URIC_MOUSE
ID URIC_MOUSE Reviewed; 303 AA.
AC P25688;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Uricase;
DE EC=1.7.3.3;
DE AltName: Full=Urate oxidase;
GN Name=Uox;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2594778; DOI=10.1073/pnas.86.23.9412;
RA Wu X., Lee C.C., Muzny D.M., Caskey C.T.;
RT "Urate oxidase: primary structure and evolutionary implications.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9412-9416(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-18; 42-52; 56-80; 86-107; 148-158; 165-185; 188-196;
RP 203-214 AND 221-236, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Kanor S., Bienvenut W.V.;
RL Submitted (OCT-2005) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-231, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-288, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=23085393; DOI=10.1016/j.febslet.2012.10.009;
RA Nakamura Y., Ogura M., Ogura K., Tanaka D., Inagaki N.;
RT "SIRT5 deacetylates and activates urate oxidase in liver mitochondria of
RT mice.";
RL FEBS Lett. 586:4076-4081(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-10; LYS-23; LYS-220 AND LYS-227, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-23; LYS-27; LYS-36;
RP LYS-118; LYS-122; LYS-164; LYS-175; LYS-185; LYS-220; LYS-227 AND LYS-277,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate,
CC which is further processed to form (S)-allantoin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + urate = 5-hydroxyisourate + H2O2;
CC Xref=Rhea:RHEA:21368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072; EC=1.7.3.3;
CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC urate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:23085393}.
CC Mitochondrion {ECO:0000269|PubMed:23085393}.
CC -!- PTM: Acetylation of Lys-118, Lys-164 and Lys-290 is observed in liver
CC mitochondria from fasted mice but not from fed mice. May be
CC deacetylated by Sirt5; however it is unclear whether Sirt5 mediates
CC deacetylation or desuccinylation of Uox; additional evidence is
CC required to validate these results (PubMed:23085393).
CC {ECO:0000269|PubMed:23085393, ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the uricase family. {ECO:0000305}.
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DR EMBL; M27695; AAA40538.1; -; mRNA.
DR EMBL; BC019771; AAH19771.1; -; mRNA.
DR CCDS; CCDS17905.1; -.
DR PIR; B36227; B36227.
DR RefSeq; NP_033500.1; NM_009474.5.
DR AlphaFoldDB; P25688; -.
DR SMR; P25688; -.
DR IntAct; P25688; 3.
DR MINT; P25688; -.
DR STRING; 10090.ENSMUSP00000029837; -.
DR iPTMnet; P25688; -.
DR PhosphoSitePlus; P25688; -.
DR SwissPalm; P25688; -.
DR SWISS-2DPAGE; P25688; -.
DR jPOST; P25688; -.
DR PaxDb; P25688; -.
DR PeptideAtlas; P25688; -.
DR PRIDE; P25688; -.
DR ProteomicsDB; 300192; -.
DR DNASU; 22262; -.
DR Ensembl; ENSMUST00000029837; ENSMUSP00000029837; ENSMUSG00000028186.
DR GeneID; 22262; -.
DR KEGG; mmu:22262; -.
DR UCSC; uc008rrp.1; mouse.
DR CTD; 391051; -.
DR MGI; MGI:98907; Uox.
DR VEuPathDB; HostDB:ENSMUSG00000028186; -.
DR eggNOG; KOG1599; Eukaryota.
DR GeneTree; ENSGT00940000153229; -.
DR InParanoid; P25688; -.
DR OMA; THRWTRM; -.
DR OrthoDB; 906540at2759; -.
DR PhylomeDB; P25688; -.
DR TreeFam; TF323438; -.
DR UniPathway; UPA00394; UER00650.
DR BioGRID-ORCS; 22262; 0 hits in 70 CRISPR screens.
DR ChiTaRS; Uox; mouse.
DR PRO; PR:P25688; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P25688; protein.
DR Bgee; ENSMUSG00000028186; Expressed in gall bladder and 74 other tissues.
DR ExpressionAtlas; P25688; baseline and differential.
DR Genevisible; P25688; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005777; C:peroxisome; IDA:MGI.
DR GO; GO:0004846; F:urate oxidase activity; IDA:MGI.
DR GO; GO:0006154; P:adenosine catabolic process; IDA:MGI.
DR GO; GO:0000255; P:allantoin metabolic process; IDA:MGI.
DR GO; GO:0006196; P:AMP catabolic process; IDA:MGI.
DR GO; GO:0046059; P:dAMP catabolic process; IDA:MGI.
DR GO; GO:0006157; P:deoxyadenosine catabolic process; IDA:MGI.
DR GO; GO:0006161; P:deoxyguanosine catabolic process; IDA:MGI.
DR GO; GO:0006149; P:deoxyinosine catabolic process; IDA:MGI.
DR GO; GO:0046055; P:dGMP catabolic process; IDA:MGI.
DR GO; GO:0046038; P:GMP catabolic process; IDA:MGI.
DR GO; GO:0006147; P:guanine catabolic process; IDA:MGI.
DR GO; GO:0009114; P:hypoxanthine catabolic process; IDA:MGI.
DR GO; GO:0006204; P:IMP catabolic process; IDA:MGI.
DR GO; GO:0006148; P:inosine catabolic process; IDA:MGI.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IBA:GO_Central.
DR GO; GO:0006144; P:purine nucleobase metabolic process; TAS:MGI.
DR GO; GO:0019628; P:urate catabolic process; IDA:MGI.
DR GO; GO:0009115; P:xanthine catabolic process; IDA:MGI.
DR InterPro; IPR002042; Uricase.
DR InterPro; IPR019842; Uricase_CS.
DR PANTHER; PTHR42874; PTHR42874; 1.
DR Pfam; PF01014; Uricase; 2.
DR PIRSF; PIRSF000241; Urate_oxidase; 1.
DR PRINTS; PR00093; URICASE.
DR TIGRFAMs; TIGR03383; urate_oxi; 1.
DR PROSITE; PS00366; URICASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Mitochondrion; Oxidoreductase;
KW Peroxisome; Phosphoprotein; Purine metabolism; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:23806337"
FT CHAIN 2..303
FT /note="Uricase"
FT /id="PRO_0000165986"
FT MOTIF 301..303
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 23
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT ACT_SITE 68
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT ACT_SITE 263
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 68..69
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 234..235
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:23806337"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 10
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 23
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 23
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 27
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 36
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 164
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 175
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 185
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 220
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 220
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 227
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 227
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939"
FT MOD_RES 277
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 288
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 303 AA; 35039 MW; F521383D05370FA2 CRC64;
MAHYHDNYGK NDEVEFVRTG YGKDMVKVLH IQRDGKYHSI KEVATSVQLT LRSKKDYLHG
DNSDIIPTDT IKNTVHVLAK LRGIRNIETF AMNICEHFLS SFNHVTRAHV YVEEVPWKRF
EKNGIKHVHA FIHTPTGTHF CEVEQMRNGP PVIHSGIKDL KVLKTTQSGF EGFLKDQFTT
LPEVKDRCFA TQVYCKWRYQ RRDVDFEAIW GAVRDIVLQK FAGPYDKGEY SPSVQKTLYD
IQVLSLSQLP EIEDMEISLP NIHYFNIDMS KMGLINKEEV LLPLDNPYGK ITGTVKRKLP
SRL
