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P25688 (URIC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
Uricase

EC=1.7.3.3
Alternative name(s):
Urate oxidase
Gene names
Name:Uox
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.

Catalytic activity

Urate + O2 + H2O = 5-hydroxyisourate + H2O2.

Pathway

Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.

Subcellular location

Peroxisome. Mitochondrion Ref.5.

Post-translational modification

Acetylation of Lys-118, Lys-164 and Lys-290 is observed in liver mitochondria from fasted mice but not from fed mice. May be deacetylated by Sirt5; however it is unclear whether Sirt5 mediates deacetylation or desuccinylation of Uox; additional evidence is required to validate these results (Ref.5). Ref.3

Sequence similarities

Belongs to the uricase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 303302Uricase
PRO_0000165986

Regions

Region68 – 692Substrate binding By similarity
Region234 – 2352Substrate binding By similarity
Motif301 – 3033Microbody targeting signal Potential

Sites

Active site1871Charge relay system By similarity
Active site2351Charge relay system By similarity
Binding site1871Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.3 Ref.6
Modified residue101N6-acetyllysine; alternate Ref.7
Modified residue101N6-succinyllysine; alternate Ref.6
Modified residue231N6-acetyllysine; alternate Ref.7
Modified residue231N6-succinyllysine; alternate Ref.6
Modified residue271N6-acetyllysine Ref.7
Modified residue361N6-acetyllysine Ref.7
Modified residue631Phosphoserine Ref.4
Modified residue1181N6-acetyllysine Ref.7
Modified residue1221N6-acetyllysine Ref.7
Modified residue1641N6-acetyllysine Ref.7
Modified residue1751N6-acetyllysine Ref.7
Modified residue1851N6-acetyllysine Ref.7
Modified residue2201N6-acetyllysine; alternate Ref.7
Modified residue2201N6-succinyllysine; alternate Ref.6
Modified residue2271N6-acetyllysine; alternate Ref.7
Modified residue2271N6-succinyllysine; alternate Ref.6
Modified residue2771N6-acetyllysine Ref.7

Sequences

Sequence LengthMass (Da)Tools
P25688 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F521383D05370FA2

FASTA30335,039
        10         20         30         40         50         60 
MAHYHDNYGK NDEVEFVRTG YGKDMVKVLH IQRDGKYHSI KEVATSVQLT LRSKKDYLHG 

        70         80         90        100        110        120 
DNSDIIPTDT IKNTVHVLAK LRGIRNIETF AMNICEHFLS SFNHVTRAHV YVEEVPWKRF 

       130        140        150        160        170        180 
EKNGIKHVHA FIHTPTGTHF CEVEQMRNGP PVIHSGIKDL KVLKTTQSGF EGFLKDQFTT 

       190        200        210        220        230        240 
LPEVKDRCFA TQVYCKWRYQ RRDVDFEAIW GAVRDIVLQK FAGPYDKGEY SPSVQKTLYD 

       250        260        270        280        290        300 
IQVLSLSQLP EIEDMEISLP NIHYFNIDMS KMGLINKEEV LLPLDNPYGK ITGTVKRKLP 


SRL 

« Hide

References

« Hide 'large scale' references
[1]"Urate oxidase: primary structure and evolutionary implications."
Wu X., Lee C.C., Muzny D.M., Caskey C.T.
Proc. Natl. Acad. Sci. U.S.A. 86:9412-9416(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[3]Kanor S., Bienvenut W.V.
Submitted (OCT-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-18; 42-52; 56-80; 86-107; 148-158; 165-185; 188-196; 203-214 AND 221-236, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Liver.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"SIRT5 deacetylates and activates urate oxidase in liver mitochondria of mice."
Nakamura Y., Ogura M., Ogura K., Tanaka D., Inagaki N.
FEBS Lett. 586:4076-4081(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-23; LYS-220 AND LYS-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-23; LYS-27; LYS-36; LYS-118; LYS-122; LYS-164; LYS-175; LYS-185; LYS-220; LYS-227 AND LYS-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27695 mRNA. Translation: AAA40538.1.
BC019771 mRNA. Translation: AAH19771.1.
CCDSCCDS17905.1.
PIRB36227.
RefSeqNP_033500.1. NM_009474.5.
UniGeneMm.10865.

3D structure databases

ProteinModelPortalP25688.
SMRP25688. Positions 14-298.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP25688. 6 interactions.
MINTMINT-4139643.

PTM databases

PhosphoSiteP25688.

2D gel databases

SWISS-2DPAGEP25688.

Proteomic databases

MaxQBP25688.
PaxDbP25688.
PRIDEP25688.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029837; ENSMUSP00000029837; ENSMUSG00000028186.
GeneID22262.
KEGGmmu:22262.
UCSCuc008rrp.1. mouse.

Organism-specific databases

CTD391051.
MGIMGI:98907. Uox.

Phylogenomic databases

eggNOGCOG3648.
HOGENOMHOG000250659.
HOVERGENHBG018060.
InParanoidP25688.
KOK00365.
OMASDIIPTD.
OrthoDBEOG79KPFH.
PhylomeDBP25688.
TreeFamTF323438.

Enzyme and pathway databases

UniPathwayUPA00394; UER00650.

Gene expression databases

BgeeP25688.
CleanExMM_UOX.
GenevestigatorP25688.

Family and domain databases

InterProIPR002042. Uricase.
IPR019842. Uricase_CS.
[Graphical view]
PfamPF01014. Uricase. 2 hits.
[Graphical view]
PIRSFPIRSF000241. Urate_oxidase. 1 hit.
PRINTSPR00093. URICASE.
TIGRFAMsTIGR03383. urate_oxi. 1 hit.
PROSITEPS00366. URICASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio302359.
PROP25688.
SOURCESearch...

Entry information

Entry nameURIC_MOUSE
AccessionPrimary (citable) accession number: P25688
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot