ID Q6PBT4_DANRE Unreviewed; 368 AA.
AC Q6PBT4; F6PBQ2; Q1LV11;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 157.
DE RecName: Full=Dual specificity protein phosphatase {ECO:0000256|PIRNR:PIRNR000939};
DE EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR000939};
DE EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000939};
GN Name=dusp5 {ECO:0000313|EMBL:AAH59592.1,
GN ECO:0000313|Ensembl:ENSDARP00000005408,
GN ECO:0000313|RefSeq:NP_997730.1, ECO:0000313|ZFIN:ZDB-GENE-010625-1};
GN Synonyms=dusp5-2 {ECO:0000313|EMBL:CAK10873.1}, wu:fc86e02
GN {ECO:0000313|RefSeq:NP_997730.1};
GN ORFNames=DKEY-262O11.5-001-2 {ECO:0000313|EMBL:CAK10873.1};
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|EMBL:CAK10873.1};
RN [1] {ECO:0000313|EMBL:AAH59592.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Wild-type {ECO:0000313|EMBL:AAH59592.1};
RC TISSUE=Eye {ECO:0000313|EMBL:AAH59592.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:NP_997730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_997730.1};
RX PubMed=15827125;
RA Weber G.J., Choe S.E., Dooley K.A., Paffett-Lugassy N.N., Zhou Y.,
RA Zon L.I.;
RT "Mutant-specific gene programs in the zebrafish.";
RL Blood 106:521-530(2005).
RN [3] {ECO:0000313|RefSeq:NP_997730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_997730.1};
RX PubMed=15802528; DOI=10.1182/blood-2004-12-4653;
RA Sumanas S., Jorniak T., Lin S.;
RT "Identification of novel vascular endothelial-specific genes by the
RT microarray analysis of the zebrafish cloche mutants.";
RL Blood 106:534-541(2005).
RN [4] {ECO:0000313|RefSeq:NP_997730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_997730.1};
RX PubMed=15937927; DOI=10.1002/dvdy.20444;
RA Qian F., Zhen F., Ong C., Jin S.W., Meng Soo H., Stainier D.Y., Lin S.,
RA Peng J., Wen Z.;
RT "Microarray analysis of zebrafish cloche mutant using amplified cDNA and
RT identification of potential downstream target genes.";
RL Dev. Dyn. 233:1163-1172(2005).
RN [5] {ECO:0000313|RefSeq:NP_997730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_997730.1};
RX PubMed=16336046; DOI=10.1371/journal.pbio.0040010;
RA Sumanas S., Lin S.;
RT "Ets1-related protein is a key regulator of vasculogenesis in zebrafish.";
RL PLoS Biol. 4:e10-e10(2006).
RN [6] {ECO:0000313|EMBL:CAK10873.1}
RP NUCLEOTIDE SEQUENCE.
RA Tracey A.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|RefSeq:NP_997730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_997730.1};
RX PubMed=18927432;
RA Pramanik K., Chun C.Z., Garnaas M.K., Samant G.V., Li K., Horswill M.A.,
RA North P.E., Ramchandran R.;
RT "Dusp-5 and Snrk-1 coordinately function during vascular development and
RT disease.";
RL Blood 113:1184-1191(2009).
RN [8] {ECO:0000313|Ensembl:ENSDARP00000005408}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000005408};
RG Ensembl;
RL Submitted (FEB-2012) to UniProtKB.
RN [9] {ECO:0000313|Ensembl:ENSDARP00000005408, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000005408};
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 [10] {ECO:0000313|RefSeq:NP_997730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_997730.1};
RX PubMed=27428998;
RA Faltermann S., Hutter S., Christen V., Hettich T., Fent K.;
RT "Anti-Inflammatory Activity of Cyanobacterial Serine Protease Inhibitors
RT Aeruginosin 828A and Cyanopeptolin 1020 in Human Hepatoma Cell Line Huh7
RT and Effects in Zebrafish (Danio rerio).";
RL Toxins 8:E219-E219(2016).
RN [11] {ECO:0000313|RefSeq:NP_997730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_997730.1};
RX PubMed=28992598;
RA Wu M., Liu S., Hu L., Qu H., Pan C., Lei P., Shen Y., Yang M.;
RT "Global transcriptomic analysis of zebrafish in response to embryonic
RT exposure to three antidepressants, amitriptyline, fluoxetine and
RT mianserin.";
RL Aquat. Toxicol. 192:274-283(2017).
RN [12] {ECO:0000313|RefSeq:NP_997730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_997730.1};
RX PubMed=28723572;
RA Quillien A., Abdalla M., Yu J., Ou J., Zhu L.J., Lawson N.D.;
RT "Robust Identification of Developmentally Active Endothelial Enhancers in
RT Zebrafish Using FANS-Assisted ATAC-Seq.";
RL Cell Rep. 20:709-720(2017).
RN [13] {ECO:0000313|RefSeq:NP_997730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_997730.1};
RX PubMed=28536097;
RA Fish J.E., Cantu Gutierrez M., Dang L.T., Khyzha N., Chen Z., Veitch S.,
RA Cheng H.S., Khor M., Antounians L., Njock M.S., Boudreau E., Herman A.M.,
RA Rhyner A.M., Ruiz O.E., Eisenhoffer G.T., Medina-Rivera A., Wilson M.D.,
RA Wythe J.D.;
RT "Dynamic regulation of VEGF-inducible genes by an ERK/ERG/p300
RT transcriptional network.";
RL Development 144:2428-2444(2017).
RN [14] {ECO:0000313|RefSeq:NP_997730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_997730.1};
RX PubMed=27615194;
RA Takeuchi M., Yamaguchi S., Sakakibara Y., Hayashi T., Matsuda K., Hara Y.,
RA Tanegashima C., Shimizu T., Kuraku S., Hibi M.;
RT "Gene expression profiling of granule cells and Purkinje cells in the
RT zebrafish cerebellum.";
RL J. Comp. Neurol. 525:1558-1585(2017).
RN [15] {ECO:0000313|Ensembl:ENSDARP00000147967}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000147967};
RG Ensembl;
RL Submitted (APR-2018) to UniProtKB.
RN [16] {ECO:0000313|RefSeq:NP_997730.1}
RP IDENTIFICATION.
RC STRAIN=Wild-type {ECO:0000313|RefSeq:NP_997730.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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|PIRNR:PIRNR000939};
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|PIRNR:PIRNR000939};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily.
CC {ECO:0000256|ARBA:ARBA00008601, ECO:0000256|PIRNR:PIRNR000939}.
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DR EMBL; BX649360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059592; AAH59592.1; -; mRNA.
DR EMBL; BX908764; CAK10873.1; -; Genomic_DNA.
DR EMBL; BX649552; CAK10873.1; JOINED; Genomic_DNA.
DR RefSeq; NP_997730.1; NM_212565.1.
DR STRING; 7955.ENSDARP00000005408; -.
DR ChEMBL; CHEMBL4523347; -.
DR PaxDb; 7955-ENSDARP00000005408; -.
DR Ensembl; ENSDART00000020249.8; ENSDARP00000005408.7; ENSDARG00000019307.9.
DR Ensembl; ENSDART00000193588.1; ENSDARP00000147967.1; ENSDARG00000110831.1.
DR GeneID; 114436; -.
DR KEGG; dre:114436; -.
DR AGR; ZFIN:ZDB-GENE-010625-1; -.
DR CTD; 1847; -.
DR ZFIN; ZDB-GENE-010625-1; dusp5.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_027074_0_2_1; -.
DR OMA; CRPYLSY; -.
DR OrthoDB; 2901840at2759; -.
DR TreeFam; TF105122; -.
DR Reactome; R-DRE-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-DRE-5675221; Negative regulation of MAPK pathway.
DR Proteomes; UP000000437; Alternate scaffold 22.
DR Proteomes; UP000000437; Chromosome 22.
DR Bgee; ENSDARG00000019307; Expressed in granulocyte and 17 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0033550; F:MAP kinase tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0001706; P:endoderm formation; IBA:GO_Central.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR CDD; cd14639; DSP_DUSP5; 1.
DR CDD; cd01446; DSP_MapKP; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR008343; MKP.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
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; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR10159:SF40; DUAL SPECIFICITY PROTEIN PHOSPHATASE 5; 1.
DR Pfam; PF00782; DSPc; 1.
DR PIRSF; PIRSF000939; MAPK_Ptase; 1.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000939};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|PIRNR:PIRNR000939};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT DOMAIN 18..136
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 171..312
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 233..290
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT ACT_SITE 256
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000939-1"
SQ SEQUENCE 368 AA; 41381 MW; C4FC6E86DF2BE894 CRC64;
MKVSSIDCRR LRKIIRKECG NCLIVDCRPY FSFSNSCIRG SVNVNLNSVV VRRSRGGPVP
LQFVIPDEKA LFRLREGSIS AVVALDDRTP HLQKLKKDSI AQIVINTLSH LTSSASICFL
KGGYENFHAH YPELCTETRS VEVSEDKSER GVSSHCDKLA SHHKPDYDQG RPVEILPFLY
LGSAYHACRQ DYLSDLHITA LLNVSRRDSR PARGQYNYKW IPVEDSHTAD ISSHFQEAID
FIERVKAEGG KVLVHCEAGI SRSPTICMAY IMKTQRLRLE QAFDVIRQRR AIISPNFSFM
GQLLQFESEV VSSTPPLVTP AAQETPTFFS GDFTLETESF ESSVFTFPTS FLTPIQPSFK
LSPITALP
//
