MPK1_ORYSJ
ID MPK1_ORYSJ Reviewed; 398 AA.
AC Q84UI5; Q0DEG3;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Mitogen-activated protein kinase 1;
DE Short=MAP kinase 1;
DE EC=2.7.11.24;
DE AltName: Full=MAP kinase 6;
DE AltName: Full=OsMAPK6;
DE AltName: Full=OsSIPK;
GN Name=MPK1; Synonyms=MAPK6, SIPK;
GN OrderedLocusNames=Os06g0154500, LOC_Os06g06090; ORFNames=OSJNBa0085L11.14;
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], FUNCTION, ACTIVITY REGULATION, AND INTERACTION
RP WITH RAC1.
RC STRAIN=cv. Kinmaze;
RX PubMed=15951489; DOI=10.1104/pp.104.057414;
RA Lieberherr D., Thao N.P., Nakashima A., Umemura K., Kawasaki T.,
RA Shimamoto K.;
RT "A sphingolipid elicitor-inducible mitogen-activated protein kinase is
RT regulated by the small GTPase OsRac1 and heterotrimeric G-protein in
RT rice.";
RL Plant Physiol. 138:1644-1652(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare; TISSUE=Leaf;
RA Rakwal R., Jwa N.S., Shibato J., Iwahashi H.;
RT "Identification of a novel rice (Oryza sativa L. japonica-type cv.
RT Nipponbare) mitogen-activated protein kinase OsSIPK, an orthologue of
RT tobacco NtSIPK.";
RL Submitted (JAN-2003) 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 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).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=23777258; DOI=10.1111/pce.12154;
RA Shi B., Ni L., Liu Y., Zhang A., Tan M., Jiang M.;
RT "OsDMI3-mediated activation of OsMPK1 regulates the activities of
RT antioxidant enzymes in abscisic acid signalling in rice.";
RL Plant Cell Environ. 37:341-352(2014).
CC -!- FUNCTION: Involved in sphingolipid elicitor (SE)-dependent defense
CC signaling pathway. Acts downstream of heterotrimeric G protein alpha
CC subunit and small GTPase RAC1. May regulate the expression of various
CC genes involved in biotic and abiotic stress response (PubMed:15951489).
CC Involved in an abscisic acid signaling pathway that regulates the
CC activities of antioxidant enzymes and the production of hydrogen
CC peroxide. Acts downstream of CCAMK (PubMed:23777258).
CC {ECO:0000269|PubMed:15951489, ECO:0000269|PubMed:23777258}.
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 sphingolipid
CC elicitor (SE). {ECO:0000250, ECO:0000269|PubMed:15951489}.
CC -!- SUBUNIT: May interact with RAC1.
CC -!- INDUCTION: Induced by hydrogen peroxide and abscisic acid (ABA).
CC {ECO:0000269|PubMed:23777258}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-225 and Tyr-227, 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; AB183398; BAD34534.1; -; mRNA.
DR EMBL; AJ535841; CAD59793.1; -; mRNA.
DR EMBL; AP006533; BAD69291.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18760.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS96224.1; -; Genomic_DNA.
DR RefSeq; XP_015643193.1; XM_015787707.1.
DR AlphaFoldDB; Q84UI5; -.
DR SMR; Q84UI5; -.
DR STRING; 4530.OS06T0154500-01; -.
DR PaxDb; Q84UI5; -.
DR PRIDE; Q84UI5; -.
DR EnsemblPlants; Os06t0154500-01; Os06t0154500-01; Os06g0154500.
DR GeneID; 4340170; -.
DR Gramene; Os06t0154500-01; Os06t0154500-01; Os06g0154500.
DR KEGG; osa:4340170; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q84UI5; -.
DR OMA; YTDLNPV; -.
DR OrthoDB; 741207at2759; -.
DR PlantReactome; R-OSA-9631623; Regulation of embryo development.
DR PlantReactome; R-OSA-9675508; Root elongation.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q84UI5; 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:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
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 InterPro; IPR008271; Ser/Thr_kinase_AS.
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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..398
FT /note="Mitogen-activated protein kinase 1"
FT /id="PRO_0000239744"
FT DOMAIN 67..352
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 225..227
FT /note="TXY"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 73..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 225
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 227
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 44858 MW; 46E2907463A7C490 CRC64;
MDAGAQPPDT EMAEAGGGQQ PPAAAAAAGA GAGAGMMENI QATLSHGGRF IQYNIFGNVF
EVTAKYKPPI LPIGKGAYGI VCSALNSETG EQVAIKKIAN AFDNKIDAKR TLREIKLLRH
MDHENIVAIR DIIPPPQRNS FNDVYIAYEL MDTDLHQIIR SNQALSEEHC QYFLYQILRG
LKYIHSANVL HRDLKPSNLL LNANCDLKIC DFGLARTTSE TDFMTEYVVT RWYRAPELLL
NSSEYTAAID VWSVGCIFME LMDRKPLFPG RDHVHQLRLL MELIGTPNEA DLDFVNENAR
RYIRQLPRHA RQSFPEKFPH VHPLAIDLVE KMLTFDPRQR ITVEGALAHP YLASLHDISD
EPVCSSPFSF DFEQHALSEE QMKDLIYQEG LAFNPDYQ
