MPK3_ORYSJ
ID MPK3_ORYSJ Reviewed; 370 AA.
AC Q6Z437; Q0E3Y5; Q9M545;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Mitogen-activated protein kinase 3;
DE Short=MAP kinase 3;
DE EC=2.7.11.24;
DE AltName: Full=MAP kinase 2;
DE AltName: Full=OsMAP3;
DE AltName: Full=OsMAPK2;
GN Name=MPK3; Synonyms=MAP3, MAPK2;
GN OrderedLocusNames=Os02g0148100, LOC_Os02g05480; ORFNames=P0479D12.11;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ho S.L., Jang J.M., Yu S.M.;
RT "Developmental regulation of a rice MAP kinase gene expression.";
RL Submitted (MAR-2000) 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
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 -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-191 and Tyr-193, 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; AF216317; AAG40581.1; -; mRNA.
DR EMBL; AF241166; AAF61238.1; -; mRNA.
DR EMBL; AP005191; BAD13057.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF07803.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS76982.1; -; Genomic_DNA.
DR EMBL; AK119650; BAG99730.1; -; mRNA.
DR RefSeq; XP_015624723.1; XM_015769237.1.
DR RefSeq; XP_015624724.1; XM_015769238.1.
DR AlphaFoldDB; Q6Z437; -.
DR SMR; Q6Z437; -.
DR IntAct; Q6Z437; 5.
DR STRING; 4530.OS02T0148100-01; -.
DR PaxDb; Q6Z437; -.
DR PRIDE; Q6Z437; -.
DR EnsemblPlants; Os02t0148100-01; Os02t0148100-01; Os02g0148100.
DR GeneID; 4328297; -.
DR Gramene; Os02t0148100-01; Os02t0148100-01; Os02g0148100.
DR KEGG; osa:4328297; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q6Z437; -.
DR OMA; SFFDFDY; -.
DR OrthoDB; 741207at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6Z437; 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: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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..370
FT /note="Mitogen-activated protein kinase 3"
FT /id="PRO_0000239746"
FT DOMAIN 32..319
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 191..193
FT /note="TXY"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 38..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 191
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 193
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 370 AA; 42469 MW; 7F03ACCA17F0E033 CRC64;
MAIMVDPPNG MGNQGKYYYS MWQTLFEIDT KYVPIKPIGR GAYGIVCSSI NRETNEKVAI
KKIHNVFDNR VDALRTLREL KLLRHLRHEN VIALKDIMMP VHRRSFKDVY LVYELMDTDL
HQIIKSPQGL SNDHCQYFLF QLLRGLKYLH SAEILHRDLK PGNLLVNANC DLKICDFGLA
RTNSSKGQFM TEYVVTRWYR APELLLCCDN YGTSIDVWSV GCIFAELLGR KPIFPGTECL
NQLKLIVNVL GTMSESDLEF IDNPKARRYI KSLPYTPGVP LASMYPHAHP LAIDLLQKML
IFDPTKRISV TEALEHPYMS PLYDPSANPP AQVPIDLDID ENISADMIRE MMWHEMLHYH
PEVVAAMSAR
