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Protein

Dihydropyrimidinase

Gene

Dpys

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyze the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate (By similarity).By similarity

Catalytic activityi

5,6-dihydrouracil + H2O = 3-ureidopropanoate.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi67 – 671Zinc 1By similarity
Metal bindingi69 – 691Zinc 1By similarity
Metal bindingi159 – 1591Zinc 1; via carbamate groupBy similarity
Metal bindingi159 – 1591Zinc 2; via carbamate groupBy similarity
Binding sitei164 – 1641SubstrateBy similarity
Metal bindingi192 – 1921Zinc 2By similarity
Metal bindingi248 – 2481Zinc 2By similarity
Metal bindingi326 – 3261Zinc 1By similarity
Binding sitei347 – 3471Substrate; via carbonyl oxygenBy similarity

GO - Molecular functioni

  1. amino acid binding Source: BHF-UCL
  2. dihydropyrimidinase activity Source: BHF-UCL
  3. phosphoprotein binding Source: BHF-UCL
  4. thymine binding Source: BHF-UCL
  5. uracil binding Source: BHF-UCL
  6. zinc ion binding Source: BHF-UCL

GO - Biological processi

  1. beta-alanine metabolic process Source: BHF-UCL
  2. protein homooligomerization Source: BHF-UCL
  3. protein homotetramerization Source: BHF-UCL
  4. pyrimidine nucleobase catabolic process Source: MGI
  5. thymine catabolic process Source: BHF-UCL
  6. uracil catabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.2.2. 3474.
ReactomeiREACT_241108. Pyrimidine catabolism.

Protein family/group databases

MEROPSiM38.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropyrimidinase (EC:3.5.2.2)
Short name:
DHP
Short name:
DHPase
Alternative name(s):
Dihydropyrimidine amidohydrolase
Hydantoinase
Gene namesi
Name:Dpys
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1928679. Dpys.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: BHF-UCL
  2. extracellular vesicular exosome Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 519519DihydropyrimidinasePRO_0000165907Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei159 – 1591N6-carboxylysineBy similarity
Modified residuei256 – 2561N6-succinyllysine1 Publication

Post-translational modificationi

Carbamylation allows a single lysine to coordinate two zinc ions.By similarity

Proteomic databases

MaxQBiQ9EQF5.
PaxDbiQ9EQF5.
PRIDEiQ9EQF5.

PTM databases

PhosphoSiteiQ9EQF5.

Expressioni

Gene expression databases

BgeeiQ9EQF5.
CleanExiMM_DPYS.
ExpressionAtlasiQ9EQF5. baseline and differential.
GenevestigatoriQ9EQF5.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi211101. 1 interaction.
IntActiQ9EQF5. 1 interaction.
MINTiMINT-1869933.

Structurei

3D structure databases

ProteinModelPortaliQ9EQF5.
SMRiQ9EQF5. Positions 6-493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0044.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiQ9EQF5.
KOiK01464.
OMAiFINTPLY.
OrthoDBiEOG7SJD48.
PhylomeDBiQ9EQF5.
TreeFamiTF314706.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro_1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9EQF5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPQGRLLIR GGRIVNDDFS QVADVLVEDG VVRALGRDLL PPEDASRGLR
60 70 80 90 100
ILDAAGKLVL PGGIDTHTHM QFPFMGSQSV DDFYQGTKAA LAGGTTMIID
110 120 130 140 150
FAIPQKGSSL IEAFETWRNW ADPKVCCDYS LHVAVTWWSD KVKEEMKTLA
160 170 180 190 200
RDKGVNSFKM FMAYKGLYMV QDEQLYAAFS QCKEIGAIAQ VHAENGDLIA
210 220 230 240 250
EGAKKMLALG ITGPEGHELC RPEAVEAEAT LRAITIASAV NCPLYVVHVM
260 270 280 290 300
SKSAAKVVAD ARRAGNVVYG EPIAAGLGTD GRQYWSEEWS HAAHHVMGPP
310 320 330 340 350
LRPDPLTPGF LMDLLANGDL TTTGSDNCTF NTCQKALGKD DFTKIPNGVN
360 370 380 390 400
GVEDRMSVIW EKGVHSGKMD ENRFVAVTST NAAKIFNLYP KKGRIAVGSD
410 420 430 440 450
ADIVIWDPEA TRRISAKTHH QAVNFNIFEG MVCHGVPLVT ISRGRVVYEA
460 470 480 490 500
GVFNVTAGHG KFIPRQPFAE YIYKRIKQRD QTCTPVPVKR APYKGEVTTL
510
KARETKEDDT AGTRMQGHS
Length:519
Mass (Da):56,725
Last modified:June 6, 2002 - v2
Checksum:iF2C53D40EC120ABD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131R → L in AAG37999. (PubMed:10956643)Curated
Sequence conflicti13 – 131R → L in AAH37086. (PubMed:15489334)Curated
Sequence conflicti37 – 371R → P in AAK00644. 1 PublicationCurated
Sequence conflicti43 – 431E → G in AAK00644. 1 PublicationCurated
Sequence conflicti206 – 2061M → T in BAB23654. (PubMed:16141072)Curated
Sequence conflicti299 – 2991P → L in AAK00644. 1 PublicationCurated
Sequence conflicti366 – 3661S → N in AAK00644. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF249296 mRNA. Translation: AAG37999.1.
AF227731 mRNA. Translation: AAK00644.1.
AK004822 mRNA. Translation: BAB23593.1.
AK004899 mRNA. Translation: BAB23654.1.
BC037086 mRNA. Translation: AAH37086.1.
CCDSiCCDS27445.1.
RefSeqiNP_001157938.1. NM_001164466.1.
NP_073559.3. NM_022722.3.
UniGeneiMm.275974.

Genome annotation databases

EnsembliENSMUST00000022915; ENSMUSP00000022915; ENSMUSG00000022304.
ENSMUST00000110306; ENSMUSP00000105935; ENSMUSG00000022304.
GeneIDi64705.
KEGGimmu:64705.
UCSCiuc007vok.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF249296 mRNA. Translation: AAG37999.1.
AF227731 mRNA. Translation: AAK00644.1.
AK004822 mRNA. Translation: BAB23593.1.
AK004899 mRNA. Translation: BAB23654.1.
BC037086 mRNA. Translation: AAH37086.1.
CCDSiCCDS27445.1.
RefSeqiNP_001157938.1. NM_001164466.1.
NP_073559.3. NM_022722.3.
UniGeneiMm.275974.

3D structure databases

ProteinModelPortaliQ9EQF5.
SMRiQ9EQF5. Positions 6-493.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211101. 1 interaction.
IntActiQ9EQF5. 1 interaction.
MINTiMINT-1869933.

Protein family/group databases

MEROPSiM38.973.

PTM databases

PhosphoSiteiQ9EQF5.

Proteomic databases

MaxQBiQ9EQF5.
PaxDbiQ9EQF5.
PRIDEiQ9EQF5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022915; ENSMUSP00000022915; ENSMUSG00000022304.
ENSMUST00000110306; ENSMUSP00000105935; ENSMUSG00000022304.
GeneIDi64705.
KEGGimmu:64705.
UCSCiuc007vok.2. mouse.

Organism-specific databases

CTDi1807.
MGIiMGI:1928679. Dpys.

Phylogenomic databases

eggNOGiCOG0044.
GeneTreeiENSGT00760000119241.
HOGENOMiHOG000219145.
HOVERGENiHBG000806.
InParanoidiQ9EQF5.
KOiK01464.
OMAiFINTPLY.
OrthoDBiEOG7SJD48.
PhylomeDBiQ9EQF5.
TreeFamiTF314706.

Enzyme and pathway databases

BRENDAi3.5.2.2. 3474.
ReactomeiREACT_241108. Pyrimidine catabolism.

Miscellaneous databases

NextBioi320175.
PROiQ9EQF5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EQF5.
CleanExiMM_DPYS.
ExpressionAtlasiQ9EQF5. baseline and differential.
GenevestigatoriQ9EQF5.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro_1.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of CRMP5, a novel member of the collapsin response mediator protein family."
    Fukada M., Watakabe I., Yuasa-Kawada J., Kawachi H., Kuroiwa A., Matsuda Y., Noda M.
    J. Biol. Chem. 275:37957-37965(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Swiss Webster / NIH.
    Tissue: Embryo.
  2. "Molecular cloning, nucleotide sequencing, characterization and overexpression of dihydropyrimidinase from mouse liver."
    Chang C.J., Huang C.J., Yang Y.S., Wu T.K.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver and Lung.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDPYS_MOUSE
AccessioniPrimary (citable) accession number: Q9EQF5
Secondary accession number(s): Q99PP1, Q9DBK3, Q9DBP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: June 6, 2002
Last modified: February 4, 2015
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.