URIC_BOVIN
ID URIC_BOVIN Reviewed; 304 AA.
AC Q3MHG7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Uricase;
DE EC=1.7.3.3;
DE AltName: Full=Urate oxidase;
GN Name=UOX;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Rumen reticulum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate,
CC which is further processed to form (S)-allantoin. {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the uricase family. {ECO:0000305}.
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DR EMBL; BC105244; AAI05245.1; -; mRNA.
DR RefSeq; NP_001069116.1; NM_001075648.2.
DR AlphaFoldDB; Q3MHG7; -.
DR SMR; Q3MHG7; -.
DR STRING; 9913.ENSBTAP00000033405; -.
DR PaxDb; Q3MHG7; -.
DR PeptideAtlas; Q3MHG7; -.
DR PRIDE; Q3MHG7; -.
DR GeneID; 514113; -.
DR KEGG; bta:514113; -.
DR CTD; 391051; -.
DR eggNOG; KOG1599; Eukaryota.
DR HOGENOM; CLU_048151_1_0_1; -.
DR InParanoid; Q3MHG7; -.
DR OrthoDB; 906540at2759; -.
DR TreeFam; TF323438; -.
DR UniPathway; UPA00394; UER00650.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0004846; F:urate oxidase activity; IBA:GO_Central.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IBA:GO_Central.
DR GO; GO:0019628; P:urate catabolic process; IBA:GO_Central.
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_0000165982"
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; 35124 MW; D6D4DBE3892D1ED3 CRC64;
MAHYHNDYQK NDEVEFVRTG YGKDMVKVLH IQRDGKYHSI KEVATSVQLT LNSRREYLHG
DNSDIIPTDT IKNTVQVLAK FKGIKSIETF AMNICEHFLS SFNHVIRVQV YVEEVPWKRF
EKNGVKHVHA FIHTPTGTHF CEVEQLRSGP PVIHSGIKDL KVLKTTQSGF EGFLKDQFTT
LPEVKDRCFA TQVYCKWRYH QGRDVDFEAT WEAVRGIVLK KFAGPYDKGE YSPSVQKTLY
DIQVLSLSQL PEIEDMEISL PNIHYFNIDM SKMGLINKEE VLLPLDNPYG RITGTVKRKL
TSRL
