MKP1_ARATH
ID MKP1_ARATH Reviewed; 784 AA.
AC Q9C5S1; Q940K2; Q9M3C4;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein-tyrosine-phosphatase MKP1;
DE EC=3.1.3.48;
DE AltName: Full=Mitogen-activated protein kinase phosphatase 1;
DE Short=AtMKP1;
GN Name=MKP1; OrderedLocusNames=At3g55270; ORFNames=T26I12.150;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11274055; DOI=10.1101/gad.192601;
RA Ulm R., Revenkova E., di Sansebastiano G.P., Bechtold N., Paszkowski J.;
RT "Mitogen-activated protein kinase phosphatase is required for genotoxic
RT stress relief in Arabidopsis.";
RL Genes Dev. 15:699-709(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 FUNCTION, INTERACTION WITH MPK6, AND MUTAGENESIS OF CYS-235.
RX PubMed=12456655; DOI=10.1093/emboj/cdf646;
RA Ulm R., Ichimura K., Mizoguchi T., Peck S.C., Zhu T., Wang X.,
RA Shinozaki K., Paszkowski J.;
RT "Distinct regulation of salinity and genotoxic stress responses by
RT Arabidopsis MAP kinase phosphatase 1.";
RL EMBO J. 21:6483-6493(2002).
RN [6]
RP FUNCTION.
RX PubMed=16913867; DOI=10.1111/j.1365-3040.2006.01555.x;
RA Kalbina I., Strid A.;
RT "The role of NADPH oxidase and MAP kinase phosphatase in UV-B-dependent
RT gene expression in Arabidopsis.";
RL Plant Cell Environ. 29:1783-1793(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP FUNCTION, INTERACTION WITH MPK6, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19789277; DOI=10.1105/tpc.109.067678;
RA Bartels S., Anderson J.C., Gonzalez Besteiro M.A., Carreri A., Hirt H.,
RA Buchala A., Metraux J.P., Peck S.C., Ulm R.;
RT "MAP kinase phosphatase1 and protein tyrosine phosphatase1 are repressors
RT of salicylic acid synthesis and SNC1-mediated responses in Arabidopsis.";
RL Plant Cell 21:2884-2897(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP FUNCTION, INTERACTION WITH MPK6, AND PHOSPHORYLATION AT THR-64; THR-109;
RP SER-558 AND SER-572.
RX PubMed=21455789; DOI=10.1007/s00299-011-1064-4;
RA Park H.C., Song E.H., Nguyen X.C., Lee K., Kim K.E., Kim H.S., Lee S.M.,
RA Kim S.H., Bae D.W., Yun D.J., Chung W.S.;
RT "Arabidopsis MAP kinase phosphatase 1 is phosphorylated and activated by
RT its substrate AtMPK6.";
RL Plant Cell Rep. 30:1523-1531(2011).
RN [11]
RP FUNCTION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=21447069; DOI=10.1111/j.1365-313x.2011.04588.x;
RA Anderson J.C., Bartels S., Gonzalez Besteiro M.A., Shahollari B., Ulm R.,
RA Peck S.C.;
RT "Arabidopsis MAP Kinase Phosphatase 1 (AtMKP1) negatively regulates MPK6-
RT mediated PAMP responses and resistance against bacteria.";
RL Plant J. 67:258-268(2011).
RN [12]
RP FUNCTION.
RX PubMed=21790814; DOI=10.1111/j.1365-313x.2011.04725.x;
RA Besteiro M.A., Bartels S., Albert A., Ulm R.;
RT "Arabidopsis MAP kinase phosphatase 1 and its target MAP kinases 3 and 6
RT antagonistically determine UV-B stress tolerance, independent of the UVR8
RT photoreceptor pathway.";
RL Plant J. 68:727-737(2011).
CC -!- FUNCTION: Protein-tyrosine-phosphatase that acts as a negative
CC regulator of MPK6 and MPK3 signaling by dephosphorylating and
CC repressing MPK6 and MPK3. Modulates defense response by repressing
CC salicylic acid (SA) production, camalexin biosynthesis and SNC1-
CC mediated responses. Acts as a negative regulator of MPK6-mediated
CC pathogen-associated molecular pattern (PAMP) responses, including MPK6
CC and MPK3 activation, accumulation of extracellular reactive oxygen
CC species and inhibition of seedling growth. Involved in UV-B stress
CC tolerance. May be involved in salt and genotoxic stress responses.
CC {ECO:0000269|PubMed:11274055, ECO:0000269|PubMed:12456655,
CC ECO:0000269|PubMed:16913867, ECO:0000269|PubMed:19789277,
CC ECO:0000269|PubMed:21447069, ECO:0000269|PubMed:21455789,
CC ECO:0000269|PubMed:21790814}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBUNIT: Interacts with MPK6. May interact with MPK3 and MPK4.
CC {ECO:0000269|PubMed:12456655, ECO:0000269|PubMed:19789277,
CC ECO:0000269|PubMed:21455789}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19789277}.
CC -!- PTM: Phosphorylated on threonine and serine residues by MPK6.
CC {ECO:0000269|PubMed:21455789}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions in Wassilewskija (Ws) ecotype (PubMed:11274055), but
CC Columbia (Col) ecotype show growth defects, elevated levels of
CC salicylic acid (SA) and constitutive defense responses
CC (PubMed:19789277). {ECO:0000269|PubMed:11274055,
CC ECO:0000269|PubMed:19789277}.
CC -!- MISCELLANEOUS: The observed mkp1 phenotype in Col ecotype is largely
CC due to the Col-specific TIR-NB-LRR receptor-like protein SNC1, which is
CC absent in Ws ecotype. {ECO:0000305|PubMed:19789277}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB75761.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF312745; AAK29382.1; -; mRNA.
DR EMBL; AL132954; CAB75761.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79361.2; -; Genomic_DNA.
DR EMBL; AY054509; AAK96700.1; -; mRNA.
DR PIR; T47666; T47666.
DR RefSeq; NP_567018.5; NM_115385.7.
DR AlphaFoldDB; Q9C5S1; -.
DR SMR; Q9C5S1; -.
DR BioGRID; 10009; 1.
DR STRING; 3702.AT3G55270.1; -.
DR iPTMnet; Q9C5S1; -.
DR PaxDb; Q9C5S1; -.
DR PeptideAtlas; Q9C5S1; -.
DR PRIDE; Q9C5S1; -.
DR ProteomicsDB; 238292; -.
DR GeneID; 824693; -.
DR KEGG; ath:AT3G55270; -.
DR Araport; AT3G55270; -.
DR TAIR; locus:2100601; AT3G55270.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_357766_0_0_1; -.
DR InParanoid; Q9C5S1; -.
DR OrthoDB; 185577at2759; -.
DR PhylomeDB; Q9C5S1; -.
DR PRO; PR:Q9C5S1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C5S1; baseline and differential.
DR Genevisible; Q9C5S1; AT.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IDA:TAIR.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:1902065; P:response to L-glutamate; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IMP:TAIR.
DR GO; GO:0010225; P:response to UV-C; IMP:TAIR.
DR Gene3D; 3.40.20.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Phosphoprotein; Plant defense; Protein phosphatase;
KW Reference proteome; Stress response.
FT CHAIN 1..784
FT /note="Protein-tyrosine-phosphatase MKP1"
FT /id="PRO_0000417330"
FT DOMAIN 149..291
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 235
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 235..241
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21455789"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21455789"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21455789"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21455789"
FT MUTAGEN 235
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12456655"
FT CONFLICT 712
FT /note="S -> N (in Ref. 4; AAK96700)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 784 AA; 85964 MW; DF14442F304BD1ED CRC64;
MVGREDAMGN DEAPPGSKKM FWRSASWSAS RTASQVPEGD EQSLNIPCAI SSGPSRRCPA
APLTPRSHHN SKARACLPPL QPLAISRRSL DEWPKAGSDD VGEWPHPPTP SGNKTGERLK
LDLSSTQQRV TDKSSGLAKR EKIAFFDKEC SKVADHIYVG GDAVAKDKSI LKNNGITHIL
NCVGFICPEY FKSDFCYRSL WLQDSPSEDI TSILYDVFDY FEDVREQSGR IFVHCCQGVS
RSTSLVIAYL MWREGQSFDD AFQYVKSARG IADPNMGFAC QLLQCQKRVH AFPLSPTSLL
RMYKMSPHSP YDPLHLVPKL LNDPCPGSLD SRGAFIIQLP SAIYIWVGRQ CETIMEKDAK
AAVCQIARYE KVEAPIMVVR EGDEPVYYWD AFASILPMIG GSVIKVQPGD RKVDAYNLDF
EIFQKAIEGG FVPTLASSNN EHETHLPARE NSWSSLKCKF ASRFDKGFRY VSKTPLSRVY
SDSMMIVHSS GSPSSTTSSS STASPPFLSP DSVCSTNSGN SLKSFSQSSG RSSLRPSIPP
SLTLPKFSSL SLLPSQTSPK ESRGVNTFLQ PSPNRKASPS LAERRGSLKG SLKLPGLADS
NRGTPAFTLH PDDSNDIVFN LEGIRNGDLY PPSDCKGTSV DSDLPEKEII SLISCSKSDR
HKSGGDTDSS GQPLACRWPS MEMITKLSRA YLDSESVIAI PLPSDAVGET GSRNLYIWIG
KSFSLDNNCS LVDSNKAADT VENVDWVQIG ESILCQMDLP KDTPIKIVRE SEDQTELLAL
LSAL
