DUS1_RAT
ID DUS1_RAT Reviewed; 367 AA.
AC Q64623; Q548G6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Dual specificity protein phosphatase 1 {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:P28563};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:P28563};
DE AltName: Full=Mitogen-activated protein kinase phosphatase 1;
DE Short=MAP kinase phosphatase 1;
DE Short=MKP-1;
DE AltName: Full=Protein-tyrosine phosphatase CL100 {ECO:0000312|EMBL:CAA58828.1};
DE AltName: Full=Protein-tyrosine phosphatase non-receptor type 16;
GN Name=Dusp1 {ECO:0000312|RGD:620897};
GN Synonyms=Cl100 {ECO:0000312|EMBL:CAA58828.1}, Mkp1, Ptpn16;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RA Muda M., Schlegel W., Arkinstall S.;
RT "Pathways regulating CL100 gene expression in pituitary cells.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar Furth;
RX PubMed=11423551; DOI=10.1074/jbc.m102326200;
RA Ryser S., Tortola S., van Haasteren G., Muda M., Li S., Schlegel W.;
RT "MAP kinase phosphatase-1 gene transcription in rat neuroendocrine cells is
RT modulated by a calcium-sensitive block to elongation in the first exon.";
RL J. Biol. Chem. 276:33319-33327(2001).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=8106404; DOI=10.1016/s0021-9258(17)41905-3;
RA Kwak S.P., Hakes D.J., Martell K.J., Dixon J.E.;
RT "Isolation and characterization of a human dual specificity protein-
RT tyrosine phosphatase gene.";
RL J. Biol. Chem. 269:3596-3604(1994).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15527789; DOI=10.1016/j.febslet.2004.09.083;
RA Price D.M., Chik C.L., Terriff D., Weller J., Humphries A., Carter D.A.,
RA Klein D.C., Ho A.K.;
RT "Mitogen-activated protein kinase phosphatase-1 (MKP-1): >100-fold
RT nocturnal and norepinephrine-induced changes in the rat pineal gland.";
RL FEBS Lett. 577:220-226(2004).
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19103603; DOI=10.1074/jbc.m808394200;
RA Bailey M.J., Coon S.L., Carter D.A., Humphries A., Kim J.S., Shi Q.,
RA Gaildrat P., Morin F., Ganguly S., Hogenesch J.B., Weller J.L., Rath M.F.,
RA Moller M., Baler R., Sugden D., Rangel Z.G., Munson P.J., Klein D.C.;
RT "Night/day changes in pineal expression of >600 genes: central role of
RT adrenergic/cAMP signaling.";
RL J. Biol. Chem. 284:7606-7622(2009).
CC -!- FUNCTION: Dual specificity phosphatase that dephosphorylates MAP kinase
CC MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity
CC during the meiotic cell cycle. {ECO:0000250|UniProtKB:P28563}.
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:P28563, 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:P28563};
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:P28563};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91790}.
CC -!- TISSUE SPECIFICITY: Brain. High level expression seen in the cingulate
CC gyrus within the retrospinal cortex, ventral and medial divisions of
CC the anterior thalamus and the medial geniculate nucleus. Expressed at
CC moderate levels in the parietal and temporal cortex. Expressed in the
CC cerebellum. {ECO:0000269|PubMed:15527789, ECO:0000269|PubMed:19103603,
CC ECO:0000269|PubMed:8106404}.
CC -!- INDUCTION: Exhibits night/day variations with a 100-fold increased
CC expression at night in the pineal gland (at protein level). Up-
CC regulation is due to a large degree to the release of norepinephrine
CC from nerve terminals in the pineal gland and cAMP signaling pathway.
CC {ECO:0000269|PubMed:15527789, ECO:0000269|PubMed:19103603}.
CC -!- PTM: Phosphorylation at Ser-359 and Ser-364 by MAPK1/ERK2 and
CC MAPK3/ERK1 reduces its rate of degradation.
CC {ECO:0000250|UniProtKB:P28563}.
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; X84004; CAA58828.1; -; mRNA.
DR EMBL; AF357203; AAK55327.1; -; Genomic_DNA.
DR PIR; S52265; S52265.
DR RefSeq; NP_446221.2; NM_053769.3.
DR AlphaFoldDB; Q64623; -.
DR SMR; Q64623; -.
DR BioGRID; 250421; 1.
DR STRING; 10116.ENSRNOP00000005383; -.
DR PaxDb; Q64623; -.
DR GeneID; 114856; -.
DR KEGG; rno:114856; -.
DR UCSC; RGD:620897; rat.
DR CTD; 1843; -.
DR RGD; 620897; Dusp1.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_027074_0_2_1; -.
DR InParanoid; Q64623; -.
DR OMA; PSCSPCN; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q64623; -.
DR TreeFam; TF105122; -.
DR Reactome; R-RNO-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:Q64623; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003977; Expressed in lung and 20 other tissues.
DR Genevisible; Q64623; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0019838; F:growth factor binding; IPI:RGD.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISS:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISO:RGD.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IDA:RGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1990869; P:cellular response to chemokine; ISO:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0001706; P:endoderm formation; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IDA:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:0090027; P:negative regulation of monocyte chemotaxis; ISO:RGD.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; ISO:RGD.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:RGD.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0009416; P:response to light stimulus; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR Gene3D; 3.40.250.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020420; Atypical_DUSP_subfamB.
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; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PIRSF; PIRSF000939; MAPK_Ptase; 1.
DR PRINTS; PR01910; ADSPHPHTASEB.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 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 1: Evidence at protein level;
KW Cell cycle; Hydrolase; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..367
FT /note="Dual specificity protein phosphatase 1"
FT /id="PRO_0000094792"
FT DOMAIN 20..137
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 173..314
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 258
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOD_RES 359
FT /note="Phosphoserine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P28563"
FT MOD_RES 364
FT /note="Phosphoserine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P28563"
SQ SEQUENCE 367 AA; 39541 MW; 5112ADF290499139 CRC64;
MVMEVGILDA GGLRALLRER AAQCLLLDCR SFFAFNAGHI VGSVNVRFST IVRRRAKGAM
GLEHIVPNTE LRGRLLAGAY HAVVLLDERS AALDGAKRDG TLALAAGALC REARSTQVFF
LQGGYEAFSA SCPELCSKQS TPMGLSLPLS TSVPDSAESG CSSCSTPLYD QGGPVEILSF
LYLGSAYHAS RKDMLDALGI TALINVSANC PNHFEGHYQY KSIPVEDNHK ADISSWFNEA
IDFIDSIKDA GGRVFVHCQA GISRSATICL AYLMRTNRVK LDEAFEFVKQ RRSIISPNFS
FMGQLLQFES QVLAPHCSAE AGSPAMAVLD RGTSTTTVFN FPVSIPVHPT NSALNYLQSP
ITTSPSC
