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Reviewed, UniProtKB/Swiss-Prot Q9EQF5 (DPYS_MOUSE)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Dihydropyrimidinase
      Short name=DHPase
      Short name=DHP
    EC=3.5.2.2
Alternative name(s):
    Dihydropyrimidine amidohydrolase
    Hydantoinase
Gene names
Name: Dpys
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homotetramer By similarity.

Post-translational modification

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

Sequence similarities

Belongs to the DHOase family. Hydantoinase/dihydropyrimidinase subfamily.

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Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Gene Ontology (GO)
   Molecular functiondihydropyrimidinase activity Ref.1

Traceable author statement. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 519519Dihydropyrimidinase
PRO_0000165907

Sites

Metal binding671Zinc 1 By similarity
Metal binding691Zinc 1 By similarity
Metal binding1591Zinc 1; via carbamate group By similarity
Metal binding1591Zinc 2; via carbamate group By similarity
Metal binding1921Zinc 2 By similarity
Metal binding2481Zinc 2 By similarity
Metal binding3261Zinc 1 By similarity
Binding site1641Substrate By similarity
Binding site3471Substrate; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue1591N6-carboxylysine By similarity

Experimental info

Sequence conflict131R → L Ref.1
Sequence conflict131R → L Ref.4
Sequence conflict371R → P in AAK00644. Ref.2
Sequence conflict431E → G in AAK00644. Ref.2
Sequence conflict2061M → T in BAB23654. Ref.3
Sequence conflict2991P → L in AAK00644. Ref.2
Sequence conflict3661S → N in AAK00644. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q9EQF5-1 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: F2C53D40EC120ABD

FASTA51956,725
        10         20         30         40         50         60 
MAPQGRLLIR GGRIVNDDFS QVADVLVEDG VVRALGRDLL PPEDASRGLR ILDAAGKLVL 

        70         80         90        100        110        120 
PGGIDTHTHM QFPFMGSQSV DDFYQGTKAA LAGGTTMIID FAIPQKGSSL IEAFETWRNW 

       130        140        150        160        170        180 
ADPKVCCDYS LHVAVTWWSD KVKEEMKTLA RDKGVNSFKM FMAYKGLYMV QDEQLYAAFS 

       190        200        210        220        230        240 
QCKEIGAIAQ VHAENGDLIA EGAKKMLALG ITGPEGHELC RPEAVEAEAT LRAITIASAV 

       250        260        270        280        290        300 
NCPLYVVHVM SKSAAKVVAD ARRAGNVVYG EPIAAGLGTD GRQYWSEEWS HAAHHVMGPP 

       310        320        330        340        350        360 
LRPDPLTPGF LMDLLANGDL TTTGSDNCTF NTCQKALGKD DFTKIPNGVN GVEDRMSVIW 

       370        380        390        400        410        420 
EKGVHSGKMD ENRFVAVTST NAAKIFNLYP KKGRIAVGSD ADIVIWDPEA TRRISAKTHH 

       430        440        450        460        470        480 
QAVNFNIFEG MVCHGVPLVT ISRGRVVYEA GVFNVTAGHG KFIPRQPFAE YIYKRIKQRD 

       490        500        510 
QTCTPVPVKR APYKGEVTTL KARETKEDDT AGTRMQGHS

« Hide

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References

« Hide 'large scale' references
[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: 10956643] [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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
+Additional computationally mapped references.

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Cross-references

Sequence databases

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.
IPIIPI00318577.
RefSeqNP_073559.2.
UniGeneMm.275974

3D structure databases

HSSPHSSP built from PDB template 1K1D based on UniProtKB Q45515.
ModBaseSearch...

Protein family/group databases

MEROPSM38.973.

Proteomic databases

PRIDEQ9EQF5.

Genome annotation databases

EnsemblENSMUSG00000022304. Mus musculus. [Contig view]
GeneID64705.
KEGGmmu:64705.
NMPDRfig|10090.3.peg.29846.

Organism-specific databases

MGIMGI:1928679. Dpys.

Phylogenomic databases

HOGENOMQ9EQF5.
HOVERGENQ9EQF5.
OMAQ9EQF5. YEAGVFS.

Enzyme and pathway databases

BRENDA3.5.2.2. 244.

Gene expression databases

ArrayExpressQ9EQF5.
BgeeQ9EQF5.
CleanExMM_DPYS.
GermOnlineENSMUSG00000022304. Mus musculus.

Family and domain databases

InterProIPR006680. Amidohydro_1.
IPR011778. D-hydantoinase.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
ProDomPD000518. DHOase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR02033. D-hydantoinase. 1 hit.
ProtoNetSearch...

Other Resources

NextBio320175.
SOURCESearch...

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Entry information

Entry nameDPYS_MOUSE
AccessionPrimary (citable) accession number: Q9EQF5
Secondary accession number(s): Q99PP1, Q9DBK3, Q9DBP7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: June 6, 2002
Last modified: June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents