ID B7ZD10_DANRE Unreviewed; 186 AA. AC B7ZD10; A0A8M1NRN1; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 24-JUL-2024, entry version 106. 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|RefSeq:NP_001139098.1, 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, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118419}; RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; 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., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA 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. RN [3] {ECO:0000313|RefSeq:NP_001139098.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001139098.1}; RX PubMed=27189481; RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I., RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y., RA Bobe J.; RT "Gene evolution and gene expression after whole genome duplication in fish: RT the PhyloFish database."; RL BMC Genomics 17:368-368(2016). RN [4] {ECO:0000313|RefSeq:NP_001139098.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001139098.1}; RG RefSeq; RL Submitted (APR-2024) to UniProtKB. 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|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 STRING; 7955.ENSDARP00000118419; -. DR PaxDb; 7955-ENSDARP00000118419; -. DR Ensembl; ENSDART00000147194.2; ENSDARP00000118419.1; ENSDARG00000092650.2. DR GeneID; 100004731; -. DR KEGG; dre:100004731; -. DR AGR; ZFIN:ZDB-GENE-090313-91; -. DR ZFIN; ZDB-GENE-090313-91; si:ch211-223p8.8. DR eggNOG; KOG1716; Eukaryota. DR HOGENOM; CLU_027074_11_3_1; -. DR OMA; KEKRWIF; -. DR OrthoDB; 1082488at2759; -. DR PhylomeDB; B7ZD10; -. DR TreeFam; TF105128; -. DR Proteomes; UP000000437; Chromosome 13. DR Bgee; ENSDARG00000092650; Expressed in muscle tissue and 3 other cell types or 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 CDD; cd14580; DUSP13A; 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; IPR000387; Tyr_Pase_dom. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. DR PANTHER; PTHR45682; AGAP008228-PA; 1. DR PANTHER; PTHR45682:SF3; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1. DR Pfam; PF00782; DSPc; 1. DR PRINTS; PR01908; ADSPHPHTASE. 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW 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="Tyrosine specific protein phosphatases" 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 //