ID DUS29_TAKRU Reviewed; 210 AA. AC P0C599; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 63. DE RecName: Full=Dual specificity phosphatase 29; DE AltName: Full=Dual specificity phosphatase DUPD1; DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q68J44}; DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q68J44}; GN Name=Dusp29; Synonyms=dupd1; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12142439; DOI=10.1126/science.1072104; RA Aparicio S., Chapman J., Stupka E., Putnam N., Chia J.M., Dehal P., RA Christoffels A., Rash S., Hoon S., Smit A., Gelpke M.D., Roach J., Oh T., RA Ho I.Y., Wong M., Detter C., Verhoef F., Predki P., Tay A., Lucas S., RA Richardson P., Smith S.F., Clark M.S., Edwards Y.J., Doggett N., RA Zharkikh A., Tavtigian S.V., Pruss D., Barnstead M., Evans C., Baden H., RA Powell J., Glusman G., Rowen L., Hood L., Tan Y.H., Elgar G., Hawkins T., RA Venkatesh B., Rokhsar D., Brenner S.; RT "Whole-genome shotgun assembly and analysis of the genome of Fugu RT rubripes."; RL Science 297:1301-1310(2002). CC -!- FUNCTION: Dual specificity phosphatase able to dephosphorylate CC phosphotyrosine, phosphoserine and phosphothreonine residues, with a CC preference for phosphotyrosine as a substrate. CC {ECO:0000250|UniProtKB:Q68J44}. CC -!- FUNCTION: Dual specificity phosphatase able to dephosphorylate CC phosphotyrosine, phosphoserine and phosphothreonine residues within the CC same substrate, with a preference for phosphotyrosine as a substrate CC (By similarity). Involved in the modulation of AMPK and MAPK1/2 CC signaling pathways (By similarity). {ECO:0000250|UniProtKB:Q68J44, CC ECO:0000250|UniProtKB:Q8BK84}. 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 Evidence={ECO:0000250|UniProtKB:Q68J44}; 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 Evidence={ECO:0000250|UniProtKB:Q68J44}; 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 Evidence={ECO:0000250|UniProtKB:Q68J44}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68J44}. Nucleus CC {ECO:0000250|UniProtKB:Q8BK84}. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class dual specificity subfamily. {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; CAAB01002848; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; P0C599; -. DR SMR; P0C599; -. DR STRING; 31033.ENSTRUP00000078835; -. DR eggNOG; KOG1716; Eukaryota. DR InParanoid; P0C599; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. 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; ISS:UniProtKB. DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB. DR CDD; cd14575; DUPD1; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR InterPro; IPR020405; Atypical_DUSP_subfamA. DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR000387; Tyr_Pase_dom. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. DR PANTHER; PTHR45682; AGAP008228-PA; 1. DR PANTHER; PTHR45682:SF6; DUAL SPECIFICITY PHOSPHATASE 29; 1. DR Pfam; PF00782; DSPc; 1. DR PRINTS; PR01908; ADSPHPHTASE. DR PRINTS; PR01909; ADSPHPHTASEA. DR SMART; SM00195; DSPc; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. PE 3: Inferred from homology; KW Cytoplasm; Hydrolase; Nucleus; Protein phosphatase; Reference proteome. FT CHAIN 1..210 FT /note="Dual specificity phosphatase 29" FT /id="PRO_0000295886" FT DOMAIN 46..194 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT ACT_SITE 139 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT BINDING 138..145 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q68J44" SQ SEQUENCE 210 AA; 23702 MW; 940C87A022441CF0 CRC64; MSSVVKSKSK NPYAAVRVDP DSDYITPGTL DLEQLFWSGP GVQYTHVNQV WPGIYIGDEK TALERPGLRD LGITHVLNAA EGKWNNVLTG ADYYSDTNIQ YYGIEADDKP TFNISQFFHP AAQFIHEALS QPHNVLVHCV MGRSRSATLV LAYLMMEHSL SVVDAIEHVR QRRCILPNHG FLKQLRALDI TLQEARLKQK TQTQGQEKPR //