URIC_CANLF
ID URIC_CANLF Reviewed; 304 AA.
AC Q5FZI9;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Uricase;
DE EC=1.7.3.3;
DE AltName: Full=Urate oxidase;
GN Name=UOX;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=15958795; DOI=10.1093/jhered/esi078;
RA Safra N., Ling G.V., Schaible R.H., Bannasch D.L.;
RT "Exclusion of urate oxidase as a candidate gene for hyperuricosuria in the
RT Dalmatian dog using an interbreed backcross.";
RL J. Hered. 96:750-754(2005).
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:0000250}.
CC -!- SIMILARITY: Belongs to the uricase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY871313; AAW65996.1; -; mRNA.
DR RefSeq; NP_001011886.1; NM_001011886.1.
DR PDB; 4MB8; X-ray; 2.40 A; A/B/C/D=1-304.
DR PDBsum; 4MB8; -.
DR AlphaFoldDB; Q5FZI9; -.
DR SMR; Q5FZI9; -.
DR STRING; 9615.ENSCAFP00000053318; -.
DR PaxDb; Q5FZI9; -.
DR GeneID; 490189; -.
DR KEGG; cfa:490189; -.
DR CTD; 391051; -.
DR eggNOG; KOG1599; Eukaryota.
DR InParanoid; Q5FZI9; -.
DR OrthoDB; 906540at2759; -.
DR BRENDA; 1.7.3.3; 1153.
DR UniPathway; UPA00394; UER00650.
DR Proteomes; UP000002254; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Oxidoreductase; Peroxisome; Phosphoprotein;
KW Purine metabolism; 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_0000165983"
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"
FT STRAND 16..34
FT /evidence="ECO:0007829|PDB:4MB8"
FT STRAND 37..52
FT /evidence="ECO:0007829|PDB:4MB8"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:4MB8"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:4MB8"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:4MB8"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:4MB8"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:4MB8"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:4MB8"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:4MB8"
FT STRAND 151..168
FT /evidence="ECO:0007829|PDB:4MB8"
FT STRAND 189..199
FT /evidence="ECO:0007829|PDB:4MB8"
FT HELIX 208..223
FT /evidence="ECO:0007829|PDB:4MB8"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:4MB8"
FT HELIX 235..249
FT /evidence="ECO:0007829|PDB:4MB8"
FT STRAND 253..262
FT /evidence="ECO:0007829|PDB:4MB8"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:4MB8"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4MB8"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:4MB8"
FT STRAND 289..297
FT /evidence="ECO:0007829|PDB:4MB8"
SQ SEQUENCE 304 AA; 35096 MW; 7AF8ECF4A2F327F3 CRC64;
MAHYHNDYKK NDEVEFVRTG YGKDMVKVLH IQRDGKYHSI KEVATSVQLT LSSKKDYVYG
DNSDIIPTDT IKNTVHVLAK FKGIKSIETF AMNICEHFLS SFNHVIRAQV YVEEVPWKRF
EKNGVKHVHA FIHNPTGTHF CEVEQMRSGP PVIHSGIKDL KVLKTTQSGF EGFIKDQFTT
LPEVKDRCFA TKVYCKWRYH QGRDVDFEAT WDTVRDIVLE KFAGPYDKGE YSPSVQKTLY
DIQVHSLSRV PEMEDMEISL PNIHYFNIDM SKMGLINKEE VLLPLDNPYG RITGTAKRKL
ASKL
