ID   DUS8_MOUSE              Reviewed;         663 AA.
AC   O09112;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   24-JAN-2024, entry version 168.
DE   RecName: Full=Dual specificity protein phosphatase 8;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
DE   AltName: Full=Neuronal tyrosine threonine phosphatase 1;
GN   Name=Dusp8; Synonyms=Nttp1;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=8733137; DOI=10.1093/hmg/5.5.675;
RA   Theodosiou A.M., Rodrigues N.R., Nesbit M.A., Ambrose H.J., Paterson H.,
RA   McLellan-Arnold E., Boyd Y., Leversha M.A., Owen N., Blake D.J.,
RA   Ashworth A., Davies K.E.;
RT   "A member of the MAP kinase phosphatase gene family in mouse containing a
RT   complex trinucleotide repeat in the coding region.";
RL   Hum. Mol. Genet. 5:675-684(1996).
RN   [2]
RP   FUNCTION.
RX   PubMed=7561881; DOI=10.1046/j.1471-4159.1995.65041823.x;
RA   Martell K.J., Seasholtz A.F., Kwak S.P., Clemens K.K., Dixon J.E.;
RT   "hVH-5: a protein tyrosine phosphatase abundant in brain that inactivates
RT   mitogen-activated protein kinase.";
RL   J. Neurochem. 65:1823-1833(1995).
CC   -!- FUNCTION: Has phosphatase activity with synthetic phosphatase
CC       substrates and negatively regulates mitogen-activated protein kinase
CC       activity, presumably by catalysing their dephosphorylation
CC       (PubMed:7561881). Expected to display protein phosphatase activity
CC       toward phosphotyrosine, phosphoserine and phosphothreonine residues
CC       (Probable). {ECO:0000269|PubMed:7561881, ECO:0000305}.
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: Monomer. {ECO:0000250|UniProtKB:Q13202}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8733137}. Nucleus
CC       {ECO:0000269|PubMed:8733137}.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in brain and lung.
CC       {ECO:0000269|PubMed:8733137}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
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DR   EMBL; X95518; CAA64772.1; -; mRNA.
DR   CCDS; CCDS22024.1; -.
DR   RefSeq; NP_032774.1; NM_008748.3.
DR   RefSeq; XP_006508572.1; XM_006508509.3.
DR   RefSeq; XP_011240291.1; XM_011241989.2.
DR   AlphaFoldDB; O09112; -.
DR   SMR; O09112; -.
DR   STRING; 10090.ENSMUSP00000049414; -.
DR   iPTMnet; O09112; -.
DR   PhosphoSitePlus; O09112; -.
DR   MaxQB; O09112; -.
DR   PaxDb; 10090-ENSMUSP00000049414; -.
DR   ProteomicsDB; 277615; -.
DR   Antibodypedia; 10181; 231 antibodies from 31 providers.
DR   DNASU; 18218; -.
DR   Ensembl; ENSMUST00000039926.10; ENSMUSP00000049414.4; ENSMUSG00000037887.12.
DR   GeneID; 18218; -.
DR   KEGG; mmu:18218; -.
DR   UCSC; uc009kmo.2; mouse.
DR   AGR; MGI:106626; -.
DR   CTD; 1850; -.
DR   MGI; MGI:106626; Dusp8.
DR   VEuPathDB; HostDB:ENSMUSG00000037887; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   GeneTree; ENSGT00940000160004; -.
DR   HOGENOM; CLU_027074_16_0_1; -.
DR   InParanoid; O09112; -.
DR   OMA; DSCFHNV; -.
DR   OrthoDB; 2901840at2759; -.
DR   PhylomeDB; O09112; -.
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; 18218; 1 hit in 77 CRISPR screens.
DR   PRO; PR:O09112; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; O09112; Protein.
DR   Bgee; ENSMUSG00000037887; Expressed in caudate-putamen and 168 other cell types or tissues.
DR   ExpressionAtlas; O09112; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0016791; F:phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR   CDD; cd14645; DSP_DUSP8; 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; IPR048035; DUSP8_DSP.
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:SF108; DUAL SPECIFICITY PROTEIN PHOSPHATASE 8; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF00581; Rhodanese; 1.
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; O09112; MM.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT   CHAIN           1..663
FT                   /note="Dual specificity protein phosphatase 8"
FT                   /id="PRO_0000094811"
FT   DOMAIN          23..138
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          160..302
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          313..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..523
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..624
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        246
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   663 AA;  68847 MW;  416F429A12C1FA7C CRC64;
     MAGDRLPRKV MDAKKLASLL RGGPGGPLVI DSRSFVEYNS CHVLSSVNIC CSKLVKRRLQ
     QGKVTIAELI QPATRSQVDA TEPQDVVVYD QSTRDASVLA ADSFLSILLS KLDGCFDSVA
     ILTGGFATFS SCFPGLCEGK PATLPSMSLS QPCLPVPSVG LTRILPHLYL GSQKDVLNKD
     LMTQNGISYV LNASNSCPKP DFICESRFMR IPINDNYCEK LLPWLDKSIE FIDKAKLSSC
     QVIVHCLAGI SRSATIAIAY IMKTMGMSSD DAYRFVKDRR PSISPNFNFL GQLLEYERSL
     KLLAALQTDG PHLGTPEPLM GPAAGIPLPR LPPSTSESAA TGSEAATAAR EGSPSAGGDA
     PIPSTAPATS ALQQGLRGLH LSSDRLQDTN RLKRSFSLDI KSAYAPSRRP DFPGPPDPGE
     APKLCKLDSP SGGTLGLPSP SPDSPDSVPE CRPRPRRRRP PASSPARSPA HGLGLNFGDT
     ARQTPRHGLS ALSAPGLPGP GQPAGPGGWV PPLDSPGTPS PDGPWCFSPE GAQGPGAVFS
     AFGRVSAGAP GPGNSSSSGG GGGGGGGGGG GGGGGGSSSS NSSSSSSSSS SSSSSSSSSS
     DLRRRDVRTG WPEEPAADAQ FKRRSCQMEF EEGMVEGRAR GEELAALGKQ TSFSGSVEVI
     EVS
//