DUS1B_ARATH
ID DUS1B_ARATH Reviewed; 167 AA.
AC Q9M8K7; Q8LDW2;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Dual specificity protein phosphatase 1B;
DE Short=AtDsPTP1B;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=MAPK phosphatase 2;
DE Short=AtMKP2;
GN Name=DSPTP1B; Synonyms=MKP2; OrderedLocusNames=At3g06110; ORFNames=F28L1.5;
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=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 [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 1).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION AS PHOSPHATASE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-109.
RC STRAIN=cv. Columbia;
RX PubMed=17586809; DOI=10.1074/jbc.m701888200;
RA Lee J.S., Ellis B.E.;
RT "Arabidopsis MAPK phosphatase 2 (MKP2) positively regulates oxidative
RT stress tolerance and inactivates the MPK3 and MPK6 MAPKs.";
RL J. Biol. Chem. 282:25020-25029(2007).
RN [7]
RP FUNCTION IN DEFENSE RESPONSE, INTERACTION WITH MPK3 AND MPK6, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20626661; DOI=10.1111/j.1365-313x.2010.04297.x;
RA Lumbreras V., Vilela B., Irar S., Sole M., Capellades M., Valls M.,
RA Coca M., Pages M.;
RT "MAPK phosphatase MKP2 mediates disease responses in Arabidopsis and
RT functionally interacts with MPK3 and MPK6.";
RL Plant J. 63:1017-1030(2010).
RN [8]
RP FUNCTION, INTERACTION WITH MPK6, MUTAGENESIS OF CYS-109, AND INDUCTION BY
RP STRESS CONDITIONS.
RX PubMed=21057191; DOI=10.4161/psb.5.11.13645;
RA Vilela B., Pages M., Lumbreras V.;
RT "Regulation of MAPK signaling and cell death by MAPK phosphatase MKP2.";
RL Plant Signal. Behav. 5:1497-1500(2010).
CC -!- FUNCTION: Has a dual specificity toward Ser/Thr and Tyr-containing
CC proteins. Prevents biotic and abiotic stress responses, including
CC ozone, oxidative stress and pathogen attacks; represses MAPK activities
CC during hypersensitive response to limit the spread of the HR response
CC after infection by necrotrophic pathogen such as Botrytis cinerea. May
CC be also involved in ABA and salt responses. Dephosphorylates MPK3 and
CC MPK6. {ECO:0000269|PubMed:17586809, ECO:0000269|PubMed:20626661,
CC ECO:0000269|PubMed:21057191}.
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;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Associates with MPK3 and MPK6. Interacts with MPK6 is promoted
CC during HR-like responses triggered by fungal elicitors, whereas
CC interaction with MPK3 in repressed. {ECO:0000269|PubMed:20626661,
CC ECO:0000269|PubMed:21057191}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Upon fungal elicitation,
CC relocalizes surrounding spherical structures that could correspond to
CC epiplasts.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M8K7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M8K7-2; Sequence=VSP_042414;
CC -!- TISSUE SPECIFICITY: Expressed in flowers, seedlings, roots, leaves, and
CC seeds. Present in stomata and meristematic cells.
CC {ECO:0000269|PubMed:20626661}.
CC -!- DEVELOPMENTAL STAGE: In flowers, expressed in stigmatic papillae,
CC anthers, pollen grains and floral abscission zones. As flowers mature,
CC progressively restricted to the abscission zones and the septum of the
CC siliques. During seed development Mainly detected in seeds endosperm
CC layer until the fourth day after germination. In young seedlings,
CC confined to the cotyledons. Later observed in roots, especially in
CC vascular organs and at branching points of lateral roots. In adult
CC leaves, particularly localized in vascular tissues and hydathodes;
CC mostly present in both young and senescent leaves, tissues undergoing
CC developmental transitions. {ECO:0000269|PubMed:20626661}.
CC -!- INDUCTION: Accumulates in response to stress conditions caused by
CC abscisic acid (ABA) or salt treatment. {ECO:0000269|PubMed:21057191}.
CC -!- DISRUPTION PHENOTYPE: Delayed wilting symptoms in response to Ralstonia
CC solanacearum and, by contrast, acceleration of disease progression
CC during Botrytis cinerea infection, suggesting that this phosphatase
CC plays differential functions in biotrophic versus necrotrophic
CC pathogen-induced responses. Prolonged MPK3 and MPK6 activation during
CC ozone treatment. {ECO:0000269|PubMed:20626661}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AC018907; AAF30304.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74344.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74345.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74346.1; -; Genomic_DNA.
DR EMBL; AK117443; BAC42108.1; -; mRNA.
DR EMBL; BT005135; AAO50668.1; -; mRNA.
DR EMBL; AY085765; AAM62982.1; -; mRNA.
DR RefSeq; NP_001189821.1; NM_001202892.1. [Q9M8K7-1]
DR RefSeq; NP_566272.1; NM_111486.3. [Q9M8K7-2]
DR RefSeq; NP_850522.1; NM_180191.3. [Q9M8K7-1]
DR AlphaFoldDB; Q9M8K7; -.
DR SMR; Q9M8K7; -.
DR BioGRID; 5119; 2.
DR STRING; 3702.AT3G06110.3; -.
DR iPTMnet; Q9M8K7; -.
DR PaxDb; Q9M8K7; -.
DR PRIDE; Q9M8K7; -.
DR ProteomicsDB; 221935; -. [Q9M8K7-1]
DR EnsemblPlants; AT3G06110.1; AT3G06110.1; AT3G06110. [Q9M8K7-2]
DR EnsemblPlants; AT3G06110.2; AT3G06110.2; AT3G06110. [Q9M8K7-1]
DR EnsemblPlants; AT3G06110.3; AT3G06110.3; AT3G06110. [Q9M8K7-1]
DR GeneID; 819784; -.
DR Gramene; AT3G06110.1; AT3G06110.1; AT3G06110. [Q9M8K7-2]
DR Gramene; AT3G06110.2; AT3G06110.2; AT3G06110. [Q9M8K7-1]
DR Gramene; AT3G06110.3; AT3G06110.3; AT3G06110. [Q9M8K7-1]
DR KEGG; ath:AT3G06110; -.
DR Araport; AT3G06110; -.
DR TAIR; locus:2082395; AT3G06110.
DR eggNOG; KOG1716; Eukaryota.
DR InParanoid; Q9M8K7; -.
DR OMA; TVYFDEC; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q9M8K7; -.
DR PRO; PR:Q9M8K7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M8K7; baseline and differential.
DR Genevisible; Q9M8K7; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; IDA:TAIR.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IC:TAIR.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:TAIR.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0034051; P:negative regulation of plant-type hypersensitive response; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR GO; GO:0010193; P:response to ozone; IMP:TAIR.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
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; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase;
KW Hypersensitive response elicitation; Nucleus; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..167
FT /note="Dual specificity protein phosphatase 1B"
FT /id="PRO_0000415897"
FT DOMAIN 24..165
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 109
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VAR_SEQ 77..86
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_042414"
FT MUTAGEN 109
FT /note="C->S: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:17586809,
FT ECO:0000269|PubMed:21057191"
SQ SEQUENCE 167 AA; 18431 MW; 57D722910B79A900 CRC64;
MEKVVDLFGV GEANSQKLLE GGKDLSEIQQ GLFIGSVAEA NNKDFLKSSN ITHVLTVAVA
LAPPYPDDFV YKVIEVVDRS ETDLTVYFDE CYSFIDQAIQ SGGGVLVHCF MGMSRSVTIV
VAYLMKKHGM GFSKAMELVR SRRHQAYPNP GFISQLQQFE KSIQGNA
