Uricase - Mus musculus (Mouse)

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P25688 (URIC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 110. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Uricase
EC=1.7.3.3

Alternative name(s):
Urate oxidase

Gene names

Name:

Uox

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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.
Sequence similarities	Belongs to the uricase family.

Ontologies

Keywords
Biological process	Purine metabolism
Cellular component	Peroxisome
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	purine nucleobase metabolic process Traceable author statement PubMed 11461119. Source: MGI urate catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrion Inferred from direct assay PubMed 14651853. Source: MGI peroxisome Traceable author statement PubMed 11461119. Source: MGI
Molecular_function	urate oxidase activity Traceable author statement PubMed 11461119. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 303

302

Uricase

PRO_0000165986

Regions

Region

68 – 69

Substrate binding By similarity

Region

234 – 235

Substrate binding By similarity

Motif

301 – 303

Microbody targeting signal Potential

Sites

Active site

187

Charge relay system By similarity

Active site

235

Charge relay system By similarity

Binding site

187

Substrate By similarity

Amino acid modifications

Modified residue

N-acetylalanine Ref.3

Modified residue

N6-acetyllysine Ref.4

Modified residue

Phosphoserine Ref.5

Modified residue

N6-acetyllysine Ref.4

Modified residue

118

N6-acetyllysine Ref.4

Modified residue

122

N6-acetyllysine Ref.4

Modified residue

164

N6-acetyllysine Ref.4

Modified residue

185

N6-acetyllysine Ref.4

Modified residue

220

N6-acetyllysine Ref.4

Modified residue

227

N6-acetyllysine Ref.4

Modified residue

231

Phosphoserine Ref.5

Modified residue

277

N6-acetyllysine Ref.4

Modified residue

290

N6-acetyllysine Ref.4

Modified residue

301

Phosphoserine Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P25688 [UniParc].

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

303

35,039

        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' referencesShow '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, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Liver.
[4]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36; LYS-55; LYS-118; LYS-122; LYS-164; LYS-185; LYS-220; LYS-227; LYS-277 AND LYS-290, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS." Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y. Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-231 AND SER-301, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M27695 mRNA. Translation: AAA40538.1. BC019771 mRNA. Translation: AAH19771.1.
IPI	IPI00223367.
PIR	B36227.
RefSeq	NP_033500.1. NM_009474.5.
UniGene	Mm.10865.
3D structure databases
ProteinModelPortal	P25688.
SMR	P25688. Positions 21-297.
ModBase	Search...
PTM databases
PhosphoSite	P25688.
2D gel databases
SWISS-2DPAGE	P25688.
Proteomic databases
PaxDb	P25688.
PRIDE	P25688.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000029837; ENSMUSP00000029837; ENSMUSG00000028186.
GeneID	22262.
KEGG	mmu:22262.
Organism-specific databases
CTD	391051.
MGI	MGI:98907. Uox.
Phylogenomic databases
eggNOG	COG3648.
HOGENOM	HOG000250659.
HOVERGEN	HBG018060.
InParanoid	P25688.
KO	K00365.
OMA	HDHSFVR.
OrthoDB	EOG4DNF4Z.
Enzyme and pathway databases
UniPathway	UPA00394; UER00650.
Gene expression databases
ArrayExpress	P25688.
Bgee	P25688.
CleanEx	MM_UOX.
Genevestigator	P25688.
GermOnline	ENSMUSG00000028186. Mus musculus.
Family and domain databases
Gene3D	3.10.270.10. 1 hit.
InterPro	IPR002042. Uricase. IPR019842. Uricase_CS. [Graphical view]
PANTHER	PTHR10395:SF1. PTHR10395:SF1. 1 hit.
Pfam	PF01014. Uricase. 2 hits. [Graphical view]
PIRSF	PIRSF000241. Urate_oxidase. 1 hit.
PRINTS	PR00093. URICASE.
TIGRFAMs	TIGR03383. urate_oxi. 1 hit.
PROSITE	PS00366. URICASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	302359.
SOURCE	Search...

Entry information

Entry name

URIC_MOUSE

Accession

Primary (citable) accession number: P25688

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents