URIC_RABIT
ID URIC_RABIT Reviewed; 300 AA.
AC P11645;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Uricase;
DE EC=1.7.3.3;
DE AltName: Full=Urate oxidase;
GN Name=UOX;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2719958; DOI=10.1016/0167-4781(89)90178-4;
RA Motojima K., Goto S.;
RT "Cloning of rabbit uricase cDNA reveals a conserved carboxy-terminal
RT tripeptide in three species.";
RL Biochim. Biophys. Acta 1008:116-118(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-35.
RX PubMed=2269363; DOI=10.1016/0014-5793(90)80801-o;
RA Motojima K., Goto S.;
RT "Two rabbit uricase mRNAs and their tissue-specific expression.";
RL FEBS Lett. 277:26-28(1990).
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.
CC -!- SIMILARITY: Belongs to the uricase family. {ECO:0000305}.
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DR EMBL; X14522; CAA32664.1; -; mRNA.
DR EMBL; X57776; CAA40922.1; -; mRNA.
DR EMBL; X57777; CAA40923.1; -; mRNA.
DR PIR; S04332; S04332.
DR RefSeq; NP_001121545.1; NM_001128073.1.
DR AlphaFoldDB; P11645; -.
DR SMR; P11645; -.
DR STRING; 9986.ENSOCUP00000019291; -.
DR GeneID; 100009266; -.
DR KEGG; ocu:100009266; -.
DR eggNOG; KOG1599; Eukaryota.
DR InParanoid; P11645; -.
DR OrthoDB; 906540at2759; -.
DR UniPathway; UPA00394; UER00650.
DR Proteomes; UP000001811; 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..300
FT /note="Uricase"
FT /id="PRO_0000165989"
FT MOTIF 298..300
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 19
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT ACT_SITE 64
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 64..65
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 231..232
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 6
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 6
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 19
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 19
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 32
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 160
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 181
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 217
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 217
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 224
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 224
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 274
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
FT MOD_RES 285
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25688"
SQ SEQUENCE 300 AA; 34501 MW; A10019A7CDA6189F CRC64;
MATTKKNEDV EFVRTGYGKD MVKVLHIQRD GKYHSIKEVA TSVQLTLSSK QDYVYGDNSD
IIPTDTIKNT VHVLAKFKGI KSIEVFAMNI CEHFLSSFNH VVRVHVYVEE VPWKRLEKNG
VQHVHAFIHT PTGTHFCEVE QRRSGLPVIH SGIKDLKVLK TTQSGFEGFI KDQFTTLPEV
KDRCFATQVY CKWRYQHSQD VDFEATWDIV RDTVLEKFAG PYDKGEYSPS VQKTLYDIQV
LTLSRVPQIE DMEISLPNIH YFNIDMSKMG LINKEEVLLP LDNPYGKITG TVKRKLSSRL
