MPK13_ORYSI
ID MPK13_ORYSI Reviewed; 506 AA.
AC A2X0M1; Q0PIU6; Q6QUV9; Q6Z831; Q9SE22;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Mitogen-activated protein kinase 13;
DE Short=MAP kinase 13;
DE EC=2.7.11.24;
DE AltName: Full=Benzothiadiazole-induced MAP kinase 2;
DE AltName: Full=MAP kinase 2;
DE AltName: Full=OsBIMK2;
DE AltName: Full=OsBWMK2;
DE AltName: Full=OsMAPK2;
DE AltName: Full=OsMPK17-2;
DE AltName: Full=Wound- and blast-induced MAPK 2;
GN Name=MPK13; Synonyms=BIMK2, BWMK2, MAPK2, MPK17-2; ORFNames=OsI_005614;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Yuanfengzao;
RA Song D., Song F., Goodman R.M., Zheng Z.;
RT "OsBIMK2, a gene encoding a map kinase, is involved in disease resistance
RT responses in rice.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Pusa Basmati;
RA Rao K.P., Kumar K., Sharma P., Sinha A.K.;
RT "Oryza sativa (indica cultivar-group) mitogen activated protein kinase 17-2
RT (MPK17-2) mRNA.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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 -!- INDUCTION: By salicylic acid (SA), ethylene and infection with rice
CC blast fungus (M.grisea).
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=EAY84381.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY524973; AAS18417.1; -; mRNA.
DR EMBL; AY524974; AAS18418.1; -; Genomic_DNA.
DR EMBL; DQ826423; ABH01190.2; -; mRNA.
DR EMBL; CM000127; EAY84381.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A2X0M1; -.
DR SMR; A2X0M1; -.
DR STRING; 39946.A2X0M1; -.
DR iPTMnet; A2X0M1; -.
DR HOGENOM; CLU_000288_181_5_1; -.
DR Proteomes; UP000007015; Chromosome 2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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 ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..506
FT /note="Mitogen-activated protein kinase 13"
FT /id="PRO_0000300871"
FT DOMAIN 13..304
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 384..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 175..177
FT /note="TXY"
FT COMPBIAS 384..401
FT /note="Basic and acidic 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 506 AA; 58281 MW; 7EBCBA768079F972 CRC64;
MEFFTEYGEA SQYQIQEVVG KGSYGVVAAA VDTHTGERVA IKKINDVFEH VSDAIRILRE
IKVLRLLRHP DIVVIKHIML PPTRREFRDI YVVFELMESD LHQVIEANHD LSPEHHRFFL
YQLLCALKYI HSANVFHRDL KPKNILANSD CKLKICDFGL ARVAFNDSPS TIFWTDYVAT
RWYRAPELCG SFFSKYTPAI DIWSIGCIFA EILTGRPLFP GRNVVHQLDL ITDLLGTPSS
ETLSRIRNEN ARGYLTGMQR KHPIPFSHKF HNADPLALRL LERLLAFDPK DRPTAEEALA
DPYFRGISKL SREPSRLPVS KFEFEFERRK LTKDDVREMI YREILEYHPQ MLQEYIRGGE
QISFLYPSGV DRFKRQFAHL EENYSRGERS TPLRRQHASL PRERVCSSVD SNNQDSDNEE
RRAISSIART MISPPRSQEK GKNRASAYPN GIINLNSNPK IYLKSASISA STCIIRGNKG
PKENGISEDM EEVVYELSDN VTRMLS
