ID   MPK8_ORYSJ              Reviewed;         569 AA.
AC   Q5SN53; Q8H0P0;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   24-JAN-2024, entry version 104.
DE   RecName: Full=Mitogen-activated protein kinase 8;
DE            Short=MAP kinase 8;
DE            EC=2.7.11.24;
DE   AltName: Full=OsWJUMK1;
DE   AltName: Full=Wound- and JA-uninducible MAP kinase 1;
GN   Name=MPK8; Synonyms=WJUMK1;
GN   OrderedLocusNames=Os01g0665200, LOC_Os01g47530;
GN   ORFNames=P0003E08.19-1;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Nipponbare; TISSUE=Leaf;
RX   PubMed=12507518; DOI=10.1016/s0006-291x(02)02868-1;
RA   Agrawal G.K., Agrawal S.K., Shibato J., Iwahashi H., Rakwal R.;
RT   "Novel rice MAP kinases OsMSRMK3 and OsWJUMK1 involved in encountering
RT   diverse environmental stresses and developmental regulation.";
RL   Biochem. Biophys. Res. Commun. 300:775-783(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
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=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   [5]
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   -!- TISSUE SPECIFICITY: Expressed in leaves and panicles.
CC       {ECO:0000269|PubMed:12507518}.
CC   -!- INDUCTION: By heavy metals, abscisic acid (ABA) and infection with rice
CC       blast fungus (M.grisea). Down-regulated by high temperature and UV-C.
CC       {ECO:0000269|PubMed:12507518, 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=BAD72352.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ512643; CAD54742.1; -; mRNA.
DR   EMBL; AP003222; BAD72351.1; -; Genomic_DNA.
DR   EMBL; AP003222; BAD72352.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015611073.1; XM_015755587.1.
DR   AlphaFoldDB; Q5SN53; -.
DR   SMR; Q5SN53; -.
DR   STRING; 39947.Q5SN53; -.
DR   PaxDb; 39947-Q5SN53; -.
DR   EnsemblPlants; Os01t0665200-04; Os01t0665200-04; Os01g0665200.
DR   GeneID; 4326853; -.
DR   Gramene; Os01t0665200-04; Os01t0665200-04; Os01g0665200.
DR   KEGG; osa:4326853; -.
DR   eggNOG; KOG0660; Eukaryota.
DR   InParanoid; Q5SN53; -.
DR   OrthoDB; 1032011at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
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:SF187; MITOGEN-ACTIVATED PROTEIN KINASE 8; 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.
DR   Genevisible; Q5SN53; OS.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..569
FT                   /note="Mitogen-activated protein kinase 8"
FT                   /id="PRO_0000239751"
FT   DOMAIN          13..304
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          404..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           175..177
FT                   /note="TXY"
FT   COMPBIAS        404..427
FT                   /note="Polar 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   569 AA;  65179 MW;  A5B701306B92AC47 CRC64;
     MDFFSEYGDA NRYKIQEVIG KGSYGVVCSA IDQHTGDKVA IKKIHNIFEH LSDAARILRE
     IKLLRLLRHP DIVEIKHIML PPSRRDFKDI YVVFELMDTD LHQVIKANDD LTKEHHQFFL
     YQMLRALKYI HTANVYHRDL KPKNILANAN CKLKICDFGL ARVAFNDTPT TVFWTDYVAT
     RWYRAPELCG SFFTKYSPAI DIWSIGCIFA EILTGKPLFP GKNVVHQLDL MTDLLGTPSM
     DTVTRIRNEK ARRYLSSMRK KQPVPFSERF PKADPAALKL LQRLLAFDPK DRPTAEEALA
     DPYFKGLAKA EREPSCQPIT KMEFEFERRK VTKEDVKELI FREILEYHPQ LLKDYMNGTE
     KTNFLYPSAL DNFRRQFANL EENGGKNGDA VPSDRKHVSL PRTTTVHSAP IPPKDHQNIT
     SQVPQRIPGR TGRGACPVIP FENLSAMGPY NQRRVVRNPV LPPATTNLSA YAYHRKSDSS
     ERELQQELEK DRMRYQPSEH FMDAKVVSHM SHDLRASSYY VSKAKSDVAD RAALQSNMMQ
     GIGPFNGIAA VGGNYNKVST VQYGVSRMY
//