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URAD_MOUSE
ID   URAD_MOUSE              Reviewed;         178 AA.
AC   Q283N4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase;
DE            Short=OHCU decarboxylase;
DE            EC=4.1.1.97 {ECO:0000269|PubMed:16462750};
DE   AltName: Full=Parahox neighbor;
DE   AltName: Full=Ureidoimidazoline (2-oxo-4-hydroxy-4-carboxy-5-) decarboxylase;
GN   Name=Urad; Synonyms=Prhoxnb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalyzes the stereoselective decarboxylation of 2-oxo-4-
CC       hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin.
CC       {ECO:0000269|PubMed:16462750}.
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         Evidence={ECO:0000269|PubMed:16462750};
CC   -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC       urate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the OHCU decarboxylase family. {ECO:0000305}.
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DR   EMBL; DQ225767; ABB46374.1; -; mRNA.
DR   EMBL; BC152959; AAI52960.1; -; mRNA.
DR   CCDS; CCDS39399.1; -.
DR   RefSeq; NP_001034767.1; NM_001039678.2.
DR   AlphaFoldDB; Q283N4; -.
DR   SMR; Q283N4; -.
DR   STRING; 10090.ENSMUSP00000098000; -.
DR   iPTMnet; Q283N4; -.
DR   PhosphoSitePlus; Q283N4; -.
DR   SwissPalm; Q283N4; -.
DR   jPOST; Q283N4; -.
DR   MaxQB; Q283N4; -.
DR   PaxDb; Q283N4; -.
DR   PRIDE; Q283N4; -.
DR   ProteomicsDB; 298255; -.
DR   DNASU; 231903; -.
DR   Ensembl; ENSMUST00000100433; ENSMUSP00000098000; ENSMUSG00000075543.
DR   GeneID; 231903; -.
DR   KEGG; mmu:231903; -.
DR   UCSC; uc009aoa.2; mouse.
DR   CTD; 646625; -.
DR   MGI; MGI:3647519; Urad.
DR   VEuPathDB; HostDB:ENSMUSG00000075543; -.
DR   eggNOG; KOG0848; Eukaryota.
DR   GeneTree; ENSGT00390000002395; -.
DR   HOGENOM; CLU_092522_1_0_1; -.
DR   InParanoid; Q283N4; -.
DR   OMA; KICHLRL; -.
DR   OrthoDB; 1547390at2759; -.
DR   PhylomeDB; Q283N4; -.
DR   TreeFam; TF323276; -.
DR   UniPathway; UPA00394; UER00652.
DR   BioGRID-ORCS; 231903; 3 hits in 71 CRISPR screens.
DR   PRO; PR:Q283N4; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q283N4; protein.
DR   Bgee; ENSMUSG00000075543; Expressed in hepatobiliary system and 13 other tissues.
DR   ExpressionAtlas; Q283N4; baseline and differential.
DR   GO; GO:0005777; C:peroxisome; IDA:MGI.
DR   GO; GO:0051997; F:2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activity; IDA:MGI.
DR   GO; GO:0016831; F:carboxy-lyase activity; IDA:MGI.
DR   GO; GO:0006154; P:adenosine catabolic process; IDA:MGI.
DR   GO; GO:0000255; P:allantoin metabolic process; IDA:MGI.
DR   GO; GO:0006196; P:AMP catabolic process; IDA:MGI.
DR   GO; GO:0046059; P:dAMP catabolic process; IDA:MGI.
DR   GO; GO:0006157; P:deoxyadenosine catabolic process; IDA:MGI.
DR   GO; GO:0006161; P:deoxyguanosine catabolic process; IDA:MGI.
DR   GO; GO:0006149; P:deoxyinosine catabolic process; IDA:MGI.
DR   GO; GO:0046055; P:dGMP catabolic process; IDA:MGI.
DR   GO; GO:0046038; P:GMP catabolic process; IDA:MGI.
DR   GO; GO:0006147; P:guanine catabolic process; IDA:MGI.
DR   GO; GO:0009114; P:hypoxanthine catabolic process; IDA:MGI.
DR   GO; GO:0006204; P:IMP catabolic process; IDA:MGI.
DR   GO; GO:0006148; P:inosine catabolic process; IDA:MGI.
DR   GO; GO:0019628; P:urate catabolic process; IDA:MGI.
DR   GO; GO:0009115; P:xanthine catabolic process; IDA:MGI.
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   1: Evidence at protein level;
KW   Decarboxylase; Lyase; Peroxisome; Purine metabolism; Reference proteome.
FT   CHAIN           1..178
FT                   /note="2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline
FT                   decarboxylase"
FT                   /id="PRO_0000315241"
FT   ACT_SITE        67
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         84..88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         119..123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   178 AA;  20017 MW;  FDA1941E8BA89293 CRC64;
     MDMVKVNSMD FGEFVDVFGN IVEKCPLIAA AVWSQRPFSG LEDLENHFFA FIDALPRSGQ
     EGILRCHPDL AGRDLQQGTL TAESQREQSQ AGLTSLDTDD RLRLQQLNAQ YRERFGFPFV
     LAARLSDRAT VPRELARRLQ CQPESELRTA LGEVKKISHL RLTDLLGAHS HSARVELP
 
 
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