ID DUS29_ORYLA Reviewed; 203 AA. AC P0C5A1; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 62. 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 Oryzias latipes (Japanese rice fish) (Japanese killifish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae; OC Oryzias. OX NCBI_TaxID=8090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T., RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A., RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S., RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S., RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K., RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome evolution."; RL Nature 447:714-719(2007). 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; BAAF04042477; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; P0C5A1; -. DR SMR; P0C5A1; -. DR STRING; 8090.ENSORLP00000029415; -. DR InParanoid; P0C5A1; -. DR Proteomes; UP000001038; Unplaced. DR Proteomes; UP000265180; Chromosome 9. DR Proteomes; UP000265200; Chromosome 9. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0033549; F:MAP kinase phosphatase activity; IBA:GO_Central. 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:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central. DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB. 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..203 FT /note="Dual specificity phosphatase 29" FT /id="PRO_0000295888" FT DOMAIN 47..193 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT ACT_SITE 138 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT BINDING 137..144 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q68J44" SQ SEQUENCE 203 AA; 23002 MW; B1556191A8B342D7 CRC64; MSSCVEKSRG RNPYAAVQVD PDSDYITPGT LDLEQLFWSG PTAQYAHVNQ VWPRIYLGDE KTALERPALK DLGITHVLNA AVGKWNNVLT GADYYTGMNI RYLGVEADDK PTFNISQYFS QAAEFIHEAL IHPVLVHCVM GRSRSATLVL AYLMIKEHLS VVDAVEHVRQ RRCILPNHGF LKQLRALDIA LQEEKLRLKR KDE //