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   16-JUN-2009, entry version 30.
DE   RecName: Full=Dual specificity protein phosphatase 10;
DE            EC=3.1.3.48;
DE            EC=3.1.3.16;
GN   Name=DUSP10;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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: Involved in the inactivation of MAP kinases. Has a
CC       specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class dual specificity subfamily.
CC   -!- SIMILARITY: Contains 1 rhodanese domain.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
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DR   EMBL; BC122694; AAI22695.1; -; mRNA.
DR   IPI; IPI00696253; -.
DR   RefSeq; NP_001029897.2; -.
DR   UniGene; Bt.2070; -.
DR   SMR; Q0IID7; 321-467.
DR   Ensembl; ENSBTAG00000001729; Bos taurus.
DR   GeneID; 541175; -.
DR   KEGG; bta:541175; -.
DR   HOVERGEN; Q0IID7; -.
DR   OMA; Q0IID7; NEHDAQD.
DR   BRENDA; 3.1.3.16; 251.
DR   BRENDA; 3.1.3.48; 251.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosph...; IEA:InterPro.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0006470; P:protein amino acid dephosphorylation; IEA:InterPro.
DR   InterPro; IPR008343; MAPK_phosph.
DR   InterPro; IPR001763; Rhodanese-like.
DR   InterPro; IPR000387; Tyr_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000340; Tyr_Pase_dual_specific.
DR   Gene3D; G3DSA:3.40.250.10; Rhodanese-like; 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   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; Phosphoprotein; Protein phosphatase.
FT   CHAIN         1    482       Dual specificity protein phosphatase 10.
FT                                /FTId=PRO_0000283703.
FT   DOMAIN      168    285       Rhodanese.
FT   DOMAIN      384    453       Tyrosine-protein phosphatase.
FT   ACT_SITE    408    408       Phosphocysteine intermediate (By
FT                                similarity).
FT   MOD_RES       4      4       Phosphoserine (By similarity).
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
//