ID   DUS10_MOUSE             Reviewed;         483 AA.
AC   Q9ESS0; Q8R3L3; Q9CZY9;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=Dual specificity protein phosphatase 10;
DE            EC=3.1.3.16 {ECO:0000250|UniProtKB:Q9Y6W6};
DE            EC=3.1.3.48 {ECO:0000250|UniProtKB:Q9Y6W6};
DE   AltName: Full=Mitogen-activated protein kinase phosphatase 5;
DE            Short=MAP kinase phosphatase 5;
DE            Short=MKP-5;
GN   Name=Dusp10; Synonyms=Mkp5;
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].
RC   STRAIN=C57BL/6J;
RX   PubMed=11060451; DOI=10.1159/000015666;
RA   Masuda K., Shima H., Kikuchi K., Watanabe Y., Matsuda Y.;
RT   "Expression and comparative chromosomal mapping of MKP-5 genes
RT   DUSP10/Dusp10.";
RL   Cytogenet. Cell Genet. 90:71-74(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Embryo, Kidney, Pancreas, Thymus, and Urinary bladder;
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].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
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).
CC   -!- FUNCTION: Protein phosphatase involved in the inactivation of MAP
CC       kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14
CC       subfamily. It preferably dephosphorylates p38.
CC       {ECO:0000250|UniProtKB:Q9Y6W6}.
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:0000250|UniProtKB:Q9Y6W6, 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         Evidence={ECO:0000250|UniProtKB:Q9Y6W6};
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:0000250|UniProtKB:Q9Y6W6};
CC   -!- SUBUNIT: Monomer. Interacts with MAPK14.
CC       {ECO:0000250|UniProtKB:Q9Y6W6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6W6}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9Y6W6}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
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; AB037908; BAB17680.1; -; mRNA.
DR   EMBL; AK011995; BAB27966.1; -; mRNA.
DR   EMBL; AK035293; BAC29019.1; -; mRNA.
DR   EMBL; AK050528; BAC34308.1; -; mRNA.
DR   EMBL; AK088024; BAC40102.1; -; mRNA.
DR   EMBL; AK088186; BAC40196.1; -; mRNA.
DR   EMBL; AK088357; BAC40300.1; -; mRNA.
DR   EMBL; AK142568; BAE25109.1; -; mRNA.
DR   EMBL; BC025066; AAH25066.1; -; mRNA.
DR   CCDS; CCDS15591.1; -.
DR   RefSeq; NP_071302.2; NM_022019.5.
DR   RefSeq; XP_006497251.1; XM_006497188.2.
DR   RefSeq; XP_006497252.1; XM_006497189.1.
DR   AlphaFoldDB; Q9ESS0; -.
DR   SMR; Q9ESS0; -.
DR   BioGRID; 211005; 1.
DR   IntAct; Q9ESS0; 1.
DR   STRING; 10090.ENSMUSP00000045838; -.
DR   iPTMnet; Q9ESS0; -.
DR   PhosphoSitePlus; Q9ESS0; -.
DR   SwissPalm; Q9ESS0; -.
DR   MaxQB; Q9ESS0; -.
DR   PaxDb; 10090-ENSMUSP00000045838; -.
DR   PeptideAtlas; Q9ESS0; -.
DR   ProteomicsDB; 279488; -.
DR   Antibodypedia; 20739; 415 antibodies from 36 providers.
DR   DNASU; 63953; -.
DR   Ensembl; ENSMUST00000048655.8; ENSMUSP00000045838.8; ENSMUSG00000039384.9.
DR   GeneID; 63953; -.
DR   KEGG; mmu:63953; -.
DR   UCSC; uc007dym.1; mouse.
DR   AGR; MGI:1927070; -.
DR   CTD; 11221; -.
DR   MGI; MGI:1927070; Dusp10.
DR   VEuPathDB; HostDB:ENSMUSG00000039384; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   GeneTree; ENSGT00940000157671; -.
DR   HOGENOM; CLU_027074_0_1_1; -.
DR   InParanoid; Q9ESS0; -.
DR   OMA; RMTCCPM; -.
DR   OrthoDB; 53899at2759; -.
DR   PhylomeDB; Q9ESS0; -.
DR   TreeFam; TF105122; -.
DR   Reactome; R-MMU-112409; RAF-independent MAPK1/3 activation.
DR   Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR   BioGRID-ORCS; 63953; 3 hits in 77 CRISPR screens.
DR   PRO; PR:Q9ESS0; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q9ESS0; Protein.
DR   Bgee; ENSMUSG00000039384; Expressed in temporalis muscle and 200 other cell types or tissues.
DR   ExpressionAtlas; Q9ESS0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0008432; F:JUN kinase binding; ISO:MGI.
DR   GO; GO:0033549; F:MAP kinase phosphatase activity; IDA:BHF-UCL.
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:0048273; F:mitogen-activated protein kinase p38 binding; 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:0008330; F:protein tyrosine/threonine phosphatase activity; ISO:MGI.
DR   GO; GO:0016311; P:dephosphorylation; ISO:MGI.
DR   GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:BHF-UCL.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:BHF-UCL.
DR   GO; GO:1905042; P:negative regulation of epithelium regeneration; IDA:BHF-UCL.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
DR   GO; GO:0046329; P:negative regulation of JNK cascade; IMP:MGI.
DR   GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISO:MGI.
DR   GO; GO:1903753; P:negative regulation of p38MAPK cascade; ISO:MGI.
DR   GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IMP:MGI.
DR   GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IMP:MGI.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI.
DR   GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; ISO:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:BHF-UCL.
DR   GO; GO:0002819; P:regulation of adaptive immune response; IMP:MGI.
DR   GO; GO:0090335; P:regulation of brown fat cell differentiation; IDA:MGI.
DR   GO; GO:0045088; P:regulation of innate immune response; IMP:MGI.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR   GO; GO:0051403; P:stress-activated MAPK cascade; IMP:MGI.
DR   CDD; cd14567; DSP_DUSP10; 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; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR10159:SF299; DUAL SPECIFICITY PROTEIN PHOSPHATASE 10; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   PRINTS; PR01908; ADSPHPHTASE.
DR   PRINTS; PR01764; MAPKPHPHTASE.
DR   SMART; SM00195; DSPc; 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.
DR   Genevisible; Q9ESS0; MM.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT   CHAIN           1..483
FT                   /note="Dual specificity protein phosphatase 10"
FT                   /id="PRO_0000094814"
FT   DOMAIN          169..286
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          322..465
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          200..216
FT                   /note="Interaction with MAP kinases"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        409
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   CONFLICT        48
FT                   /note="T -> A (in Ref. 1; BAB17680)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="P -> S (in Ref. 2; BAB27966)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        386
FT                   /note="Q -> R (in Ref. 1; BAB17680)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   483 AA;  52532 MW;  7797A1877D986AA8 CRC64;
     MPPSPLDDRV VVALSRPVRP QDLNLCLDSS YLGSASPGSG SHAPVLATAV VTLKAANLTY
     MPSSSGSARS LNCGCSSTSC CTVATYDKDH QAQTQAIAAG TATTAIGTST TCPANQMVNN
     NENTGSVLSP SGGVGSPVSG TPKQLASIKI IYPNDLAKKM TKCSKSHLPS QGPVIIDCRP
     FMEYNKSHIQ GAVHINCADK ISRRRLQQGK ITVLDLISCR EGKDSFKRIF SKEIIVYDEN
     TNEPSRVTPS QPLHIVLESL KREGKEPLVL KGGLSSFKQN HGNLCDNSLQ LQECREVGGG
     ASAASSMLPQ SVPTTPDIEN AELTPILPFL FLGNEQDAQD LDTMQRLNIG YVINVTTHLP
     LYHYEKGLFN YKRLPATDSN KQNLRQYFEE AFEFIEEAHQ CGKGLLIHCQ AGVSRSATIV
     IAYLMKHTRM TMTDAYKFVK GKRPIISPNL NFMGQLLEFE EDLNNGVTPR ILTPKLMGME
     TVV
//