ID   MPK5_ORYSI              Reviewed;         369 AA.
AC   A2XFC8; Q0PIU7; Q7FNE2; Q8GZZ3; Q8S3T6; Q9AXF2; Q9FQM3; Q9FSE6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   08-NOV-2023, entry version 81.
DE   RecName: Full=Mitogen-activated protein kinase 5;
DE            Short=MAP kinase 5;
DE            EC=2.7.11.24;
DE   AltName: Full=Benzothiadiazole-induced MAP kinase 1;
DE   AltName: Full=MAP kinase 2;
DE   AltName: Full=Multiple stress-responsive MAP kinase 2;
DE   AltName: Full=OsBIMK1;
DE   AltName: Full=OsMAP1;
DE   AltName: Full=OsMAPK2;
DE   AltName: Full=OsMAPK5;
DE   AltName: Full=OsMPK3;
DE   AltName: Full=OsMSRMK2;
GN   Name=MPK5; Synonyms=BIMK1, MAPK2, MAPK5, MPK3, MSRMK2;
GN   ORFNames=OsI_010771;
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 [MRNA], AND INDUCTION.
RC   STRAIN=cv. Yuanfengzao;
RX   PubMed=12355160; DOI=10.1007/s00425-002-0794-5;
RA   Song F., Goodman R.M.;
RT   "OsBIMK1, a rice MAP kinase gene involved in disease resistance
RT   responses.";
RL   Planta 215:997-1005(2002).
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 3
RT   (MPK3) 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   INTERACTION WITH MKK1.
RX   PubMed=12177502; DOI=10.1104/pp.006072;
RA   Wen J.-Q., Oono K., Imai R.;
RT   "Two novel mitogen-activated protein signaling components, OsMEK1 and
RT   OsMAP1, are involved in a moderate low-temperature signaling pathway in
RT   rice.";
RL   Plant Physiol. 129:1880-1891(2002).
RN   [5]
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   -!- FUNCTION: Involved in disease resistance and abiotic stress tolerance
CC       signaling pathways. {ECO:0000250}.
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   -!- SUBUNIT: Interacts with MKK1. {ECO:0000269|PubMed:12177502}.
CC   -!- INDUCTION: By benzothiadiazole (BTH), dichloroisonicotinic acid,
CC       probenazole, jasmonic acid, wounding and infection with P.syringae and
CC       M.grisea. {ECO:0000269|PubMed:12355160}.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-194 and Tyr-196, 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; AF332873; AAK01710.1; -; mRNA.
DR   EMBL; DQ826422; ABH01189.1; -; mRNA.
DR   EMBL; CM000128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A2XFC8; -.
DR   SMR; A2XFC8; -.
DR   STRING; 39946.A2XFC8; -.
DR   Proteomes; UP000007015; Chromosome 3.
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:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR008351; MAPK_JNK.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR   PANTHER; PTHR24055:SF391; MITOGEN-ACTIVATED PROTEIN KINASE 3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01772; JNKMAPKINASE.
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   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Plant defense;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..369
FT                   /note="Mitogen-activated protein kinase 5"
FT                   /id="PRO_0000300870"
FT   DOMAIN          36..322
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOTIF           194..196
FT                   /note="TXY"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         42..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         194
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         196
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        340
FT                   /note="F -> I (in Ref. 2; ABH01189)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        367
FT                   /note="I -> F (in Ref. 1; AAK01710)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   369 AA;  42995 MW;  417D81732635F2D3 CRC64;
     MDGAPVAEFR PTMTHGGRYL LYDIFGNKFE VTNKYQPPIM PIGRGAYGIV CSVMNFETRE
     MVAIKKIANA FNNDMDAKRT LREIKLLRHL DHENIIGIRD VIPPPIPQAF NDVYIATELM
     DTDLHHIIRS NQELSEEHCQ YFLYQILRGL KYIHSANVIH RDLKPSNLLL NANCDLKICD
     FGLARPSSES DMMTEYVVTR WYRAPELLLN STDYSAAIDV WSVGCIFMEL INRQPLFPGR
     DHMHQMRLIT EVIGTPTDDE LGFIRNEDAR KYMRHLPQYP RRTFASMFPR VQPAALDLIE
     RMLTFNPLQR ITVEEALDHP YLERLHDIAD EPICLEPFSF DFEQKALNED QMKQLIFNEA
     IEMNPNIRY
//