MPK11_ORYSJ
ID MPK11_ORYSJ Reviewed; 570 AA.
AC Q5VN19; Q0DC96; Q5VN20;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Mitogen-activated protein kinase 11;
DE Short=MAP kinase 11;
DE EC=2.7.11.24;
GN Name=MPK11; OrderedLocusNames=Os06g0367900, LOC_Os06g26340;
GN ORFNames=OSJNBa0015G09.36-1, OSJNBa0015G09.36-2;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VN19-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VN19-2; Sequence=VSP_019262, VSP_019263;
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-188 and Tyr-190, 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; AP005763; BAD69155.1; -; Genomic_DNA.
DR EMBL; AP005763; BAD69156.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19527.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS97726.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS97727.1; -; Genomic_DNA.
DR EMBL; AK065641; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK066968; BAG90204.1; -; mRNA.
DR EMBL; AK100081; BAG94435.1; -; mRNA.
DR RefSeq; XP_015643951.1; XM_015788465.1. [Q5VN19-1]
DR RefSeq; XP_015643953.1; XM_015788467.1. [Q5VN19-2]
DR AlphaFoldDB; Q5VN19; -.
DR SMR; Q5VN19; -.
DR STRING; 4530.OS06T0367900-01; -.
DR PaxDb; Q5VN19; -.
DR PRIDE; Q5VN19; -.
DR EnsemblPlants; Os06t0367900-01; Os06t0367900-01; Os06g0367900. [Q5VN19-1]
DR EnsemblPlants; Os06t0367900-02; Os06t0367900-02; Os06g0367900. [Q5VN19-2]
DR GeneID; 4341010; -.
DR Gramene; Os06t0367900-01; Os06t0367900-01; Os06g0367900. [Q5VN19-1]
DR Gramene; Os06t0367900-02; Os06t0367900-02; Os06g0367900. [Q5VN19-2]
DR KEGG; osa:4341010; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_5_1; -.
DR InParanoid; Q5VN19; -.
DR OMA; QIQGVHA; -.
DR OrthoDB; 741207at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; Q5VN19; baseline and differential.
DR Genevisible; Q5VN19; 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 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.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..570
FT /note="Mitogen-activated protein kinase 11"
FT /id="PRO_0000239754"
FT DOMAIN 26..317
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 188..190
FT /note="TXY"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 32..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 188
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 190
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 416..421
FT /note="STIVHS -> RAFNYR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_019262"
FT VAR_SEQ 422..570
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_019263"
SQ SEQUENCE 570 AA; 64524 MW; 56B9FDFF251177ED CRC64;
MQTSNFRKKN AAEVDFFMGY GDVNRYEVLE VIGKGSYGLV CSANDIHTGE KVAIKKIHNI
FEHISDAARI LREIKLLRLL RHPDIVEIKH IMLPPSKMDF RDIYVVFELM ESDLHQVIKA
NDDLTREHYQ FFLYQMLRAL KYIHTANVYH RDLKPKNILA NANCKLKICD FGLARVAFTD
APTTVFWTDY VATRWYRAPE LCGSFYSKYT PAIDIWSIGC IFAEVLIGKP LFPGKNVVHQ
LDLITDLLGT PSLDAISQVR NDKARKYLTC MRKKQPASFS HKFLKADPLA LQLLRKLLAF
DPKDRPSAQE ALADPYFNGL AKVEREPSCQ PIPKMEFEFE RRRATKEDIK ELIFQEILEY
HPQLLKEHIS GTERPNFHHL SVVDQFRKQF TQVEENLNGS GAAVSLQRKH SSLPRSTIVH
SAAIPAKDYK HVASSSTKLA VDGSWNAQIQ GVHANIAGEP STIVRPAVSS ERSLAPTLQW
QPNMTHFLNH ALCYQNTVFS GSLLDATGPA QAIPRTTPYV DYRSGNLDLY QHHVSREDVQ
SDTATAQAHA ASHGPVPAVS YSLPGTYRIT
