MPK8_ARATH
ID MPK8_ARATH Reviewed; 589 AA.
AC Q9LM33; Q9LMS2; Q9MB23;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Mitogen-activated protein kinase 8;
DE Short=AtMPK8;
DE Short=MAP kinase 8;
DE EC=2.7.11.24;
GN Name=MPK8; OrderedLocusNames=At1g18150; ORFNames=T10F20.15, T10O22.12;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Mizoguchi T., Ichimura K., Shinozaki K.;
RT "Arabidopsis thaliana mRNA for MAP kinase.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12119167; DOI=10.1016/s1360-1385(02)02302-6;
RG MAPK group;
RT "Mitogen-activated protein kinase cascades in plants: a new nomenclature.";
RL Trends Plant Sci. 7:301-308(2002).
RN [6]
RP GENE FAMILY.
RX PubMed=16537113; DOI=10.1016/j.tplants.2006.02.007;
RA Hamel L.P., Nicole M.C., Sritubtim S., Morency M.J., Ellis M., Ehlting J.,
RA Beaudoin N., Barbazuk B., Klessig D., Lee J., Martin G., Mundy J.,
RA Ohashi Y., Scheel D., Sheen J., Xing T., Zhang S., Seguin A., Ellis B.E.;
RT "Ancient signals: comparative genomics of plant MAPK and MAPKK gene
RT families.";
RL Trends Plant Sci. 11:192-198(2006).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP INTERACTION WITH CAM3; CAM4 AND CAM7, AUTOPHOSPHORYLATION, AND MUTAGENESIS
RP OF LYS-133; LYS-134; THR-266 AND TYR-268.
RX PubMed=21419340; DOI=10.1016/j.molcel.2011.02.029;
RA Takahashi F., Mizoguchi T., Yoshida R., Ichimura K., Shinozaki K.;
RT "Calmodulin-dependent activation of MAP kinase for ROS homeostasis in
RT Arabidopsis.";
RL Mol. Cell 41:649-660(2011).
CC -!- FUNCTION: MKK3-MPK8 and CAMs-MPK8 modules negatively regulates ROS
CC accumulation through controlling expression of the RBOHD gene during
CC wounding. {ECO:0000269|PubMed:21419340}.
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 (By similarity). Activated by two independent
CC mechanisms, the binding of CAMs in a calcium-dependent manner and the
CC phosphorylation by MAP kinase kinase MKK3. Activated in response to
CC mechanical wounding, hydrogen peroxide and jasmonic acid (JA).
CC {ECO:0000250, ECO:0000269|PubMed:21419340}.
CC -!- SUBUNIT: Interacts with CAM3, CAM4 AND CAM7 in an calcium-dependent
CC manner. {ECO:0000269|PubMed:21419340}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:21419340}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-266 and Tyr-268, which activates the
CC enzyme (By similarity). Autophosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: More susceptible to oxidative stress.
CC {ECO:0000269|PubMed:21419340}.
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=AAF78388.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA92222.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB038693; BAA92222.1; ALT_FRAME; mRNA.
DR EMBL; AC034107; AAF97831.1; -; Genomic_DNA.
DR EMBL; AC069551; AAF78388.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29679.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29680.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29681.1; -; Genomic_DNA.
DR EMBL; AY045931; AAK76605.1; -; mRNA.
DR EMBL; AY142618; AAN13187.1; -; mRNA.
DR RefSeq; NP_001185027.1; NM_001198098.1.
DR RefSeq; NP_173253.1; NM_101675.4.
DR RefSeq; NP_849685.1; NM_179354.3.
DR AlphaFoldDB; Q9LM33; -.
DR SMR; Q9LM33; -.
DR BioGRID; 23633; 42.
DR IntAct; Q9LM33; 1.
DR STRING; 3702.AT1G18150.3; -.
DR iPTMnet; Q9LM33; -.
DR PaxDb; Q9LM33; -.
DR PRIDE; Q9LM33; -.
DR ProteomicsDB; 239069; -.
DR EnsemblPlants; AT1G18150.1; AT1G18150.1; AT1G18150.
DR EnsemblPlants; AT1G18150.2; AT1G18150.2; AT1G18150.
DR EnsemblPlants; AT1G18150.3; AT1G18150.3; AT1G18150.
DR GeneID; 838394; -.
DR Gramene; AT1G18150.1; AT1G18150.1; AT1G18150.
DR Gramene; AT1G18150.2; AT1G18150.2; AT1G18150.
DR Gramene; AT1G18150.3; AT1G18150.3; AT1G18150.
DR KEGG; ath:AT1G18150; -.
DR Araport; AT1G18150; -.
DR TAIR; locus:2194040; AT1G18150.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_5_1; -.
DR InParanoid; Q9LM33; -.
DR OMA; GHTGAQQ; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; Q9LM33; -.
DR PRO; PR:Q9LM33; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LM33; baseline and differential.
DR Genevisible; Q9LM33; AT.
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:0005516; F:calmodulin binding; IPI:TAIR.
DR GO; GO:0004707; F:MAP kinase activity; ISS:TAIR.
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 GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..589
FT /note="Mitogen-activated protein kinase 8"
FT /id="PRO_0000245808"
FT DOMAIN 104..395
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 18..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 266..268
FT /note="TXY"
FT COMPBIAS 541..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 230
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 110..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 266
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 268
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 271
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MUTAGEN 133
FT /note="K->M: Abolishes CAM4-dependent activity."
FT /evidence="ECO:0000269|PubMed:21419340"
FT MUTAGEN 134
FT /note="K->R: Abolishes CAM4-dependent activity."
FT /evidence="ECO:0000269|PubMed:21419340"
FT MUTAGEN 266
FT /note="T->A: Do not affect CAM4-dependent activity; when
FT associated with F-268."
FT /evidence="ECO:0000269|PubMed:21419340"
FT MUTAGEN 268
FT /note="Y->F: Do not affect CAM4-dependent activity; when
FT associated with A-266."
FT /evidence="ECO:0000269|PubMed:21419340"
FT CONFLICT 179..180
FT /note="RD -> PH (in Ref. 1; BAA92222)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="D -> E (in Ref. 1; BAA92222)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="I -> L (in Ref. 1; BAA92222)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="G -> V (in Ref. 1; BAA92222)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 66231 MW; 96769BA5E164BD74 CRC64;
MGGGGNLVDG VRRWLFQRPS SSSSSSSSNN NNNNHEQPIF NSSSFSSSSN PNHSANSGEL
IIEEDLDFSG LTLINVPKRN HLPMDPHKKG ETEFFTEYGE ANRYQIQEVV GKGSYGVVAS
AVDSHTGERV AIKKINDVFE HVSDATRILR EIKLLRLLRH PDVVEIKHIM LPPSRREFRD
IYVVFELMES DLHQVIKAND DLTPEHYQFF LYQLLRGLKY VHAANVFHRD LKPKNILANA
DCKLKICDFG LARVSFNDAP TAIFWTDYVA TRWYRAPELC GSFFSKYTPA IDIWSVGCIF
AEMLLGKPLF PGKNVVHQLD LMTDFLGTPP PESISRIRNE KARRYLSSMR KKQPVPFSHK
FPKADPLALR LLERLLAFDP KDRASAEDAL ADPYFSGLSN SEREPTTQPI SKLEFDFERK
KLVKDDVREL IYREILEYHP QMLEEYLRGG DQLSFMYPSG VDRFKRQFAH LEENQGKPGA
AGGGRSTALH RHHASLPRER VPAPNGETAE ESSDVERRAA AAVASTLESE EADNGGGYSA
RNLMKSASIS GSKCIGVQSK TDKEDTIAEE EDNETVAELT DKVASLHNS
