MPK9_ORYSJ
ID MPK9_ORYSJ Reviewed; 700 AA.
AC Q6L5D4; Q75I00;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Mitogen-activated protein kinase 9;
DE Short=MAP kinase 9;
DE EC=2.7.11.24;
GN Name=MPK9; OrderedLocusNames=Os05g0582400, LOC_Os05g50560;
GN ORFNames=OJ1651_G11.11, OSJNBb0035N21.16;
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [2]
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 [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 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-269 and Tyr-271, 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=AAS16898.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAT44204.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC098573; AAT44204.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC134929; AAS16898.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q6L5D4; -.
DR SMR; Q6L5D4; -.
DR STRING; 39947.Q6L5D4; -.
DR PaxDb; Q6L5D4; -.
DR PRIDE; Q6L5D4; -.
DR InParanoid; Q6L5D4; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..700
FT /note="Mitogen-activated protein kinase 9"
FT /id="PRO_0000239752"
FT DOMAIN 107..398
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 475..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 269..271
FT /note="TXY"
FT ACT_SITE 233
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 113..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 269
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 271
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 700 AA; 79081 MW; DE9705AB1060A025 CRC64;
MAVKMRIGRR RAIQQGIAEG GFEWRRVWGC READSRGALW ELVWGERSVR ERNAAGAAEE
VIALFIMDEM CDPASNLEYV VEKAKCDVHR TSSAEEFFTE YGDANRYRIQ EVIGKGSYGV
VCSAIDLHTR QKVAIKKVHN IFEHVSDAAR ILREIKLLRL LRHPDIVEIK HIMLPPSRRD
FKDIYVVFEL MESDLHQVIK ANDDLTKEHY QFFLYQLLRA LKYIHTASVY HRDLKPKNIL
ANSNCKLKIC DFGLARVAFN DTPTTVFWTD YVATRWYRAP ELCGSFFSKY TPAIDIWSIG
CIFAEVLTGK PLFPGKNVVH QLDLMTDLLG TPSMDTISRV RNEKARRYLS SMRKKDPVPF
SQKFPNADPL ALKLLQRLLA FDPKDRPTAE EALTDPYFKG LSKIDREPSC QPIRKLEFEF
EQKKLSKEDI RELIFQEILE YHPQLQKNYR NGRERATFLY PSAVDQFKKQ FSNLEESNGS
GSAIPMERKH ASLPRSTTVH STPIPPKEQP LAASLKSSRP VSDEPCKNPW VMGGFSGNIP
TSSQVSQVAK PVAPGRPVGS VFPYETGSTN DPYGPRGPVM SSGYPPQQQI SQAYGYHQVP
ARMNCVEQSQ AMDAYKMHSQ SQTQAYAYPN SKVTADVALD MRGSTFHHSA GSKNGSLDRM
VTQTDIYTRS LNGIVAAATS AGVGTNRKVG AVPISTSRMY
