MPK13_ORYSJ
ID MPK13_ORYSJ Reviewed; 506 AA.
AC Q0E459; Q6QUV9; Q6Z831; Q9SE22;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Mitogen-activated protein kinase 13;
DE Short=MAP kinase 13;
DE EC=2.7.11.24;
DE AltName: Full=Benzothiadiazole-induced MAP kinase 2;
DE AltName: Full=MAP kinase 2;
DE AltName: Full=OsBIMK2;
DE AltName: Full=OsBWMK2;
DE AltName: Full=OsMAPK2;
DE AltName: Full=OsMPK17-2;
DE AltName: Full=Wound- and blast-induced MAPK 2;
GN Name=MPK13; Synonyms=BIMK2, BWMK2, MAPK2, MPK17-2;
GN OrderedLocusNames=Os02g0135200, LOC_Os02g04230; ORFNames=P0585B01.25;
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].
RA Cheong Y.H., Moon B.C., Kim J.K., Cho M.J.;
RT "Novel plant MAP kinases phosphorylate defense-related transcription
RT factors.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Aichi asahi;
RA Wang D.-P., Zhao W.-S., Wang M., Meng X.-B., Lin R.-M., Zhang S.-H.,
RA Peng Y.-L.;
RT "Oryza sativa (japonica cultivar-group) wound and blast induced MAPK
RT (BWMK2) mRNA.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [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 salicylic acid (SA), ethylene and infection with rice
CC blast fungus (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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF23903.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF194416; AAF23903.1; ALT_FRAME; mRNA.
DR EMBL; AY588939; AAT00625.1; -; mRNA.
DR EMBL; AP004799; BAD10093.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF07729.1; -; Genomic_DNA.
DR EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015626451.1; XM_015770965.1.
DR RefSeq; XP_015626452.1; XM_015770966.1.
DR RefSeq; XP_015626453.1; XM_015770967.1.
DR RefSeq; XP_015626454.1; XM_015770968.1.
DR AlphaFoldDB; Q0E459; -.
DR SMR; Q0E459; -.
DR STRING; 4530.OS02T0135200-00; -.
DR PaxDb; Q0E459; -.
DR PRIDE; Q0E459; -.
DR GeneID; 4328223; -.
DR KEGG; osa:4328223; -.
DR eggNOG; KOG0660; Eukaryota.
DR InParanoid; Q0E459; -.
DR OrthoDB; 741207at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
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..506
FT /note="Mitogen-activated protein kinase 13"
FT /id="PRO_0000239756"
FT DOMAIN 13..304
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 384..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 175..177
FT /note="TXY"
FT COMPBIAS 384..401
FT /note="Basic and acidic 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 506 AA; 58281 MW; 7EBCBA768079F972 CRC64;
MEFFTEYGEA SQYQIQEVVG KGSYGVVAAA VDTHTGERVA IKKINDVFEH VSDAIRILRE
IKVLRLLRHP DIVVIKHIML PPTRREFRDI YVVFELMESD LHQVIEANHD LSPEHHRFFL
YQLLCALKYI HSANVFHRDL KPKNILANSD CKLKICDFGL ARVAFNDSPS TIFWTDYVAT
RWYRAPELCG SFFSKYTPAI DIWSIGCIFA EILTGRPLFP GRNVVHQLDL ITDLLGTPSS
ETLSRIRNEN ARGYLTGMQR KHPIPFSHKF HNADPLALRL LERLLAFDPK DRPTAEEALA
DPYFRGISKL SREPSRLPVS KFEFEFERRK LTKDDVREMI YREILEYHPQ MLQEYIRGGE
QISFLYPSGV DRFKRQFAHL EENYSRGERS TPLRRQHASL PRERVCSSVD SNNQDSDNEE
RRAISSIART MISPPRSQEK GKNRASAYPN GIINLNSNPK IYLKSASISA STCIIRGNKG
PKENGISEDM EEVVYELSDN VTRMLS
