MPK14_ORYSJ
ID MPK14_ORYSJ Reviewed; 542 AA.
AC Q75KK8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Mitogen-activated protein kinase 14;
DE Short=MAP kinase 14;
DE EC=2.7.11.24;
GN Name=MPK14; OrderedLocusNames=Os05g0143500, LOC_Os05g05160;
GN ORFNames=OJ1264_A04.20, OJ1607_F09.3;
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 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 [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 -!- 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}.
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DR EMBL; AC104277; AAS98446.1; -; Genomic_DNA.
DR EMBL; AC104283; AAU90196.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS92219.1; -; Genomic_DNA.
DR EMBL; AK063944; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015639438.1; XM_015783952.1.
DR AlphaFoldDB; Q75KK8; -.
DR SMR; Q75KK8; -.
DR STRING; 4530.OS05T0143500-02; -.
DR PaxDb; Q75KK8; -.
DR PRIDE; Q75KK8; -.
DR EnsemblPlants; Os05t0143500-02; Os05t0143500-02; Os05g0143500.
DR GeneID; 9267958; -.
DR Gramene; Os05t0143500-02; Os05t0143500-02; Os05g0143500.
DR KEGG; osa:9267958; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_5_1; -.
DR InParanoid; Q75KK8; -.
DR OMA; TATSRWY; -.
DR OrthoDB; 741207at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; Q75KK8; baseline and differential.
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 ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..542
FT /note="Mitogen-activated protein kinase 14"
FT /id="PRO_0000239757"
FT DOMAIN 13..304
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 388..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 175..177
FT /note="TXY"
FT COMPBIAS 489..505
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 542 AA; 61762 MW; 1E797CEF2BD8631A CRC64;
MDFFTEYGEG NRYKIEEVIG KGSYGVVCSA LDTHTGDKVA IKKINDIFEH VSDATRILRE
IKLLRLLRHP DIVEIKHILL PPSRREFKDI YVVFELMESD LHQVIKANDD LTPEHYQFFL
YQLLRGLKYI HTANVFHRDL KPKNILANAD CKLKICDFGL ARVAFSDTPT AIFWTDYIAT
RWYRAPELCG SFFSKYTPAI DIWSIGCIFA ELLTGKPLFP GKNVVHQLDI ITDLLGTPSP
ETISRIRNEK ARRYLNSMRR KKPIPFTQKF PNADPLAMRL LERMLAFDPK DRPSAEEALA
DPYFKNIANV DREPSAQPIT KLEFEFERRR ITKEDIRELI YREILEYHPK MLREFLEGTE
STGFMYPSAV DHFKKQFAYL EEHYAKGSTA APPERQHNSL PRPCVVYSDN RPQSTASVTE
DLSRCLIRDN NLKSQDSASV GASRIPQGAA ARPGKAVGSV LRYGNCSTSA AEQQYEQRRV
VRNPAIAPNS SVPLGSSYPR RNQTCKSETG DVERIDSSQT GPPKPYVANK LPATVDGRSG
HW
