ID DUS6_RAT Reviewed; 381 AA.
AC Q64346;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-APR-2013, entry version 96.
DE RecName: Full=Dual specificity protein phosphatase 6;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=Mitogen-activated protein kinase phosphatase 3;
DE Short=MAP kinase phosphatase 3;
DE Short=MKP-3;
GN Name=Dusp6; Synonyms=Mkp3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Neuron;
RX PubMed=8626780; DOI=10.1074/jbc.271.8.4319;
RA Muda M., Boschert U., Dickinson R., Martinou J.-C., Martinou I.,
RA Camps M., Schlegel W., Arkinstall S.;
RT "MKP-3, a novel cytosolic protein-tyrosine phosphatase that
RT exemplifies a new class of mitogen-activated protein kinase
RT phosphatase.";
RL J. Biol. Chem. 271:4319-4326(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8631996; DOI=10.1074/jbc.271.7.3795;
RA Mourey R.J., Vega Q.C., Campbell J.S., Wenderoth M.P., Hauschka S.D.,
RA Krebs E.G., Dixon J.E.;
RT "A novel cytoplasmic dual specificity protein tyrosine phosphatase
RT implicated in muscle and neuronal differentiation.";
RL J. Biol. Chem. 271:3795-3802(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Inactivates MAP kinases. Has a specificity for the ERK
CC family. Implicated in muscle and neuronal differentiation.
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.
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; X94185; CAA63895.1; -; mRNA.
DR EMBL; U42627; AAB06202.1; -; mRNA.
DR EMBL; BC087003; AAH87003.1; -; mRNA.
DR IPI; IPI00211712; -.
DR RefSeq; NP_446335.1; NM_053883.2.
DR UniGene; Rn.4313; -.
DR PDB; 2FYS; X-ray; 2.50 A; C/D=60-76.
DR PDBsum; 2FYS; -.
DR ProteinModelPortal; Q64346; -.
DR SMR; Q64346; 1-154, 205-347.
DR STRING; 10116.ENSRNOP00000032969; -.
DR Ensembl; ENSRNOT00000037844; ENSRNOP00000032969; ENSRNOG00000023896.
DR GeneID; 116663; -.
DR KEGG; rno:116663; -.
DR UCSC; RGD:70978; rat.
DR CTD; 1848; -.
DR RGD; 70978; Dusp6.
DR eggNOG; COG2453; -.
DR GeneTree; ENSGT00700000104093; -.
DR HOGENOM; HOG000294079; -.
DR HOVERGEN; HBG007347; -.
DR KO; K04459; -.
DR OrthoDB; EOG4GB76F; -.
DR BindingDB; Q64346; -.
DR ChEMBL; CHEMBL5511; -.
DR EvolutionaryTrace; Q64346; -.
DR NextBio; 619455; -.
DR Genevestigator; Q64346; -.
DR GermOnline; ENSRNOG00000023896; Rattus norvegicus.
DR GO; GO:0005829; C:cytosol; IBA:RefGenome.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:RefGenome.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR GO; GO:0030154; P:cell differentiation; IEP:RGD.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:RefGenome.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:RefGenome.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:RefGenome.
DR GO; GO:0042663; P:regulation of endodermal cell fate specification; IBA:RefGenome.
DR GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IBA:RefGenome.
DR GO; GO:0060420; P:regulation of heart growth; IBA:RefGenome.
DR GO; GO:0042493; P:response to drug; IEP:RGD.
DR GO; GO:0070848; P:response to growth factor stimulus; IEP:RGD.
DR GO; GO:0051409; P:response to nitrosative stress; IEA:Compara.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR020422; Dual-sp_phosphatase_subgr_cat.
DR InterPro; IPR024950; DUSP.
DR InterPro; IPR008343; MKP.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR PANTHER; PTHR10159; PTHR10159; 1.
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; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; Rhodanese-like; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; FALSE_NEG.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Hydrolase; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1 381 Dual specificity protein phosphatase 6.
FT /FTId=PRO_0000094806.
FT DOMAIN 30 148 Rhodanese.
FT DOMAIN 206 381 Tyrosine-protein phosphatase.
FT ACT_SITE 293 293 Phosphocysteine intermediate (By
FT similarity).
FT MOD_RES 331 331 Phosphoserine (By similarity).
SQ SEQUENCE 381 AA; 42319 MW; C511E00CB68F2888 CRC64;
MIDTLRPVPF ASEMAISKTV AWLNEQLELG NEQLLLMDCR PQELYESSHI ESAINVAIPG
IMLRRLQKGN LPVRALFTRC EDRDRFTRRC GTDTVVLYDE NSSDWNENTG GESVLGLLLK
KLKDEGCRAF YLEGGFSKFQ AEFALHCETN LDGSCSSSSP PLPVLGLGGL RISSDSSSDI
ESDLDRDPNS ATDSDGSPLS NSQPSFPVEI LPFLYLGCAK DSTNLDVLEE FGIKYILNVT
PNLPNLFENA GEFKYKQIPI SDHWSQNLSQ FFPEAISFID EARGKNCGVL VHCLAGISRS
VTVTVAYLMQ KLNLSMNDAY DIVKMKKSNI SPNFNFMGQL LDFERTLGLS SPCDNRVPAQ
QLYFTAPSNQ NVYQVDSLQS T
//
