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Protein

Uricase

Gene

Uox

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathway:iurate degradation

This protein is involved in step 1 of the subpathway that synthesizes (S)-allantoin from urate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Uricase (Uox), Uricase (Uox)
  2. 5-hydroxyisourate hydrolase (Urah)
  3. 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (Urad)
This subpathway is part of the pathway urate degradation, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-allantoin from urate, the pathway urate degradation and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei187 – 1871Charge relay systemBy similarity
Binding sitei187 – 1871SubstrateBy similarity
Active sitei235 – 2351Charge relay systemBy similarity

GO - Molecular functioni

  • urate oxidase activity Source: MGI

GO - Biological processi

  • purine nucleobase metabolic process Source: MGI
  • urate catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Purine metabolism

Enzyme and pathway databases

UniPathwayiUPA00394; UER00650.

Names & Taxonomyi

Protein namesi
Recommended name:
Uricase (EC:1.7.3.3)
Alternative name(s):
Urate oxidase
Gene namesi
Name:Uox
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:98907. Uox.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
  • peroxisome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 303302UricasePRO_0000165986Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei10 – 101N6-acetyllysine; alternate1 Publication
Modified residuei10 – 101N6-succinyllysine; alternate1 Publication
Modified residuei23 – 231N6-acetyllysine; alternate1 Publication
Modified residuei23 – 231N6-succinyllysine; alternate1 Publication
Modified residuei27 – 271N6-acetyllysine1 Publication
Modified residuei36 – 361N6-acetyllysine1 Publication
Modified residuei63 – 631Phosphoserine1 Publication
Modified residuei118 – 1181N6-acetyllysine1 Publication
Modified residuei122 – 1221N6-acetyllysine1 Publication
Modified residuei164 – 1641N6-acetyllysine1 Publication
Modified residuei175 – 1751N6-acetyllysine1 Publication
Modified residuei185 – 1851N6-acetyllysine1 Publication
Modified residuei220 – 2201N6-acetyllysine; alternate1 Publication
Modified residuei220 – 2201N6-succinyllysine; alternate1 Publication
Modified residuei227 – 2271N6-acetyllysine; alternate1 Publication
Modified residuei227 – 2271N6-succinyllysine; alternate1 Publication
Modified residuei277 – 2771N6-acetyllysine1 Publication

Post-translational modificationi

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 (PubMed:23085393).2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP25688.
PaxDbiP25688.
PRIDEiP25688.

2D gel databases

SWISS-2DPAGEP25688.

PTM databases

PhosphoSiteiP25688.

Expressioni

Gene expression databases

BgeeiP25688.
CleanExiMM_UOX.
ExpressionAtlasiP25688. baseline and differential.
GenevisibleiP25688. MM.

Interactioni

Protein-protein interaction databases

IntActiP25688. 6 interactions.
MINTiMINT-4139643.
STRINGi10090.ENSMUSP00000029837.

Structurei

3D structure databases

ProteinModelPortaliP25688.
SMRiP25688. Positions 14-298.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 692Substrate bindingBy similarity
Regioni234 – 2352Substrate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi301 – 3033Microbody targeting signalSequence Analysis

Sequence similaritiesi

Belongs to the uricase family.Curated

Phylogenomic databases

eggNOGiCOG3648.
GeneTreeiENSGT00390000010863.
HOGENOMiHOG000250659.
HOVERGENiHBG018060.
InParanoidiP25688.
KOiK00365.
OMAiKDRCFAT.
OrthoDBiEOG79KPFH.
PhylomeDBiP25688.
TreeFamiTF323438.

Family and domain databases

InterProiIPR002042. Uricase.
IPR019842. Uricase_CS.
[Graphical view]
PfamiPF01014. Uricase. 2 hits.
[Graphical view]
PIRSFiPIRSF000241. Urate_oxidase. 1 hit.
PRINTSiPR00093. URICASE.
TIGRFAMsiTIGR03383. urate_oxi. 1 hit.
PROSITEiPS00366. URICASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHYHDNYGK NDEVEFVRTG YGKDMVKVLH IQRDGKYHSI KEVATSVQLT
60 70 80 90 100
LRSKKDYLHG DNSDIIPTDT IKNTVHVLAK LRGIRNIETF AMNICEHFLS
110 120 130 140 150
SFNHVTRAHV YVEEVPWKRF EKNGIKHVHA FIHTPTGTHF CEVEQMRNGP
160 170 180 190 200
PVIHSGIKDL KVLKTTQSGF EGFLKDQFTT LPEVKDRCFA TQVYCKWRYQ
210 220 230 240 250
RRDVDFEAIW GAVRDIVLQK FAGPYDKGEY SPSVQKTLYD IQVLSLSQLP
260 270 280 290 300
EIEDMEISLP NIHYFNIDMS KMGLINKEEV LLPLDNPYGK ITGTVKRKLP

SRL
Length:303
Mass (Da):35,039
Last modified:January 23, 2007 - v2
Checksum:iF521383D05370FA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27695 mRNA. Translation: AAA40538.1.
BC019771 mRNA. Translation: AAH19771.1.
CCDSiCCDS17905.1.
PIRiB36227.
RefSeqiNP_033500.1. NM_009474.5.
UniGeneiMm.10865.

Genome annotation databases

EnsembliENSMUST00000029837; ENSMUSP00000029837; ENSMUSG00000028186.
GeneIDi22262.
KEGGimmu:22262.
UCSCiuc008rrp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27695 mRNA. Translation: AAA40538.1.
BC019771 mRNA. Translation: AAH19771.1.
CCDSiCCDS17905.1.
PIRiB36227.
RefSeqiNP_033500.1. NM_009474.5.
UniGeneiMm.10865.

3D structure databases

ProteinModelPortaliP25688.
SMRiP25688. Positions 14-298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP25688. 6 interactions.
MINTiMINT-4139643.
STRINGi10090.ENSMUSP00000029837.

PTM databases

PhosphoSiteiP25688.

2D gel databases

SWISS-2DPAGEP25688.

Proteomic databases

MaxQBiP25688.
PaxDbiP25688.
PRIDEiP25688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029837; ENSMUSP00000029837; ENSMUSG00000028186.
GeneIDi22262.
KEGGimmu:22262.
UCSCiuc008rrp.1. mouse.

Organism-specific databases

CTDi391051.
MGIiMGI:98907. Uox.

Phylogenomic databases

eggNOGiCOG3648.
GeneTreeiENSGT00390000010863.
HOGENOMiHOG000250659.
HOVERGENiHBG018060.
InParanoidiP25688.
KOiK00365.
OMAiKDRCFAT.
OrthoDBiEOG79KPFH.
PhylomeDBiP25688.
TreeFamiTF323438.

Enzyme and pathway databases

UniPathwayiUPA00394; UER00650.

Miscellaneous databases

NextBioi302359.
PROiP25688.
SOURCEiSearch...

Gene expression databases

BgeeiP25688.
CleanExiMM_UOX.
ExpressionAtlasiP25688. baseline and differential.
GenevisibleiP25688. MM.

Family and domain databases

InterProiIPR002042. Uricase.
IPR019842. Uricase_CS.
[Graphical view]
PfamiPF01014. Uricase. 2 hits.
[Graphical view]
PIRSFiPIRSF000241. Urate_oxidase. 1 hit.
PRINTSiPR00093. URICASE.
TIGRFAMsiTIGR03383. urate_oxi. 1 hit.
PROSITEiPS00366. URICASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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], CLEAVAGE OF INITIATOR METHIONINE [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.

Entry informationi

Entry nameiURIC_MOUSE
AccessioniPrimary (citable) accession number: P25688
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.