HIUH_MOUSE
ID HIUH_MOUSE Reviewed; 118 AA.
AC Q9CRB3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=5-hydroxyisourate hydrolase;
DE Short=HIU hydrolase;
DE Short=HIUHase;
DE EC=3.5.2.17;
DE AltName: Full=Transthyretin-related protein;
GN Name=Urah;
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], 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].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Lung;
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 [4]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-11; ARG-51; HIS-102;
RP 115-TYR--SER-118 AND SER-118.
RX PubMed=17085964;
RA Lee Y., Park B.C., Lee do H., Bae K.-H., Cho S., Lee C.H., Lee J.S.,
RA Myung P.K., Park S.G.;
RT "Mouse transthyretin-related protein is a hydrolase which degrades 5-
RT hydroxyisourate, the end product of the uricase reaction.";
RL Mol. Cells 22:141-145(2006).
RN [5]
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 hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-
CC 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-
CC dihydro-1H-imidazole-5-carboxylate + H(+); Xref=Rhea:RHEA:23736,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18072,
CC ChEBI:CHEBI:58639; EC=3.5.2.17;
CC Evidence={ECO:0000269|PubMed:16462750, ECO:0000269|PubMed:17085964};
CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC urate: step 2/3.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- MISCELLANEOUS: HIU hydrolysis also occurs spontaneously, but more
CC slowly.
CC -!- SIMILARITY: Belongs to the transthyretin family. 5-hydroxyisourate
CC hydrolase subfamily. {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; DQ225768; ABB46375.1; -; mRNA.
DR EMBL; AK004470; BAB23318.1; -; mRNA.
DR EMBL; AK013117; BAB28659.1; -; mRNA.
DR EMBL; BC051545; AAH51545.1; -; mRNA.
DR CCDS; CCDS21986.1; -.
DR RefSeq; NP_084097.1; NM_029821.2.
DR RefSeq; XP_006536336.1; XM_006536273.1.
DR AlphaFoldDB; Q9CRB3; -.
DR SMR; Q9CRB3; -.
DR STRING; 10090.ENSMUSP00000026554; -.
DR iPTMnet; Q9CRB3; -.
DR PhosphoSitePlus; Q9CRB3; -.
DR SwissPalm; Q9CRB3; -.
DR jPOST; Q9CRB3; -.
DR MaxQB; Q9CRB3; -.
DR PaxDb; Q9CRB3; -.
DR PeptideAtlas; Q9CRB3; -.
DR PRIDE; Q9CRB3; -.
DR ProteomicsDB; 273362; -.
DR Ensembl; ENSMUST00000026554; ENSMUSP00000026554; ENSMUSG00000025481.
DR Ensembl; ENSMUST00000185612; ENSMUSP00000140559; ENSMUSG00000025481.
DR Ensembl; ENSMUST00000211372; ENSMUSP00000147522; ENSMUSG00000025481.
DR GeneID; 76974; -.
DR KEGG; mmu:76974; -.
DR UCSC; uc009kif.1; mouse.
DR CTD; 76974; -.
DR MGI; MGI:1916142; Urah.
DR VEuPathDB; HostDB:ENSMUSG00000025481; -.
DR eggNOG; KOG3006; Eukaryota.
DR GeneTree; ENSGT00940000153229; -.
DR HOGENOM; CLU_115536_1_0_1; -.
DR InParanoid; Q9CRB3; -.
DR OMA; ENQNYHI; -.
DR PhylomeDB; Q9CRB3; -.
DR TreeFam; TF300210; -.
DR BRENDA; 3.5.2.17; 3474.
DR UniPathway; UPA00394; UER00651.
DR BioGRID-ORCS; 76974; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Urah; mouse.
DR PRO; PR:Q9CRB3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CRB3; protein.
DR Bgee; ENSMUSG00000025481; Expressed in left lobe of liver and 184 other tissues.
DR ExpressionAtlas; Q9CRB3; baseline and differential.
DR Genevisible; Q9CRB3; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005777; C:peroxisome; IDA:MGI.
DR GO; GO:0016787; F:hydrolase activity; IDA:MGI.
DR GO; GO:0033971; F:hydroxyisourate hydrolase 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:0006144; P:purine nucleobase metabolic process; IBA:GO_Central.
DR GO; GO:0019628; P:urate catabolic process; IDA:MGI.
DR GO; GO:0009115; P:xanthine catabolic process; IDA:MGI.
DR CDD; cd05822; TLP_HIUase; 1.
DR Gene3D; 2.60.40.180; -; 1.
DR InterPro; IPR014306; Hydroxyisourate_hydrolase.
DR InterPro; IPR000895; Transthyretin/HIU_hydrolase.
DR InterPro; IPR023416; Transthyretin/HIU_hydrolase_d.
DR InterPro; IPR036817; Transthyretin/HIU_hydrolase_sf.
DR InterPro; IPR023419; Transthyretin_CS.
DR PANTHER; PTHR10395; PTHR10395; 1.
DR Pfam; PF00576; Transthyretin; 1.
DR PRINTS; PR00189; TRNSTHYRETIN.
DR SMART; SM00095; TR_THY; 1.
DR SUPFAM; SSF49472; SSF49472; 1.
DR TIGRFAMs; TIGR02962; hdxy_isourate; 1.
DR PROSITE; PS00769; TRANSTHYRETIN_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Peroxisome; Purine metabolism; Reference proteome.
FT CHAIN 1..118
FT /note="5-hydroxyisourate hydrolase"
FT /id="PRO_0000315282"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 11
FT /note="H->N: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:17085964"
FT MUTAGEN 51
FT /note="R->E: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:17085964"
FT MUTAGEN 51
FT /note="R->K: No effect."
FT /evidence="ECO:0000269|PubMed:17085964"
FT MUTAGEN 102
FT /note="H->N: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:17085964"
FT MUTAGEN 115..118
FT /note="Missing: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:17085964"
FT MUTAGEN 118
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:17085964"
SQ SEQUENCE 118 AA; 13559 MW; 0679CCC15BD919F7 CRC64;
MATESSPLTT HVLDTASGLP AQGLCLRLSR LEAPCQQWME LRTSYTNLDG RCPGLLTPSQ
IKPGTYKLFF DTERYWKERG QESFYPYVEV VFTITKETQK FHVPLLLSPW SYTTYRGS
