MPK12_ARATH
ID MPK12_ARATH Reviewed; 372 AA.
AC Q8GYQ5; O82361;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Mitogen-activated protein kinase 12 {ECO:0000303|PubMed:12119167};
DE Short=AtMPK12 {ECO:0000303|PubMed:12119167};
DE Short=MAP kinase 12 {ECO:0000303|PubMed:12119167};
DE EC=2.7.11.24 {ECO:0000269|PubMed:19000167, ECO:0000269|PubMed:27923039};
GN Name=MPK12 {ECO:0000303|PubMed:12119167};
GN OrderedLocusNames=At2g46070 {ECO:0000312|Araport:AT2G46070};
GN ORFNames=T3F17.28 {ECO:0000312|EMBL:AAC62906.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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, MUTAGENESIS OF LYS-70, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP ACTIVATION, INTERACTION WITH IBR5/SKIP33, AND CATALYTIC ACTIVITY.
RX PubMed=19000167; DOI=10.1111/j.1365-313x.2008.03741.x;
RA Lee J.S., Wang S., Sritubtim S., Chen J.-G., Ellis B.E.;
RT "Arabidopsis mitogen-activated protein kinase MPK12 interacts with the MAPK
RT phosphatase IBR5 and regulates auxin signaling.";
RL Plant J. 57:975-985(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH HT1.
RC STRAIN=cv. Columbia;
RX PubMed=27694184; DOI=10.1105/tpc.16.00131;
RA Horak H., Sierla M., Toldsepp K., Wang C., Wang Y.-S., Nuhkat M., Valk E.,
RA Pechter P., Merilo E., Salojaervi J., Overmyer K., Loog M., Brosche M.,
RA Schroeder J.I., Kangasjaervi J., Kollist H.;
RT "A dominant mutation in the HT1 kinase uncovers roles of MAP kinases and
RT GHR1 in CO2-induced stomatal closure.";
RL Plant Cell 28:2493-2509(2016).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-53; LYS-70 AND TYR-122,
RP INTERACTION WITH HT1 AND IBR5, CATALYTIC ACTIVITY, AND AUTOPHOSPHORYLATION.
RC STRAIN=cv. Columbia, and cv. Cvi-0;
RX PubMed=27923039; DOI=10.1371/journal.pbio.2000322;
RA Jakobson L., Vaahtera L., Toldsepp K., Nuhkat M., Wang C., Wang Y.S.,
RA Horak H., Valk E., Pechter P., Sindarovska Y., Tang J., Xiao C., Xu Y.,
RA Gerst Talas U., Garcia-Sosa A.T., Kangasjaervi S., Maran U., Remm M.,
RA Roelfsema M.R., Hu H., Kangasjaervi J., Loog M., Schroeder J.I.,
RA Kollist H., Brosche M.;
RT "Natural variation in Arabidopsis Cvi-0 accession reveals an important role
RT of MPK12 in guard cell CO2 signaling.";
RL PLoS Biol. 14:E2000322-E2000322(2016).
CC -!- FUNCTION: Negative regulator of the auxin transduction signaling
CC pathway (PubMed:19000167). Involved in stomatal movement regulation by
CC phosphorylating and repressing HT1 and HT1-mediated GHR1
CC phosphorylation (PubMed:27694184, PubMed:27923039). Required for CO(2)-
CC mediated stomatal movements (e.g. closure) (PubMed:27923039).
CC {ECO:0000269|PubMed:19000167, ECO:0000269|PubMed:27694184,
CC ECO:0000269|PubMed:27923039}.
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 Evidence={ECO:0000269|PubMed:19000167, ECO:0000269|PubMed:27923039};
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; Evidence={ECO:0000269|PubMed:19000167,
CC ECO:0000269|PubMed:27923039};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with IBR5/SKIP33 (PubMed:19000167, PubMed:27923039).
CC Binds to HT1 (PubMed:27694184, PubMed:27923039).
CC {ECO:0000269|PubMed:19000167, ECO:0000269|PubMed:27694184,
CC ECO:0000269|PubMed:27923039}.
CC -!- INTERACTION:
CC Q8GYQ5; Q84JU4: IBR5; NbExp=8; IntAct=EBI-2128461, EBI-604555;
CC Q8GYQ5; Q94A06: MKK1; NbExp=2; IntAct=EBI-2128461, EBI-994464;
CC Q8GYQ5; Q9FJV0: MKK6; NbExp=2; IntAct=EBI-2128461, EBI-1238868;
CC Q8GYQ5; Q9FX43: MKK9; NbExp=2; IntAct=EBI-2128461, EBI-2128545;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19000167}. Cell
CC membrane {ECO:0000269|PubMed:27923039}; Peripheral membrane protein
CC {ECO:0000269|PubMed:27923039}; Cytoplasmic side
CC {ECO:0000269|PubMed:27923039}. Note=Seems to translocate at the plasma
CC membrane upon interaction with HT1. {ECO:0000269|PubMed:27923039}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8GYQ5-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, stems, leaves,
CC flowers and siliques, mostly around stomata.
CC {ECO:0000269|PubMed:19000167}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Autophosphorylated (PubMed:27923039). Dually phosphorylated on
CC Thr-199 and Tyr-201, which activates the enzyme (By similarity).
CC Activated by auxin. Dephosphorylated and inactivated by IBR5.
CC {ECO:0000250, ECO:0000269|PubMed:27923039}.
CC -!- DISRUPTION PHENOTYPE: Lethal in homozygous plants (PubMed:27923039).
CC Abolished CO(2)-mediated stomatal closure (PubMed:27694184,
CC PubMed:27923039). Increased stomatal opening (PubMed:27923039).
CC {ECO:0000269|PubMed:27694184, ECO:0000269|PubMed:27923039}.
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=AAC62906.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005397; AAC62906.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC10639.1; -; Genomic_DNA.
DR EMBL; AK117449; BAC42114.1; -; mRNA.
DR EMBL; BT024898; ABD85169.1; -; mRNA.
DR PIR; D84898; D84898.
DR RefSeq; NP_001325006.1; NM_001337177.1.
DR RefSeq; NP_182131.2; NM_130170.4. [Q8GYQ5-1]
DR AlphaFoldDB; Q8GYQ5; -.
DR SMR; Q8GYQ5; -.
DR BioGRID; 4550; 3.
DR IntAct; Q8GYQ5; 6.
DR STRING; 3702.AT2G46070.1; -.
DR iPTMnet; Q8GYQ5; -.
DR PaxDb; Q8GYQ5; -.
DR PRIDE; Q8GYQ5; -.
DR ProteomicsDB; 238902; -. [Q8GYQ5-1]
DR EnsemblPlants; AT2G46070.1; AT2G46070.1; AT2G46070. [Q8GYQ5-1]
DR GeneID; 819215; -.
DR Gramene; AT2G46070.1; AT2G46070.1; AT2G46070. [Q8GYQ5-1]
DR KEGG; ath:AT2G46070; -.
DR Araport; AT2G46070; -.
DR TAIR; locus:2062897; AT2G46070.
DR eggNOG; KOG0660; Eukaryota.
DR InParanoid; Q8GYQ5; -.
DR OMA; DMKSERA; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; Q8GYQ5; -.
DR PRO; PR:Q8GYQ5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GYQ5; baseline and differential.
DR Genevisible; Q8GYQ5; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA: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:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0080026; P:response to indolebutyric acid; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Auxin signaling pathway; Cell membrane;
KW Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..372
FT /note="Mitogen-activated protein kinase 12"
FT /id="PRO_0000245812"
FT DOMAIN 41..327
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 210..372
FT /note="IBR5 binding"
FT /evidence="ECO:0000305|PubMed:19000167"
FT MOTIF 199..201
FT /note="TXY"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 47..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 53
FT /note="Involved in HT1 binding"
FT /evidence="ECO:0000269|PubMed:27923039"
FT MOD_RES 199
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 201
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MUTAGEN 53
FT /note="G->R: Increased stomatal opening and altered CO(2)
FT and ozone (O(3)) responses. Weaker interaction with HT1.
FT Strongly suppressed inhibition of HT1 activity. Loss of
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:27923039"
FT MUTAGEN 70
FT /note="K->R: Loss of kinase activity. Reduced inhibition of
FT HT1 activity. Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:19000167,
FT ECO:0000269|PubMed:27923039"
FT MUTAGEN 122
FT /note="Y->C: Hyperactive kinase, can inhibit HT1 activity."
FT /evidence="ECO:0000269|PubMed:27923039"
SQ SEQUENCE 372 AA; 42475 MW; 1A8FF099D1DC80B9 CRC64;
MSGESSSGST EHCIKVVPTH GGRYVQYNVY GQLFEVSRKY VPPIRPIGRG ACGIVCAAVN
SVTGEKVAIK KIGNAFDNII DAKRTLREIK LLRHMDHENV ITIKDIVRPP QRDIFNDVYI
VYELMDTDLQ RILRSNQTLT SDQCRFLVYQ LLRGLKYVHS ANILHRDLRP SNVLLNSKNE
LKIGDFGLAR TTSDTDFMTE YVVTRWYRAP ELLLNCSEYT AAIDIWSVGC ILGEIMTGQP
LFPGKDYVHQ LRLITELVGS PDNSSLGFLR SDNARRYVRQ LPRYPKQQFA ARFPKMPTTA
IDLLERMLVF DPNRRISVDE ALGHAYLSPH HDVAKEPVCS TPFSFDFEHP SCTEEHIKEL
IYKESVKFNP DH
