb; Q5Z9J0; -.
DR PRIDE; 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; LPVENHK; -.
DR OrthoDB; 741207at2759; -.
DR PRO; PR:Q5Z9J0; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q5Z9J0; 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:0006952; P:defense response; IEA:UniProtKB-KW.
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 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
