Skip Header

Contribute Send feedback
Read comments (?) or add your own

P70583 (DUT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxyuridine 5'-triphosphate nucleotidohydrolase
Short name=dUTPase
EC=3.6.1.23
Alternative name(s):
PPAR-interacting protein 4
Short name=PIP4
dUTP pyrophosphatase
Gene names
Name:Dut
Synonyms:Dutp
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. Inhibits peroxisome proliferator-activated receptor (PPAR) activity by binding of its N-terminal to PPAR, preventing the latter's dimerization with retinoid X receptor.

Catalytic activity

dUTP + H2O = dUMP + diphosphate.

Cofactor

Magnesium By similarity.

Pathway

Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.

Subcellular location

Cytoplasm. Nucleus. Note: Binding to PPAR induces translocation to the nucleus.

Tissue specificity

Expressed in all tissues examined. Higher levels in heart and kidney.

Miscellaneous

Each trimer binds three substrate molecules. The ligands are bound between subunits, and for each substrate molecule, residues from adjacent subunits contribute to the binding interactions.

Sequence similarities

Belongs to the dUTPase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 205205Deoxyuridine 5'-triphosphate nucleotidohydrolase
PRO_0000182926

Regions

Region126 – 1283Substrate binding By similarity
Region140 – 1434Substrate binding By similarity
Region199 – 2002Substrate binding By similarity

Sites

Binding site1511Substrate; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue1321N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P70583 [UniParc].

Last modified July 11, 2001. Version 3.
Checksum: A9D54EBF5ED015C4

FASTA20522,003
        10         20         30         40         50         60 
MPLLCALLRS RLQPSLLRSL TLTSAQSLSC GGSRGVRTWS ARTGPGACAD PAVSVSKRAR 

        70         80         90        100        110        120 
AEDDASLRFV RLSEHATAPT RGSARAAGYD LYSAYDYTIP SMEKALVKTD IQIAVPSGCY 

       130        140        150        160        170        180 
GRVAPRSGLA VKHFIDVGAG VIDEDYRGNV GVVLFNFGKE KFEVKKGDRI AQLICERILY 

       190        200 
PDLEEVQTLD NTERGSGGFG STGKN

« Hide

References

[1]"Cloning and identification of rat deoxyuridine triphosphatase as an inhibitor of peroxisome proliferator-activated receptor alpha."
Chu R.Y., Lin Y.L., Rao M.S., Reddy J.K.
J. Biol. Chem. 271:27670-27676(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[2]Chu R.Y., Lin Y.L., Rao M.S., Reddy J.K.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U64030 mRNA. Translation: AAC34734.2.
IPIIPI00189772.
PIRT10819.
RefSeqNP_001035361.1. NM_001040271.1.
NP_446044.1. NM_053592.2.
UniGeneRn.6102.

3D structure databases

ProteinModelPortalP70583.
SMRP70583. Positions 67-205.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000009549.

PTM databases

PhosphoSiteP70583.

Proteomic databases

PaxDbP70583.
PRIDEP70583.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000009549; ENSRNOP00000009549; ENSRNOG00000007221.
GeneID497778.
KEGGrno:497778.
UCSCRGD:620849. rat.

Organism-specific databases

CTD1854.
RGD620849. Dut.

Phylogenomic databases

eggNOGCOG0756.
GeneTreeENSGT00390000018390.
HOGENOMHOG000028966.
HOVERGENHBG000175.
InParanoidP70583.
KOK01520.
OMAYGTEFSA.
OrthoDBEOG4R5043.

Enzyme and pathway databases

UniPathwayUPA00610; UER00666.

Gene expression databases

GenevestigatorP70583.
GermOnlineENSRNOG00000007221. Rattus norvegicus.

Family and domain databases

InterProIPR008180. dUTP_pyroPase.
IPR008181. dUTP_pyroPase_sf.
[Graphical view]
PANTHERPTHR11241. PTHR11241. 1 hit.
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00576. dut. 1 hit.
ProtoNetSearch...

Other

NextBio697760.

Entry information

Entry nameDUT_RAT
AccessionPrimary (citable) accession number: P70583
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2001
Last modified: April 3, 2013
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents