DUS8_MOUSE
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 03-AUG-2022, entry version 160.
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; O09112; -.
DR PRIDE; O09112; -.
DR ProteomicsDB; 277615; -.
DR Antibodypedia; 10181; 214 antibodies from 30 providers.
DR DNASU; 18218; -.
DR Ensembl; ENSMUST00000039926; ENSMUSP00000049414; ENSMUSG00000037887.
DR GeneID; 18218; -.
DR KEGG; mmu:18218; -.
DR UCSC; uc009kmo.2; mouse.
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; ICESHFM; -.
DR OrthoDB; 1576308at2759; -.
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 72 CRISPR screens.
DR PRO; PR:O09112; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O09112; protein.
DR Bgee; ENSMUSG00000037887; Expressed in caudate-putamen and 166 other tissues.
DR ExpressionAtlas; O09112; baseline and differential.
DR Genevisible; O09112; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
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 GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.40.250.10; -; 1.
DR Gene3D; 3.90.190.10; -; 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 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; SSF52799; 1.
DR SUPFAM; SSF52821; SSF52821; 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 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
