ID B7ZD10_DANRE Unreviewed; 186 AA. AC B7ZD10; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 13-NOV-2019, entry version 84. 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 Name=si:ch211-223p8.8 {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 Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000118419, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000118419, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118419, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA 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., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA 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., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human 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, with CC a 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, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CC Evidence={ECO:0000256|RuleBase:RU366038}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl- CC [protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA- CC COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; CC EC=3.1.3.16; Evidence={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, CC Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; CC Evidence={ECO:0000256|RuleBase:RU366038}; CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC Non-receptor class dual specificity subfamily. CC {ECO:0000256|RuleBase:RU366038, ECO:0000256|SAAS:SAAS00543478}. 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 STRING; 7955.ENSDARP00000118419; -. DR PaxDb; B7ZD10; -. DR Ensembl; ENSDART00000147194; ENSDARP00000118419; ENSDARG00000092650. DR GeneID; 100004731; -. DR KEGG; dre:100004731; -. DR ZFIN; ZDB-GENE-090313-91; si:ch211-223p8.8. DR eggNOG; KOG1716; Eukaryota. DR eggNOG; COG2453; LUCA. DR GeneTree; ENSGT00940000162682; -. DR InParanoid; B7ZD10; -. DR KO; K14165; -. DR OMA; GKMCCKG; -. DR OrthoDB; 1576308at2759; -. DR PhylomeDB; B7ZD10; -. DR TreeFam; TF105128; -. DR Proteomes; UP000000437; Chromosome 13. DR Bgee; ENSDARG00000092650; Expressed in 6 organ(s), highest expression level in muscle tissue. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:UniProtKB-UniRule. DR Gene3D; 3.90.190.10; -; 1. DR InterPro; IPR020417; Atypical_DUSP. 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_PHOSPHATASE_dom. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. DR Pfam; PF00782; DSPc; 1. DR PRINTS; PR01908; ADSPHPHTASE. DR PRINTS; PR01909; ADSPHPHTASEA. DR SMART; SM00195; DSPc; 1. DR SUPFAM; SSF52799; SSF52799; 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 Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Hydrolase {ECO:0000256|RuleBase:RU366038, KW ECO:0000256|SAAS:SAAS01097268}; Membrane {ECO:0000256|SAM:Phobius}; KW Protein phosphatase {ECO:0000256|RuleBase:RU366038}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 134 154 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 34 180 Tyrosine-protein phosphatase. FT {ECO:0000259|PROSITE:PS50054}. FT DOMAIN 102 160 TYR_PHOSPHATASE_2. {ECO:0000259|PROSITE: FT PS50056}. 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 //