MPK5_ORYSI
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 03-AUG-2022, entry version 78.
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; 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:0006468; P:protein phosphorylation; IEA:InterPro.
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 Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01772; JNKMAPKINASE.
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.
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
