DUS1_ARATH
ID DUS1_ARATH Reviewed; 198 AA.
AC Q9ZR37; B3H4F5; F4J449; Q9LUG6;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Dual specificity protein phosphatase 1;
DE Short=AtDsPTP1;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
GN Name=DSPTP1; OrderedLocusNames=At3g23610; ORFNames=MDB19.10;
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] (ISOFORM 1), FUNCTION AS DUAL-SPECIFICITY
RP PROTEIN PHOSPHATASE, MUTAGENESIS OF CYS-135, TISSUE SPECIFICITY, AND
RP ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=10036776; DOI=10.1046/j.1365-313x.1998.00327.x;
RA Gupta R., Huang Y., Kieber J., Luan S.;
RT "Identification of a dual-specificity protein phosphatase that inactivates
RT a MAP kinase from Arabidopsis.";
RL Plant J. 16:581-589(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 INTERACTION WITH CALMODULIN, AND MUTAGENESIS OF ILE-32; LEU-35 AND LYS-166.
RC STRAIN=cv. Columbia;
RX PubMed=14570888; DOI=10.1074/jbc.m310709200;
RA Yoo J.H., Cheong M.S., Park C.Y., Moon B.C., Kim M.C., Kang Y.H.,
RA Park H.C., Choi M.S., Lee J.H., Jung W.Y., Yoon H.W., Chung W.S., Lim C.O.,
RA Lee S.Y., Cho M.J.;
RT "Regulation of the dual specificity protein phosphatase, DsPTP1, through
RT interactions with calmodulin.";
RL J. Biol. Chem. 279:848-858(2004).
CC -!- FUNCTION: Has a dual specificity toward Ser/Thr and Tyr-containing
CC proteins. Dephosphorylates MPK4 in vitro.
CC {ECO:0000269|PubMed:10036776}.
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 -!- ACTIVITY REGULATION: Inhibited by sodium vanadate and sodium tungstate.
CC NaF and spermifine repress specifically phosphoserine and
CC phosphothreonine phosphatase activity. {ECO:0000269|PubMed:10036776}.
CC -!- SUBUNIT: Interacts with calmodulin (CaM) in a calcium Ca(2+)-dependent
CC manner. {ECO:0000269|PubMed:14570888}.
CC -!- INTERACTION:
CC Q9ZR37; Q9ZNV8: AHP2; NbExp=3; IntAct=EBI-25512239, EBI-1100687;
CC Q9ZR37; A0A178WKP3: AXX17_At1g14230; NbExp=3; IntAct=EBI-25512239, EBI-25516605;
CC Q9ZR37; Q9FJ55: CIPK19; NbExp=3; IntAct=EBI-25512239, EBI-16967606;
CC Q9ZR37; Q84WK5: GID8; NbExp=3; IntAct=EBI-25512239, EBI-4466510;
CC Q9ZR37; Q84JU4: IBR5; NbExp=3; IntAct=EBI-25512239, EBI-604555;
CC Q9ZR37; Q9S7U9: MKK2; NbExp=5; IntAct=EBI-25512239, EBI-994350;
CC Q9ZR37; Q8GYH7: MMS21; NbExp=3; IntAct=EBI-25512239, EBI-25512915;
CC Q9ZR37; Q39023: MPK3; NbExp=3; IntAct=EBI-25512239, EBI-349526;
CC Q9ZR37; Q9FMC8: OFP13; NbExp=3; IntAct=EBI-25512239, EBI-15204858;
CC Q9ZR37; Q93ZX1: RFC4; NbExp=3; IntAct=EBI-25512239, EBI-4470690;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9ZR37-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZR37-2; Sequence=VSP_042412;
CC Name=3;
CC IsoId=Q9ZR37-3; Sequence=VSP_042413;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers.
CC {ECO:0000269|PubMed:10036776}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02780.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Y18620; CAA77232.1; -; mRNA.
DR EMBL; AB023036; BAB02780.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76784.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76785.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76786.1; -; Genomic_DNA.
DR RefSeq; NP_001118683.1; NM_001125211.3. [Q9ZR37-2]
DR RefSeq; NP_001189955.1; NM_001203026.1. [Q9ZR37-3]
DR RefSeq; NP_189003.1; NM_113265.1. [Q9ZR37-1]
DR AlphaFoldDB; Q9ZR37; -.
DR SMR; Q9ZR37; -.
DR BioGRID; 7273; 11.
DR IntAct; Q9ZR37; 10.
DR STRING; 3702.AT3G23610.3; -.
DR iPTMnet; Q9ZR37; -.
DR PaxDb; Q9ZR37; -.
DR PRIDE; Q9ZR37; -.
DR ProteomicsDB; 222229; -. [Q9ZR37-1]
DR EnsemblPlants; AT3G23610.1; AT3G23610.1; AT3G23610. [Q9ZR37-1]
DR EnsemblPlants; AT3G23610.2; AT3G23610.2; AT3G23610. [Q9ZR37-2]
DR EnsemblPlants; AT3G23610.3; AT3G23610.3; AT3G23610. [Q9ZR37-3]
DR GeneID; 821941; -.
DR Gramene; AT3G23610.1; AT3G23610.1; AT3G23610. [Q9ZR37-1]
DR Gramene; AT3G23610.2; AT3G23610.2; AT3G23610. [Q9ZR37-2]
DR Gramene; AT3G23610.3; AT3G23610.3; AT3G23610. [Q9ZR37-3]
DR KEGG; ath:AT3G23610; -.
DR Araport; AT3G23610; -.
DR TAIR; locus:2088080; AT3G23610.
DR eggNOG; KOG1716; Eukaryota.
DR InParanoid; Q9ZR37; -.
DR OMA; CAYLMWK; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q9ZR37; -.
DR PRO; PR:Q9ZR37; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9ZR37; baseline and differential.
DR Genevisible; Q9ZR37; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; 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:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IDA: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; Calmodulin-binding; Cytoplasm; Hydrolase; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..198
FT /note="Dual specificity protein phosphatase 1"
FT /id="PRO_0000415896"
FT DOMAIN 50..191
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..47
FT /note="CaM binding domain 1"
FT REGION 151..180
FT /note="CaM binding domain 2"
FT ACT_SITE 135
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VAR_SEQ 191..198
FT /note="VSDQFFSF -> GKQVTIAQCQA (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042412"
FT VAR_SEQ 192..198
FT /note="SDQFFSF -> VVEEKTVPCKYLLHASSFFSIKQGSKLRLHNVRREDH (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_042413"
FT MUTAGEN 32
FT /note="I->R: Impaired CaM binding and loss of phosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:14570888"
FT MUTAGEN 35
FT /note="L->R: Impaired CaM binding."
FT /evidence="ECO:0000269|PubMed:14570888"
FT MUTAGEN 135
FT /note="C->S: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10036776"
FT MUTAGEN 166
FT /note="K->E: Impaired CaM binding."
FT /evidence="ECO:0000269|PubMed:14570888"
SQ SEQUENCE 198 AA; 22017 MW; EBF1C98A177E6450 CRC64;
MSSRDRGSPS SSSSSSSLPG IEKYNEKVKN QIQALVRVIK VARTYRDDNV PSLIEQGLYL
GSVAAASNKN VLKSYNVTHI LTVASSLRPA HPDDFVYKVV RVVDKEDTNL EMYFDECVDF
IDEAKRQGGS VLVHCFVGKS RSVTIVVAYL MKKHGMTLAQ ALQHVKSKRP VASPNAGFIR
QLQDLEKSMQ VSDQFFSF
