MPK1_ARATH
ID MPK1_ARATH Reviewed; 370 AA.
AC Q39021; Q9SY63;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Mitogen-activated protein kinase 1;
DE Short=AtMPK1;
DE Short=MAP kinase 1;
DE EC=2.7.11.24;
GN Name=MPK1; OrderedLocusNames=At1g10210; ORFNames=F14N23.9;
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], ACTIVITY REGULATION, TISSUE SPECIFICITY, AND
RP PHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=8130795; DOI=10.1046/j.1365-313x.1994.5010111.x;
RA Mizoguchi T., Gotoh Y., Nishida E., Yamaguchi-Shinozaki K., Hayashida N.,
RA Iwasaki T., Kamada H., Shinozaki K.;
RT "Characterization of two cDNAs that encode MAP kinase homologues in
RT Arabidopsis thaliana and analysis of the possible role of auxin in
RT activating such kinase activities in cultured cells.";
RL Plant J. 5:111-122(1994).
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 INTERACTION WITH MKK3.
RX PubMed=17933903; DOI=10.1105/tpc.106.050039;
RA Doczi R., Brader G., Pettko-Szandtner A., Rajh I., Djamei A., Pitzschke A.,
RA Teige M., Hirt H.;
RT "The Arabidopsis mitogen-activated protein kinase kinase MKK3 is upstream
RT of group C mitogen-activated protein kinases and participates in pathogen
RT signaling.";
RL Plant Cell 19:3266-3279(2007).
RN [8]
RP INTERACTION WITH MKK3.
RC STRAIN=cv. Columbia;
RX PubMed=25680457; DOI=10.1007/s11103-015-0295-0;
RA Matsuoka D., Yasufuku T., Furuya T., Nanmori T.;
RT "An abscisic acid inducible Arabidopsis MAPKKK, MAPKKK18 regulates leaf
RT senescence via its kinase activity.";
RL Plant Mol. Biol. 87:565-575(2015).
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:0000305|PubMed:8130795}.
CC -!- SUBUNIT: Interacts with MKK3. {ECO:0000269|PubMed:17933903,
CC ECO:0000269|PubMed:25680457}.
CC -!- INTERACTION:
CC Q39021; Q8LGS1: MARD1; NbExp=5; IntAct=EBI-1238932, EBI-4443654;
CC Q39021; O80396: MKK3; NbExp=4; IntAct=EBI-1238932, EBI-2358337;
CC Q39021; O23160: MYB73; NbExp=3; IntAct=EBI-1238932, EBI-25506855;
CC Q39021; Q9LNV3: STP2; NbExp=3; IntAct=EBI-1238932, EBI-25512884;
CC Q39021; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-1238932, EBI-15192297;
CC -!- TISSUE SPECIFICITY: Highest levels in the stem. Present in the leaf,
CC root and flower, but not in seeds. {ECO:0000269|PubMed:8130795}.
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 (By similarity). Autophosphorylated on threonine and tyrosine
CC residues (Probable). Phosphorylated on Ser residue. {ECO:0000250,
CC ECO:0000269|PubMed:8130795, 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; D14713; BAA03535.1; -; mRNA.
DR EMBL; AC005489; AAD32871.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28553.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28554.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58066.1; -; Genomic_DNA.
DR EMBL; AY059937; AAL24419.1; -; mRNA.
DR EMBL; BT000062; AAN15381.1; -; mRNA.
DR PIR; F86236; F86236.
DR RefSeq; NP_001031017.1; NM_001035940.2.
DR RefSeq; NP_001320530.1; NM_001331892.1.
DR RefSeq; NP_172492.1; NM_100895.3.
DR AlphaFoldDB; Q39021; -.
DR SMR; Q39021; -.
DR BioGRID; 22799; 157.
DR IntAct; Q39021; 7.
DR STRING; 3702.AT1G10210.2; -.
DR iPTMnet; Q39021; -.
DR PaxDb; Q39021; -.
DR PRIDE; Q39021; -.
DR ProteomicsDB; 238270; -.
DR EnsemblPlants; AT1G10210.1; AT1G10210.1; AT1G10210.
DR EnsemblPlants; AT1G10210.2; AT1G10210.2; AT1G10210.
DR EnsemblPlants; AT1G10210.3; AT1G10210.3; AT1G10210.
DR GeneID; 837559; -.
DR Gramene; AT1G10210.1; AT1G10210.1; AT1G10210.
DR Gramene; AT1G10210.2; AT1G10210.2; AT1G10210.
DR Gramene; AT1G10210.3; AT1G10210.3; AT1G10210.
DR KEGG; ath:AT1G10210; -.
DR Araport; AT1G10210; -.
DR TAIR; locus:2012808; AT1G10210.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q39021; -.
DR OMA; SFFDFDY; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; Q39021; -.
DR BRENDA; 2.7.11.24; 399.
DR PRO; PR:Q39021; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39021; baseline and differential.
DR Genevisible; Q39021; 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:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0004707; F:MAP kinase activity; IDA:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA: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:0009734; P:auxin-activated signaling pathway; TAS:TAIR.
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; 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; 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 ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..370
FT /note="Mitogen-activated protein kinase 1"
FT /id="PRO_0000186310"
FT DOMAIN 32..319
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 191..193
FT /note="TXY"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 38..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 61
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 CONFLICT 129
FT /note="V -> R (in Ref. 1; BAA03535)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="L -> I (in Ref. 1; BAA03535)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="D -> V (in Ref. 1; BAA03535)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="G -> C (in Ref. 1; BAA03535)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="V -> A (in Ref. 1; BAA03535)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="M -> I (in Ref. 1; BAA03535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 42644 MW; F2962D7881C87A1B CRC64;
MATLVDPPNG IRNEGKHYFS MWQTLFEIDT KYMPIKPIGR GAYGVVCSSV NSDTNEKVAI
KKIHNVYENR IDALRTLREL KLLRHLRHEN VIALKDVMMP IHKMSFKDVY LVYELMDTDL
HQIIKSSQVL SNDHCQYFLF QLLRGLKYIH SANILHRDLK PGNLLVNANC DLKICDFGLA
RASNTKGQFM TEYVVTRWYR APELLLCCDN YGTSIDVWSV GCIFAELLGR KPIFQGTECL
NQLKLIVNIL GSQREEDLEF IDNPKAKRYI RSLPYSPGMS LSRLYPGAHV LAIDLLQKML
VFDPSKRISV SEALQHPYMA PLYDPNANPP AQVPIDLDVD EDLREEMIRE MMWNEMLHYH
PQASTLNTEL
