DPYS_MOUSE
ID DPYS_MOUSE Reviewed; 519 AA.
AC Q9EQF5; Q99PP1; Q9DBK3; Q9DBP7;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Dihydropyrimidinase;
DE Short=DHP;
DE Short=DHPase;
DE EC=3.5.2.2 {ECO:0000250|UniProtKB:Q55DL0};
DE AltName: Full=Dihydropyrimidine amidohydrolase;
DE AltName: Full=Hydantoinase;
GN Name=Dpys;
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].
RC STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX PubMed=10956643; DOI=10.1074/jbc.m003277200;
RA Fukada M., Watakabe I., Yuasa-Kawada J., Kawachi H., Kuroiwa A.,
RA Matsuda Y., Noda M.;
RT "Molecular characterization of CRMP5, a novel member of the collapsin
RT response mediator protein family.";
RL J. Biol. Chem. 275:37957-37965(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Chang C.J., Huang C.J., Yang Y.S., Wu T.K.;
RT "Molecular cloning, nucleotide sequencing, characterization and
RT overexpression of dihydropyrimidinase from mouse liver.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [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).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-256, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the second step of the reductive pyrimidine
CC degradation, the reversible hydrolytic ring opening of
CC dihydropyrimidines. Can catalyze the ring opening of 5,6-dihydrouracil
CC to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino
CC isobutyrate (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouracil + H2O = 3-(carbamoylamino)propanoate + H(+);
CC Xref=Rhea:RHEA:16121, ChEBI:CHEBI:11892, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15901; EC=3.5.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q55DL0};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q55DL0};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q55DL0};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q55DL0}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family. {ECO:0000305}.
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DR EMBL; AF249296; AAG37999.1; -; mRNA.
DR EMBL; AF227731; AAK00644.1; -; mRNA.
DR EMBL; AK004822; BAB23593.1; -; mRNA.
DR EMBL; AK004899; BAB23654.1; -; mRNA.
DR EMBL; BC037086; AAH37086.1; -; mRNA.
DR CCDS; CCDS27445.1; -.
DR RefSeq; NP_001157938.1; NM_001164466.1.
DR RefSeq; NP_073559.3; NM_022722.3.
DR AlphaFoldDB; Q9EQF5; -.
DR SMR; Q9EQF5; -.
DR BioGRID; 211101; 2.
DR STRING; 10090.ENSMUSP00000022915; -.
DR MEROPS; M38.973; -.
DR iPTMnet; Q9EQF5; -.
DR PhosphoSitePlus; Q9EQF5; -.
DR SwissPalm; Q9EQF5; -.
DR jPOST; Q9EQF5; -.
DR MaxQB; Q9EQF5; -.
DR PaxDb; Q9EQF5; -.
DR PeptideAtlas; Q9EQF5; -.
DR PRIDE; Q9EQF5; -.
DR ProteomicsDB; 277401; -.
DR Antibodypedia; 13364; 314 antibodies from 27 providers.
DR DNASU; 64705; -.
DR Ensembl; ENSMUST00000022915; ENSMUSP00000022915; ENSMUSG00000022304.
DR Ensembl; ENSMUST00000110306; ENSMUSP00000105935; ENSMUSG00000022304.
DR GeneID; 64705; -.
DR KEGG; mmu:64705; -.
DR UCSC; uc007vok.2; mouse.
DR CTD; 1807; -.
DR MGI; MGI:1928679; Dpys.
DR VEuPathDB; HostDB:ENSMUSG00000022304; -.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; Q9EQF5; -.
DR OMA; SAETHHM; -.
DR OrthoDB; 719800at2759; -.
DR PhylomeDB; Q9EQF5; -.
DR TreeFam; TF314706; -.
DR BRENDA; 3.5.2.2; 3474.
DR Reactome; R-MMU-73621; Pyrimidine catabolism.
DR BioGRID-ORCS; 64705; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Dpys; mouse.
DR PRO; PR:Q9EQF5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9EQF5; protein.
DR Bgee; ENSMUSG00000022304; Expressed in left lobe of liver and 40 other tissues.
DR ExpressionAtlas; Q9EQF5; baseline and differential.
DR Genevisible; Q9EQF5; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016597; F:amino acid binding; ISS:BHF-UCL.
DR GO; GO:0004157; F:dihydropyrimidinase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:BHF-UCL.
DR GO; GO:0002059; F:thymine binding; ISS:BHF-UCL.
DR GO; GO:0002058; F:uracil binding; ISS:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; ISS:BHF-UCL.
DR GO; GO:0019482; P:beta-alanine metabolic process; ISS:BHF-UCL.
DR GO; GO:0006248; P:CMP catabolic process; IDA:MGI.
DR GO; GO:0006249; P:dCMP catabolic process; IDA:MGI.
DR GO; GO:0046074; P:dTMP catabolic process; ISO:MGI.
DR GO; GO:0046079; P:dUMP catabolic process; IDA:MGI.
DR GO; GO:0006208; P:pyrimidine nucleobase catabolic process; ISO:MGI.
DR GO; GO:0006210; P:thymine catabolic process; ISS:BHF-UCL.
DR GO; GO:0046050; P:UMP catabolic process; IDA:MGI.
DR GO; GO:0006212; P:uracil catabolic process; ISS:BHF-UCL.
DR GO; GO:0019860; P:uracil metabolic process; ISO:MGI.
DR CDD; cd01314; D-HYD; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..519
FT /note="Dihydropyrimidinase"
FT /id="PRO_0000165907"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14117"
FT MOD_RES 159
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT MOD_RES 256
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 510
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQF6"
FT CONFLICT 13
FT /note="R -> L (in Ref. 1; AAG37999 and 4; AAH37086)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="R -> P (in Ref. 2; AAK00644)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="E -> G (in Ref. 2; AAK00644)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="M -> T (in Ref. 3; BAB23654)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="P -> L (in Ref. 2; AAK00644)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="S -> N (in Ref. 2; AAK00644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 56725 MW; F2C53D40EC120ABD CRC64;
MAPQGRLLIR GGRIVNDDFS QVADVLVEDG VVRALGRDLL PPEDASRGLR ILDAAGKLVL
PGGIDTHTHM QFPFMGSQSV DDFYQGTKAA LAGGTTMIID FAIPQKGSSL IEAFETWRNW
ADPKVCCDYS LHVAVTWWSD KVKEEMKTLA RDKGVNSFKM FMAYKGLYMV QDEQLYAAFS
QCKEIGAIAQ VHAENGDLIA EGAKKMLALG ITGPEGHELC RPEAVEAEAT LRAITIASAV
NCPLYVVHVM SKSAAKVVAD ARRAGNVVYG EPIAAGLGTD GRQYWSEEWS HAAHHVMGPP
LRPDPLTPGF LMDLLANGDL TTTGSDNCTF NTCQKALGKD DFTKIPNGVN GVEDRMSVIW
EKGVHSGKMD ENRFVAVTST NAAKIFNLYP KKGRIAVGSD ADIVIWDPEA TRRISAKTHH
QAVNFNIFEG MVCHGVPLVT ISRGRVVYEA GVFNVTAGHG KFIPRQPFAE YIYKRIKQRD
QTCTPVPVKR APYKGEVTTL KARETKEDDT AGTRMQGHS
