DUS3_MOUSE
ID DUS3_MOUSE Reviewed; 185 AA.
AC Q9D7X3;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Dual specificity protein phosphatase 3;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=T-DSP11;
DE AltName: Full=Vaccinia H1-related phosphatase;
DE Short=VHR;
GN Name=Dusp3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Aoyama K., Matsuda T., Aoki N.;
RT "Molecular cloning and characterization of novel putative dual specificity
RT protein phosphatases T-DSP6 and T-DSP11 with low molecular masses
RT containing a single catalytic domain but not cdc25 homology domain.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 90-104 AND 159-176, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VRK3.
RX PubMed=16845380; DOI=10.1038/ncb1447;
RA Kang T.H., Kim K.T.;
RT "Negative regulation of ERK activity by VRK3-mediated activation of VHR
RT phosphatase.";
RL Nat. Cell Biol. 8:863-869(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Shows activity both for tyrosine-protein phosphate and
CC serine-protein phosphate, but displays a strong preference toward
CC phosphotyrosines. Specifically dephosphorylates and inactivates ERK1
CC and ERK2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:16845380}.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
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 -!- 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 -!- SUBUNIT: Interacts with VRK3, which seems to activate it's phosphatase
CC activity. {ECO:0000269|PubMed:16845380}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16845380}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AF280809; AAK69507.1; -; mRNA.
DR EMBL; AK008734; BAB25864.1; -; mRNA.
DR EMBL; BC016269; AAH16269.1; -; mRNA.
DR CCDS; CCDS25482.1; -.
DR RefSeq; NP_082483.1; NM_028207.3.
DR AlphaFoldDB; Q9D7X3; -.
DR SMR; Q9D7X3; -.
DR BioGRID; 215327; 6.
DR IntAct; Q9D7X3; 4.
DR MINT; Q9D7X3; -.
DR STRING; 10090.ENSMUSP00000003612; -.
DR iPTMnet; Q9D7X3; -.
DR PhosphoSitePlus; Q9D7X3; -.
DR SwissPalm; Q9D7X3; -.
DR EPD; Q9D7X3; -.
DR jPOST; Q9D7X3; -.
DR MaxQB; Q9D7X3; -.
DR PaxDb; Q9D7X3; -.
DR PRIDE; Q9D7X3; -.
DR ProteomicsDB; 277533; -.
DR DNASU; 72349; -.
DR Ensembl; ENSMUST00000003612; ENSMUSP00000003612; ENSMUSG00000003518.
DR Ensembl; ENSMUST00000107172; ENSMUSP00000102790; ENSMUSG00000003518.
DR GeneID; 72349; -.
DR KEGG; mmu:72349; -.
DR UCSC; uc007lqa.2; mouse.
DR CTD; 1845; -.
DR MGI; MGI:1919599; Dusp3.
DR VEuPathDB; HostDB:ENSMUSG00000003518; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000163690; -.
DR InParanoid; Q9D7X3; -.
DR OrthoDB; 1576308at2759; -.
DR TreeFam; TF105128; -.
DR Reactome; R-MMU-202670; ERKs are inactivated.
DR BioGRID-ORCS; 72349; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Dusp3; mouse.
DR PRO; PR:Q9D7X3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D7X3; protein.
DR Bgee; ENSMUSG00000003518; Expressed in ascending aorta and 246 other tissues.
DR ExpressionAtlas; Q9D7X3; baseline and differential.
DR Genevisible; Q9D7X3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001772; C:immunological synapse; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; ISO:MGI.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; ISO:MGI.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:MGI.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0016311; P:dephosphorylation; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0050922; P:negative regulation of chemotaxis; ISO:MGI.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISO:MGI.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0050868; P:negative regulation of T cell activation; ISO:MGI.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:BHF-UCL.
DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; IMP:BHF-UCL.
DR GO; GO:0120183; P:positive regulation of focal adhesion disassembly; ISO:MGI.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IMP:BHF-UCL.
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; PTHR45682; 1.
DR Pfam; PF00782; DSPc; 1.
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 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Nucleus; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..185
FT /note="Dual specificity protein phosphatase 3"
FT /id="PRO_0000094796"
FT DOMAIN 28..179
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 124
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 185 AA; 20472 MW; 62E519E41BE575D5 CRC64;
MSSSFELSVQ DLNDLLSDGS GCYSLPSQPC NEVVPRVYVG NASVAQDITQ LQKLGITHVL
NAAEGRSFMH VNTSASFYED SGITYLGIKA NDTQEFNLSA YFERATDFID QALAHKNGRV
LVHCREGYSR SPTLVIAYLM MRQKMDVKSA LSTVRQNREI GPNDGFLAQL CQLNDRLAKE
GKVKL
