ID   MPK13_ORYSI             Reviewed;         506 AA.
AC   A2X0M1; Q0PIU6; Q6QUV9; Q6Z831; Q9SE22;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   27-MAR-2024, entry version 82.
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   ORFNames=OsI_005614;
OS   Oryza sativa subsp. indica (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=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Yuanfengzao;
RA   Song D., Song F., Goodman R.M., Zheng Z.;
RT   "OsBIMK2, a gene encoding a map kinase, is involved in disease resistance
RT   responses in rice.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Pusa Basmati;
RA   Rao K.P., Kumar K., Sharma P., Sinha A.K.;
RT   "Oryza sativa (indica cultivar-group) mitogen activated protein kinase 17-2
RT   (MPK17-2) mRNA.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [4]
RP   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).
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=EAY84381.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY524973; AAS18417.1; -; mRNA.
DR   EMBL; AY524974; AAS18418.1; -; Genomic_DNA.
DR   EMBL; DQ826423; ABH01190.2; -; mRNA.
DR   EMBL; CM000127; EAY84381.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A2X0M1; -.
DR   SMR; A2X0M1; -.
DR   STRING; 39946.A2X0M1; -.
DR   iPTMnet; A2X0M1; -.
DR   HOGENOM; CLU_000288_181_5_1; -.
DR   Proteomes; UP000007015; Chromosome 2.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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.
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_0000300871"
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
//