DUS5_RAT
ID DUS5_RAT Reviewed; 384 AA.
AC O54838;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Dual specificity protein phosphatase 5;
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q16690};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q16690};
DE AltName: Full=MAP-kinase phosphatase CPG21;
GN Name=Dusp5;
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=Wistar;
RX PubMed=9699150; DOI=10.1007/bf02737120;
RA Hevroni D., Rattner A., Bundman M., Lederfein D., Gabarah A., Mangelus M.,
RA Silverman M.A., Kedar H., Naor C., Kornuc M., Hanoch T., Seger R.,
RA Theill L.E., Nedivi E., Richter-Levin G., Citri Y.;
RT "Hippocampal plasticity involves extensive gene induction and multiple
RT cellular mechanisms.";
RL J. Mol. Neurosci. 10:75-98(1998).
CC -!- FUNCTION: Dual specificity protein phosphatase; active with
CC phosphotyrosine, phosphoserine and phosphothreonine residues. The
CC highest relative activity is toward ERK1.
CC {ECO:0000250|UniProtKB:Q16690}.
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:Q16690, 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:Q16690};
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:Q16690};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AF013144; AAB94858.1; -; mRNA.
DR RefSeq; NP_598262.1; NM_133578.1.
DR AlphaFoldDB; O54838; -.
DR SMR; O54838; -.
DR STRING; 10116.ENSRNOP00000018889; -.
DR PhosphoSitePlus; O54838; -.
DR PaxDb; O54838; -.
DR GeneID; 171109; -.
DR KEGG; rno:171109; -.
DR CTD; 1847; -.
DR RGD; 620854; Dusp5.
DR eggNOG; KOG1716; Eukaryota.
DR InParanoid; O54838; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; O54838; -.
DR Reactome; R-RNO-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:O54838; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IDA:RGD.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; ISO:RGD.
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:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISO:RGD.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; ISO:RGD.
DR GO; GO:0001706; P:endoderm formation; IBA:GO_Central.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0045906; P:negative regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0120277; P:positive regulation of cerebral blood circulation; IMP:RGD.
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; 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; 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 2: Evidence at transcript level;
KW Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..384
FT /note="Dual specificity protein phosphatase 5"
FT /id="PRO_0000094803"
FT DOMAIN 19..141
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 178..319
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOTIF 53..74
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 263
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 384 AA; 42094 MW; 5644069B8D348700 CRC64;
MKVTSLDGRR LRKMLRKEAE ARCVVLDCRP YLAFAASSVR GSLNVNLNSV VLRRARGGAV
SARYVLADEA ARARLLQEGG GGVAAVVVLD QGSRHWQKLR EESAARVVLT SLLACLSAGP
RVYFLKGGYE TFYSQYPECC VDAKPISQEK LEGERGLLSQ CGKPILSVAY RPAYDQGGPV
EILPFLYLGS AYHASKCEFL ANLHITALLN VSRRTSEACT THLHYKWIPV EDSHTADISS
HFQEAIDFID CVREEGGKVL VHCEAGVSRS PTICMAYLMK TKQFRLKEAF EYIKQRRSVV
SPNFGFMGQL LQYESEILPS TPTPQPPSCQ GEAASSTFIG HLQTLSPDMQ GAYCTFPTSV
LAPVPTHATV AELHRSPVAT ATSC
