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 27-MAR-2024, entry version 133. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q9ZR37; -. DR iPTMnet; Q9ZR37; -. DR PaxDb; 3702-AT3G23610-3; -. 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; AT3G23610; DSPTP1. DR eggNOG; KOG1716; Eukaryota. DR InParanoid; Q9ZR37; -. DR OMA; CAYLMWK; -. DR OrthoDB; 3035478at2759; -. DR PhylomeDB; Q9ZR37; -. DR PRO; PR:Q9ZR37; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9ZR37; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005516; F:calmodulin binding; IDA:TAIR. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. 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:0006470; P:protein dephosphorylation; IDA:TAIR. DR CDD; cd14498; DSP; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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 PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR10159:SF519; DUAL SPECIFICITY PROTEIN PHOSPHATASE MPK3; 1. DR Pfam; PF00782; DSPc; 1. DR PRINTS; PR01908; ADSPHPHTASE. DR SMART; SM00195; DSPc; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. DR Genevisible; Q9ZR37; AT. 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 //