MPK13_ARATH
ID MPK13_ARATH Reviewed; 363 AA.
AC Q9LQQ9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Mitogen-activated protein kinase 13;
DE Short=AtMPK13;
DE Short=MAP kinase 13;
DE EC=2.7.11.24;
GN Name=MPK13; OrderedLocusNames=At1g07880; ORFNames=F24B9.3;
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=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 [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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) 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 ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=15474000; DOI=10.1016/j.febslet.2004.08.051;
RA Melikant B., Giuliani C., Halbmayer-Watzina S., Limmongkon A.,
RA Heberle-Bors E., Wilson C.;
RT "The Arabidopsis thaliana MEK AtMKK6 activates the MAP kinase AtMPK13.";
RL FEBS Lett. 576:5-8(2004).
RN [7]
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 [8]
RP ACTIVITY REGULATION.
RX PubMed=21098735; DOI=10.1105/tpc.110.077164;
RA Kosetsu K., Matsunaga S., Nakagami H., Colcombet J., Sasabe M., Soyano T.,
RA Takahashi Y., Hirt H., Machida Y.;
RT "The MAP kinase MPK4 is required for cytokinesis in Arabidopsis thaliana.";
RL Plant Cell 22:3778-3790(2010).
RN [9]
RP INTERACTION WITH MKK6.
RX PubMed=21575092; DOI=10.1111/j.1365-313x.2011.04642.x;
RA Zeng Q., Chen J.G., Ellis B.E.;
RT "AtMPK4 is required for male-specific meiotic cytokinesis in Arabidopsis.";
RL Plant J. 67:895-906(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21904115; DOI=10.4161/psb.6.10.17089;
RA Zeng Q., Sritubtim S., Ellis B.E.;
RT "AtMKK6 and AtMPK13 are required for lateral root formation in
RT Arabidopsis.";
RL Plant Signal. Behav. 6:1436-1439(2011).
CC -!- FUNCTION: MKK6-MPK13 module positively regulates lateral root
CC formation. {ECO:0000269|PubMed:21904115}.
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 the MAP kinase kinase
CC MKK6 in vitro. {ECO:0000250, ECO:0000269|PubMed:15474000,
CC ECO:0000269|PubMed:21098735}.
CC -!- SUBUNIT: Interacts with MKK6. {ECO:0000269|PubMed:21575092}.
CC -!- INTERACTION:
CC Q9LQQ9; Q9S7U9: MKK2; NbExp=2; IntAct=EBI-2358762, EBI-994350;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LQQ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LQQ9-2; Sequence=VSP_036334, VSP_036335;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and flower buds.
CC {ECO:0000269|PubMed:15474000}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-191 and Tyr-193, which activates the
CC enzyme. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: RNAi MPK13 displays fewer lateral roots.
CC {ECO:0000269|PubMed:21904115}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
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; AC007583; AAF75067.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28197.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28198.1; -; Genomic_DNA.
DR EMBL; BX818168; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT015822; AAU94385.1; -; mRNA.
DR PIR; C86214; C86214.
DR RefSeq; NP_001030990.1; NM_001035913.2. [Q9LQQ9-1]
DR RefSeq; NP_172266.2; NM_100662.4. [Q9LQQ9-2]
DR AlphaFoldDB; Q9LQQ9; -.
DR SMR; Q9LQQ9; -.
DR BioGRID; 22544; 2.
DR IntAct; Q9LQQ9; 2.
DR MINT; Q9LQQ9; -.
DR STRING; 3702.AT1G07880.2; -.
DR iPTMnet; Q9LQQ9; -.
DR PaxDb; Q9LQQ9; -.
DR PRIDE; Q9LQQ9; -.
DR ProteomicsDB; 238275; -. [Q9LQQ9-1]
DR EnsemblPlants; AT1G07880.1; AT1G07880.1; AT1G07880. [Q9LQQ9-2]
DR EnsemblPlants; AT1G07880.2; AT1G07880.2; AT1G07880. [Q9LQQ9-1]
DR GeneID; 837303; -.
DR Gramene; AT1G07880.1; AT1G07880.1; AT1G07880. [Q9LQQ9-2]
DR Gramene; AT1G07880.2; AT1G07880.2; AT1G07880. [Q9LQQ9-1]
DR KEGG; ath:AT1G07880; -.
DR Araport; AT1G07880; -.
DR TAIR; locus:2026484; AT1G07880.
DR eggNOG; KOG0660; Eukaryota.
DR InParanoid; Q9LQQ9; -.
DR OMA; EIMTFRP; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; Q9LQQ9; -.
DR PRO; PR:Q9LQQ9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQQ9; baseline and differential.
DR Genevisible; Q9LQQ9; 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: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:0010311; P:lateral root formation; IMP:UniProtKB.
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 InterPro; IPR008271; Ser/Thr_kinase_AS.
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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..363
FT /note="Mitogen-activated protein kinase 13"
FT /id="PRO_0000245813"
FT DOMAIN 33..319
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 191..193
FT /note="TXY"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 39..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 191
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 193
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q39026"
FT VAR_SEQ 249..254
FT /note="LLGSPD -> VSKLKP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_036334"
FT VAR_SEQ 255..363
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_036335"
FT CONFLICT Q9LQQ9-2:243
FT /note="L -> P (in Ref. 3; BX818168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 42195 MW; 88472CBA140DB739 CRC64;
MEKREDGGIL TYDGRYVMYN VLGNIFELSS KYIPPIEPIG RGAYGIVCCA TNSETNEEVA
IKKIANAFDN RVDAKRTLRE IKLLSHMDHD NVIKIKDIIE LPEKERFEDV YIVYELMDTD
LHQIIRSTQT LTDDHCQYFL YQILRGLKYI HSANVLHRDL KPSNLVLNTN CDLKICDFGL
ARTSNETEIM TEYVVTRWYR APELLLNSSE YTGAIDIWSV GCIFMEILRR ETLFPGKDYV
QQLKLITELL GSPDDSDLDF LRSDNARKYV KQLPHVQKQS FREKFPNISP MALDLAEKML
VFDPSKRITV DEALKQPYLA SLHEINEEPT CPTPFSFDFE ETALDEQDIK ELVWRESLHF
KNM
