URIC_PIG
ID URIC_PIG Reviewed; 304 AA.
AC P16164;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Uricase;
DE EC=1.7.3.3;
DE AltName: Full=Urate oxidase;
GN Name=UOX;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
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 [MRNA] OF 7-38.
RX PubMed=3344434; DOI=10.1126/science.3344434;
RA Lee C.C., Wu X., Gibbs R.A., Cook R.G., Muzny D.M., Caskey C.T.;
RT "Generation of cDNA probes directed by amino acid sequence: cloning of
RT urate oxidase.";
RL Science 239:1288-1291(1988).
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 -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the uricase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/UP/";
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DR EMBL; M27697; AAA31141.1; -; mRNA.
DR EMBL; M19733; AAA31140.1; -; mRNA.
DR PIR; C36227; C36227.
DR RefSeq; NP_999435.1; NM_214270.1.
DR AlphaFoldDB; P16164; -.
DR SMR; P16164; -.
DR STRING; 9823.ENSSSCP00000024781; -.
DR PaxDb; P16164; -.
DR PeptideAtlas; P16164; -.
DR PRIDE; P16164; -.
DR Ensembl; ENSSSCT00015087661; ENSSSCP00015035726; ENSSSCG00015065247.
DR Ensembl; ENSSSCT00030059752; ENSSSCP00030027373; ENSSSCG00030042839.
DR Ensembl; ENSSSCT00035036996; ENSSSCP00035014752; ENSSSCG00035027951.
DR Ensembl; ENSSSCT00040020425; ENSSSCP00040008566; ENSSSCG00040015135.
DR Ensembl; ENSSSCT00045063004; ENSSSCP00045044403; ENSSSCG00045036383.
DR Ensembl; ENSSSCT00050069554; ENSSSCP00050029895; ENSSSCG00050051079.
DR Ensembl; ENSSSCT00060021426; ENSSSCP00060008810; ENSSSCG00060016087.
DR Ensembl; ENSSSCT00065080836; ENSSSCP00065035195; ENSSSCG00065059057.
DR GeneID; 397510; -.
DR KEGG; ssc:397510; -.
DR CTD; 391051; -.
DR eggNOG; KOG1599; Eukaryota.
DR InParanoid; P16164; -.
DR OrthoDB; 906540at2759; -.
DR BRENDA; 1.7.3.3; 6170.
DR UniPathway; UPA00394; UER00650.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0004846; F:urate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Acetylation; Oxidoreductase; Peroxisome; Phosphoprotein; Purine metabolism;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT CHAIN 2..304
FT /note="Uricase"
FT /id="PRO_0000165988"
FT MOTIF 302..304
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 264
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 235..236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 10
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 23
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 23
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 27
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 36
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 164
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 175
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 185
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 221
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 221
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 228
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 228
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 278
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 289
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
SQ SEQUENCE 304 AA; 35008 MW; 62066026C59F7FA3 CRC64;
MAHYRNDYKK NDEVEFVRTG YGKDMIKVLH IQRDGKYHSI KEVATSVQLT LSSKKDYLHG
DNSDVIPTDT IKNTVNVLAK FKGIKSIETF AVTICEHFLS SFKHVIRAQV YVEEVPWKRF
EKNGVKHVHA FIYTPTGTHF CEVEQIRNGP PVIHSGIKDL KVLKTTQSGF EGFIKDQFTT
LPEVKDRCFA TQVYCKWRYH QGRDVDFEAT WDTVRSIVLQ KFAGPYDKGE YSPSVQKTLY
DIQVLTLGQV PEIEDMEISL PNIHYLNIDM SKMGLINKEE VLLPLDNPYG RITGTVKRKL
TSRL
