ID URAD_HUMAN Reviewed; 173 AA. AC A6NGE7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 2. DT 24-JAN-2024, entry version 107. DE RecName: Full=Putative 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase; DE Short=OHCU decarboxylase; DE EC=4.1.1.97; DE AltName: Full=Parahox neighbor; DE AltName: Full=Ureidoimidazoline (2-oxo-4-hydroxy-4-carboxy-5-) decarboxylase; GN Name=URAD; Synonyms=PRHOXNB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [2] RP LACK OF TISSUE SPECIFICITY. RX PubMed=16462750; DOI=10.1038/nchembio768; RA Ramazzina I., Folli C., Secchi A., Berni R., Percudani R.; RT "Completing the uric acid degradation pathway through phylogenetic RT comparison of whole genomes."; RL Nat. Chem. Biol. 2:144-148(2006). CC -!- FUNCTION: Catalyzes the stereoselective decarboxylation of 2-oxo-4- CC hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin. CC {ECO:0000305}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5- CC carboxylate + H(+) = (S)-allantoin + CO2; Xref=Rhea:RHEA:26301, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15678, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:58639; EC=4.1.1.97; CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from CC urate: step 3/3. CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Apparently not expressed. CC -!- SIMILARITY: Belongs to the OHCU decarboxylase family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. In primates the genes CC coding for the enzymes for the degradation of uric acid were CC inactivated and converted to pseudogenes (PubMed:16462750). CC {ECO:0000305|PubMed:16462750}. 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; AL591024; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS45020.1; -. DR RefSeq; NP_001099047.1; NM_001105577.1. DR AlphaFoldDB; A6NGE7; -. DR SMR; A6NGE7; -. DR BioGRID; 571472; 1. DR IntAct; A6NGE7; 1. DR STRING; 9606.ENSP00000333490; -. DR iPTMnet; A6NGE7; -. DR PhosphoSitePlus; A6NGE7; -. DR BioMuta; URAD; -. DR MassIVE; A6NGE7; -. DR PaxDb; 9606-ENSP00000333490; -. DR Antibodypedia; 48958; 9 antibodies from 7 providers. DR DNASU; 646625; -. DR Ensembl; ENST00000332715.6; ENSP00000333490.4; ENSG00000183463.6. DR GeneID; 646625; -. DR KEGG; hsa:646625; -. DR MANE-Select; ENST00000332715.6; ENSP00000333490.4; NM_001105577.2; NP_001099047.1. DR UCSC; uc010aan.2; human. DR AGR; HGNC:17785; -. DR CTD; 646625; -. DR GeneCards; URAD; -. DR HGNC; HGNC:17785; URAD. DR HPA; ENSG00000183463; Tissue enriched (intestine). DR MIM; 615804; gene. DR neXtProt; NX_A6NGE7; -. DR PharmGKB; PA142671135; -. DR VEuPathDB; HostDB:ENSG00000183463; -. DR eggNOG; KOG0848; Eukaryota. DR GeneTree; ENSGT00940000153229; -. DR HOGENOM; CLU_092522_1_1_1; -. DR InParanoid; A6NGE7; -. DR OMA; RCQNERA; -. DR OrthoDB; 2903165at2759; -. DR PhylomeDB; A6NGE7; -. DR TreeFam; TF323276; -. DR PathwayCommons; A6NGE7; -. DR SignaLink; A6NGE7; -. DR UniPathway; UPA00394; UER00652. DR BioGRID-ORCS; 646625; 12 hits in 1087 CRISPR screens. DR GenomeRNAi; 646625; -. DR Pharos; A6NGE7; Tdark. DR PRO; PR:A6NGE7; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; A6NGE7; Protein. DR Bgee; ENSG00000183463; Expressed in mucosa of transverse colon and 28 other cell types or tissues. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0016831; F:carboxy-lyase activity; ISS:UniProtKB. DR GO; GO:0000255; P:allantoin metabolic process; IEA:InterPro. DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.3330.10; Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase; 1. DR InterPro; IPR018020; OHCU_decarboxylase. DR InterPro; IPR017580; OHCU_decarboxylase-1. DR InterPro; IPR036778; OHCU_decarboxylase_sf. DR NCBIfam; TIGR03164; UHCUDC; 1. DR PANTHER; PTHR43466; 2-OXO-4-HYDROXY-4-CARBOXY-5-UREIDOIMIDAZOLINE DECARBOXYLASE-RELATED; 1. DR PANTHER; PTHR43466:SF1; 2-OXO-4-HYDROXY-4-CARBOXY-5-UREIDOIMIDAZOLINE DECARBOXYLASE-RELATED; 1. DR Pfam; PF09349; OHCU_decarbox; 1. DR SUPFAM; SSF158694; UraD-Like; 1. PE 5: Uncertain; KW Decarboxylase; Lyase; Peroxisome; Purine metabolism; Reference proteome. FT CHAIN 1..173 FT /note="Putative 2-oxo-4-hydroxy-4-carboxy-5- FT ureidoimidazoline decarboxylase" FT /id="PRO_0000315240" FT MOTIF 171..173 FT /note="Microbody targeting signal" FT /evidence="ECO:0000255" FT ACT_SITE 67 FT /note="Proton donor" FT /evidence="ECO:0000255" FT BINDING 68 FT /ligand="substrate" FT /evidence="ECO:0000255" FT BINDING 84..88 FT /ligand="substrate" FT /evidence="ECO:0000255" FT BINDING 119..123 FT /ligand="substrate" FT /evidence="ECO:0000255" FT VARIANT 57 FT /note="Q -> P (in dbSNP:rs3897926)" FT /id="VAR_053987" SQ SEQUENCE 173 AA; 19130 MW; 521C44BEF163077C CRC64; MDIEKVNSMD LGEFVDVFGN ATERCPLIAA AVWSQRPFSD LEDLEKHFFA FIDALAQSGQ EGILRCHPDL AGSELQRGTL TAESQREQSG AGLRSLGADE RLRLAELNAQ YRARFGFPFV LAARFSDRTA VPRELARRLL CPSAQELRTA LGEVKKIGSL RLADLLRADP AKL //