URAD_HUMAN
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 03-AUG-2022, entry version 100.
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}.
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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 PaxDb; A6NGE7; -.
DR PeptideAtlas; A6NGE7; -.
DR PRIDE; A6NGE7; -.
DR Antibodypedia; 48958; 8 antibodies from 6 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 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; KICHLRL; -.
DR OrthoDB; 1547390at2759; -.
DR PhylomeDB; A6NGE7; -.
DR TreeFam; TF323276; -.
DR PathwayCommons; A6NGE7; -.
DR SignaLink; A6NGE7; -.
DR UniPathway; UPA00394; UER00652.
DR BioGRID-ORCS; 646625; 9 hits in 1016 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 27 other tissues.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0051997; F:2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activity; IEA:RHEA.
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 GO; GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.3330.10; -; 1.
DR InterPro; IPR018020; OHCU_decarboxylase.
DR InterPro; IPR017580; OHCU_decarboxylase-1.
DR InterPro; IPR036778; OHCU_decarboxylase_sf.
DR Pfam; PF09349; OHCU_decarbox; 1.
DR SUPFAM; SSF158694; SSF158694; 1.
DR TIGRFAMs; TIGR03164; UHCUDC; 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
