URIC_DROME
ID URIC_DROME Reviewed; 352 AA.
AC P16163; Q29QG8; Q9VLX4;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Uricase;
DE EC=1.7.3.3;
DE AltName: Full=Urate oxidase;
GN Name=Uro; Synonyms=UO; ORFNames=CG7171;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Salivary gland;
RX PubMed=2118989; DOI=10.1128/mcb.10.10.5114-5127.1990;
RA Wallrath L.L., Burnett J.B., Friedman T.B.;
RT "Molecular characterization of the Drosophila melanogaster urate oxidase
RT gene, an ecdysone-repressible gene expressed only in the Malpighian
RT tubules.";
RL Mol. Cell. Biol. 10:5114-5127(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2006) 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.
CC {ECO:0000269|PubMed:2118989}.
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 -!- ACTIVITY REGULATION: Repressed by 20-hydroxyecdysone.
CC {ECO:0000269|PubMed:2118989}.
CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC urate: step 1/3.
CC -!- INTERACTION:
CC P16163; Q9VW53: Mtr3; NbExp=4; IntAct=EBI-173238, EBI-92844;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:2118989}.
CC -!- TISSUE SPECIFICITY: Malpighian tubules. {ECO:0000269|PubMed:2118989}.
CC -!- DEVELOPMENTAL STAGE: Third instar larvae and adult.
CC {ECO:0000269|PubMed:2118989}.
CC -!- SIMILARITY: Belongs to the uricase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABC86484.1; Type=Frameshift; Evidence={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; X51940; CAA36203.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52555.1; -; Genomic_DNA.
DR EMBL; BT024422; ABC86484.1; ALT_SEQ; mRNA.
DR PIR; A35920; A35920.
DR RefSeq; NP_476779.1; NM_057431.3.
DR AlphaFoldDB; P16163; -.
DR SMR; P16163; -.
DR BioGRID; 60199; 13.
DR DIP; DIP-20028N; -.
DR IntAct; P16163; 15.
DR STRING; 7227.FBpp0079109; -.
DR PaxDb; P16163; -.
DR DNASU; 34060; -.
DR EnsemblMetazoa; FBtr0079486; FBpp0079109; FBgn0003961.
DR GeneID; 34060; -.
DR KEGG; dme:Dmel_CG7171; -.
DR CTD; 34060; -.
DR FlyBase; FBgn0003961; Uro.
DR VEuPathDB; VectorBase:FBgn0003961; -.
DR eggNOG; KOG1599; Eukaryota.
DR GeneTree; ENSGT00940000153229; -.
DR HOGENOM; CLU_048151_1_0_1; -.
DR InParanoid; P16163; -.
DR OMA; THRWTRM; -.
DR OrthoDB; 906540at2759; -.
DR PhylomeDB; P16163; -.
DR UniPathway; UPA00394; UER00650.
DR BioGRID-ORCS; 34060; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34060; -.
DR PRO; PR:P16163; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0003961; Expressed in adult Malpighian tubule (Drosophila) and 13 other tissues.
DR ExpressionAtlas; P16163; baseline and differential.
DR Genevisible; P16163; DM.
DR GO; GO:0005777; C:peroxisome; ISS:FlyBase.
DR GO; GO:0004846; F:urate oxidase activity; ISS:FlyBase.
DR GO; GO:0019428; P:allantoin biosynthetic process; TAS:FlyBase.
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 Oxidoreductase; Peroxisome; Purine metabolism; Reference proteome.
FT CHAIN 1..352
FT /note="Uricase"
FT /id="PRO_0000165991"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 350..352
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 41
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT ACT_SITE 86
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT ACT_SITE 308
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 86..87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT BINDING 279..280
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D0VWQ1"
FT CONFLICT 114
FT /note="R -> K (in Ref. 1; CAA36203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 40062 MW; 1D0E00F8AD0FC96F CRC64;
MFATPLRQPA AANHQTPKNS AGMDEHGKPY QYEITDHGYG KDAVKVLHVS RNGPVHAIQE
FEVGTHLKLY SKKDYYQGNN SDIVATDSQK NTVYLLAKKH GIESPEKFAL LLARHFINKY
SHVEEAHVHV EAYPWQRVCQ EETRTNVNGK CENGVQGNCD FSSIDNRSLH NHAFIFTPTA
LHYCDVVIRR TDPKQTVITG IKGLRVLKTT QSSFVNFVND EFRSLPDQYD RIFSTVVDCS
WEYSDTENLD FLRAWQTVKN IIIRNFAGDP QVGVSSPSVQ HTLYLSERQV LDVLPQVSVI
SMTMPNKHYF NFDTKPFQKI APGDNNEVFI PVDKPHGTIY AQLARKNINS HL
