ID B7ZD10_DANRE Unreviewed; 186 AA. AC B7ZD10; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-DEC-2022, entry version 97. DE RecName: Full=Dual specificity protein phosphatase {ECO:0000256|RuleBase:RU366038}; DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU366038}; DE EC=3.1.3.48 {ECO:0000256|RuleBase:RU366038}; GN OrderedLocusNames=si:ch211-223p8.8 GN {ECO:0000313|Ensembl:ENSDARP00000118419, GN ECO:0000313|ZFIN:ZDB-GENE-090313-91}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000118419}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000118419} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118419}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [2] {ECO:0000313|Ensembl:ENSDARP00000118419} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118419}; RG Ensembl; RL Submitted (AUG-2013) to UniProtKB. 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. {ECO:0000256|ARBA:ARBA00025567}. 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:0000256|RuleBase:RU366038}. 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:0000256|ARBA:ARBA00001512, CC ECO:0000256|RuleBase:RU366038}; 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:0000256|ARBA:ARBA00001482, CC ECO:0000256|RuleBase:RU366038}; 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:0000256|RuleBase:RU366038}; CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class dual specificity subfamily. CC {ECO:0000256|ARBA:ARBA00008601, ECO:0000256|RuleBase:RU366038}. 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; AL929005; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001139098.1; NM_001145626.1. DR AlphaFoldDB; B7ZD10; -. DR SMR; B7ZD10; -. DR STRING; 7955.ENSDARP00000118419; -. DR PaxDb; B7ZD10; -. DR Ensembl; ENSDART00000147194.2; ENSDARP00000118419.1; ENSDARG00000092650.2. DR GeneID; 100004731; -. DR KEGG; dre:100004731; -. DR ZFIN; ZDB-GENE-090313-91; si:ch211-223p8.8. DR eggNOG; KOG1716; Eukaryota. DR GeneTree; ENSGT00940000162682; -. DR HOGENOM; CLU_027074_11_3_1; -. DR InParanoid; B7ZD10; -. DR OMA; DMYMSHD; -. DR OrthoDB; 1576308at2759; -. DR PhylomeDB; B7ZD10; -. DR TreeFam; TF105128; -. DR Bgee; ENSDARG00000092650; Expressed in muscle tissue and 3 other tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. 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; IBA:GO_Central. DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central. DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro. DR Gene3D; 3.90.190.10; -; 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; IPR000387; Tyr_Pase_dom. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. DR PANTHER; PTHR45682; AGAP008228-PA; 1. DR Pfam; PF00782; DSPc; 1. DR PRINTS; PR01909; ADSPHPHTASEA. DR SMART; SM00195; DSPc; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366038}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912, KW ECO:0000256|RuleBase:RU366038}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 134..154 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 33..181 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000259|PROSITE:PS50054" FT DOMAIN 102..160 FT /note="TYR_PHOSPHATASE_2" FT /evidence="ECO:0000259|PROSITE:PS50056" FT ACT_SITE 126 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR620405-1" SQ SEQUENCE 186 AA; 20928 MW; 57A32CE6E991307A CRC64; MEDTDQILDN VLHKSPTIEE LEGILHGGQL SCNHVDEVWP NLFLGDMYMS HDRYGLWSLG VTHVLNAAHG KMCCKGNDDY YGTTVKYYGV PANDLPTFDI SPFFYPSAQY IHDALSTTGA KVFVHCAVGM SRSAALVLAY LMIYCNFSLV DAILKVKERR WIFPNRGFLK QLITLDNELK LQGTSN //