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   27-MAR-2024, entry version 161.
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,
RC   Pancreas, 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; this interaction activates DUSP3
CC       phosphatase 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   PDB; 8TO0; EM; 7.70 A; Fx/Fy/Fz=1-185.
DR   PDBsum; 8TO0; -.
DR   AlphaFoldDB; Q9D7X3; -.
DR   EMDB; EMD-41431; -.
DR   SMR; Q9D7X3; -.
DR   BioGRID; 215327; 7.
DR   IntAct; Q9D7X3; 4.
DR   MINT; Q9D7X3; -.
DR   STRING; 10090.ENSMUSP00000102790; -.
DR   iPTMnet; Q9D7X3; -.
DR   PhosphoSitePlus; Q9D7X3; -.
DR   SwissPalm; Q9D7X3; -.
DR   EPD; Q9D7X3; -.
DR   jPOST; Q9D7X3; -.
DR   MaxQB; Q9D7X3; -.
DR   PaxDb; 10090-ENSMUSP00000003612; -.
DR   ProteomicsDB; 277533; -.
DR   Pumba; Q9D7X3; -.
DR   DNASU; 72349; -.
DR   Ensembl; ENSMUST00000003612.13; ENSMUSP00000003612.7; ENSMUSG00000003518.14.
DR   Ensembl; ENSMUST00000107172.8; ENSMUSP00000102790.2; ENSMUSG00000003518.14.
DR   GeneID; 72349; -.
DR   KEGG; mmu:72349; -.
DR   UCSC; uc007lqa.2; mouse.
DR   AGR; MGI:1919599; -.
DR   CTD; 1845; -.
DR   MGI; MGI:1919599; Dusp3.
DR   VEuPathDB; HostDB:ENSMUSG00000003518; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   GeneTree; ENSGT00940000163690; -.
DR   InParanoid; Q9D7X3; -.
DR   OrthoDB; 1082488at2759; -.
DR   TreeFam; TF105128; -.
DR   Reactome; R-MMU-202670; ERKs are inactivated.
DR   BioGRID-ORCS; 72349; 4 hits in 78 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 249 other cell types or tissues.
DR   ExpressionAtlas; Q9D7X3; baseline and differential.
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:0001701; P:in utero embryonic development; 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:0051893; P:regulation of focal adhesion assembly; IMP:BHF-UCL.
DR   CDD; cd14579; DUSP3; 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:SF1; DUAL SPECIFICITY PROTEIN PHOSPHATASE 3; 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.
DR   Genevisible; Q9D7X3; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase; Nucleus;
KW   Protein phosphatase; 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
//