DUS10_BOVIN
ID DUS10_BOVIN Reviewed; 482 AA.
AC Q0IID7;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
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};
GN Name=DUSP10;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; BC122694; AAI22695.1; -; mRNA.
DR RefSeq; NP_001029897.2; NM_001034725.2.
DR RefSeq; XP_005216894.1; XM_005216837.3.
DR AlphaFoldDB; Q0IID7; -.
DR SMR; Q0IID7; -.
DR STRING; 9913.ENSBTAP00000002265; -.
DR PaxDb; Q0IID7; -.
DR Ensembl; ENSBTAT00000002265; ENSBTAP00000002265; ENSBTAG00000001729.
DR GeneID; 541175; -.
DR KEGG; bta:541175; -.
DR CTD; 11221; -.
DR VEuPathDB; HostDB:ENSBTAG00000001729; -.
DR VGNC; VGNC:28249; DUSP10.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000157671; -.
DR HOGENOM; CLU_027074_0_1_1; -.
DR InParanoid; Q0IID7; -.
DR OMA; FIYKRLP; -.
DR OrthoDB; 1576308at2759; -.
DR TreeFam; TF105122; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000001729; Expressed in oocyte and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0008432; F:JUN kinase binding; IEA:Ensembl.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; ISS:UniProtKB.
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; IEA:Ensembl.
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: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:0010633; P:negative regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:1905042; P:negative regulation of epithelium regeneration; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; IBA:GO_Central.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; IEA:Ensembl.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IEA:Ensembl.
DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IEA:Ensembl.
DR GO; GO:0002819; P:regulation of adaptive immune response; IEA:Ensembl.
DR GO; GO:0090335; P:regulation of brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IEA:Ensembl.
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..482
FT /note="Dual specificity protein phosphatase 10"
FT /id="PRO_0000283703"
FT DOMAIN 168..285
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 321..464
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 199..215
FT /note="Interaction with MAP kinases"
FT /evidence="ECO:0000250"
FT ACT_SITE 408
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 482 AA; 52389 MW; 11392A5321B94BBF CRC64;
MPPSPLDDRV VVALSRPVRP QDLNLCLDSS YLGSAAPGST SHPPVIATTV VSLKAANLTY
MPSSSGSARS LNCGCSSASC CTVATYDKDN QAPTQAIAAG TATTAIGSST TCPASQMVNN
SENAGSLSPS GGVGSPMAGT PKQLASIKII YPNDLAKKMT KCSKSHLPSQ GPVIIDCRPF
MEYNKSHIQG AVHINCADKI SRRRLQQGKI TVLDLISCRE GKDSFKRIFS KEIIVYDENT
NEPSRVVPSQ PLHIVLESLK REGKEPLVLK GGLSSFKQNH ENLCDNSLQL QECREVGGGA
SAASSMLPQS IPSTPDIENA ELTPILPFLF LGNEQDAQDL ETMQRLNIGY VINVTTHLPL
YHYEKGLFNY KRLPATDSNK QNLRQYFEEA FEFIEEAHQC GKGLLIHCQA GVSRSATIVI
AYLMKHTRMT MTDAYKFVKG KRPIISPNLN FMGQLLEFEE DLNNGVTPRI LTPKLMGVET
VV
