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P25688

- URIC_MOUSE

UniProt

P25688 - URIC_MOUSE

Protein

Uricase

Gene

Uox

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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.

    Pathwayi

    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

    1. urate oxidase activity Source: MGI

    GO - Biological processi

    1. purine nucleobase metabolic process Source: MGI
    2. urate catabolic process Source: UniProtKB-UniPathway

    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: Chromosome 3

    Organism-specific databases

    MGIiMGI:98907. Uox.

    Subcellular locationi

    Peroxisome 1 Publication. Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: MGI
    2. peroxisome Source: MGI

    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).4 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.
    GenevestigatoriP25688.

    Interactioni

    Protein-protein interaction databases

    IntActiP25688. 6 interactions.
    MINTiMINT-4139643.

    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.
    HOGENOMiHOG000250659.
    HOVERGENiHBG018060.
    InParanoidiP25688.
    KOiK00365.
    OMAiSDIIPTD.
    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

    MAHYHDNYGK NDEVEFVRTG YGKDMVKVLH IQRDGKYHSI KEVATSVQLT    50
    LRSKKDYLHG DNSDIIPTDT IKNTVHVLAK LRGIRNIETF AMNICEHFLS 100
    SFNHVTRAHV YVEEVPWKRF EKNGIKHVHA FIHTPTGTHF CEVEQMRNGP 150
    PVIHSGIKDL KVLKTTQSGF EGFLKDQFTT LPEVKDRCFA TQVYCKWRYQ 200
    RRDVDFEAIW GAVRDIVLQK FAGPYDKGEY SPSVQKTLYD IQVLSLSQLP 250
    EIEDMEISLP NIHYFNIDMS KMGLINKEEV LLPLDNPYGK ITGTVKRKLP 300
    SRL 303
    Length:303
    Mass (Da):35,039
    Last modified:January 23, 2007 - v2
    Checksum:iF521383D05370FA2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27695 mRNA. Translation: AAA40538.1 .
    BC019771 mRNA. Translation: AAH19771.1 .
    CCDSi CCDS17905.1.
    PIRi B36227.
    RefSeqi NP_033500.1. NM_009474.5.
    UniGenei Mm.10865.

    3D structure databases

    ProteinModelPortali P25688.
    SMRi P25688. Positions 14-298.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P25688. 6 interactions.
    MINTi MINT-4139643.

    PTM databases

    PhosphoSitei P25688.

    2D gel databases

    SWISS-2DPAGE P25688.

    Proteomic databases

    MaxQBi P25688.
    PaxDbi P25688.
    PRIDEi P25688.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029837 ; ENSMUSP00000029837 ; ENSMUSG00000028186 .
    GeneIDi 22262.
    KEGGi mmu:22262.
    UCSCi uc008rrp.1. mouse.

    Organism-specific databases

    CTDi 391051.
    MGIi MGI:98907. Uox.

    Phylogenomic databases

    eggNOGi COG3648.
    HOGENOMi HOG000250659.
    HOVERGENi HBG018060.
    InParanoidi P25688.
    KOi K00365.
    OMAi SDIIPTD.
    OrthoDBi EOG79KPFH.
    PhylomeDBi P25688.
    TreeFami TF323438.

    Enzyme and pathway databases

    UniPathwayi UPA00394 ; UER00650 .

    Miscellaneous databases

    NextBioi 302359.
    PROi P25688.
    SOURCEi Search...

    Gene expression databases

    Bgeei P25688.
    CleanExi MM_UOX.
    Genevestigatori P25688.

    Family and domain databases

    InterProi IPR002042. Uricase.
    IPR019842. Uricase_CS.
    [Graphical view ]
    Pfami PF01014. Uricase. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000241. Urate_oxidase. 1 hit.
    PRINTSi PR00093. URICASE.
    TIGRFAMsi TIGR03383. urate_oxi. 1 hit.
    PROSITEi PS00366. URICASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
      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: October 1, 2014
    This is version 122 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