Reviewed, UniProtKB/Swiss-Prot Q21773 (DHP1_CAEEL)

Names and origin

Protein names

Recommended name:
    Dihydropyrimidinase 1
    EC=3.5.2.2
Alternative name(s):
    CeCRMP/DHP-1
    UlipB

Gene names

Name:	dhp-1
ORF Names:	R06C7.3

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	489 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	5,6-dihydrouracil + H2O = 3-ureidopropanoate. Ref.1
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homotetramer By similarity.
Subcellular location	Nucleus. Ref.1
Tissue specificity	In L1-L2 larvae, expressed in body hypodermal cells, hemidesmosomes and in a neuronal cell between the pharynx and ring neuropil. In adults, expression is seen in body hypodermal cells and pharynx. Ref.1
Developmental stage	Expressed in dorsal regions of embryos at late gastrula stage, transiently expressed in the developmental process of 3-fold embryo to L1-L2 larval stage. Ref.1
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.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dihydropyrimidinase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 489	489	Dihydropyrimidinase 1		PRO_0000165929
Sites
	Metal binding	61	1	Zinc 1 By similarity
	Metal binding	63	1	Zinc 1 By similarity
	Metal binding	156	1	Zinc 1; via carbamate group By similarity
	Metal binding	156	1	Zinc 2; via carbamate group By similarity
	Metal binding	189	1	Zinc 2 By similarity
	Metal binding	245	1	Zinc 2 By similarity
	Metal binding	323	1	Zinc 1 By similarity
	Binding site	161	1	Substrate By similarity
	Binding site	295	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	344	1	Substrate; via carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	156	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q21773-1 [UniParc]. Last modified June 6, 2002. Version 2. Checksum: 314590019ACF2975	FASTA	489	53,798
	10 20 30 40 50 60 MSPPLVIKNG TVVNEDGMFK ADVLVRNGII VEVSPNITAL PDTEVIDATD RLVIPGGIDP 70 80 90 100 110 120 HTHMQMPYMG EVTKDDFLKG TEAAVAGGTT MIIDFCCPDH RNGESLIAGY NRWRSWADPK 130 140 150 160 170 180 VCCDYGLSVA ITMWRPETAE QMAIITSPEF GVNSFKFYMA YENTLMVRDD ELFRGMQECA 190 200 210 220 230 240 KLRALARVHC ENGSVIKEKE IDLLAKGVTG PEGHTQSRPE EIEAEATNRA CVLAAQANCP 250 260 270 280 290 300 VYIVHVMTKG AASAISHHRA QGSIVFGEPI AAGLALDGSH YYNEDWLHAA RYVMSPPLSR 310 320 330 340 350 360 DPTTPELLMK LLAAGELHLT GTDNCTYDCR QKSLGKGNFT KIPNGINGVE DRMSVVWEKG 370 380 390 400 410 420 VHSGIIDPMR YVSITSSTAA KIFNIYPRKG RIAVGSDADI VIFNPNATRT ISKDTHHHNL 430 440 450 460 470 480 DFNIFEGINC HGVAEVTISR GRIVWAHGKL QTVPGSGKFI PLLANSPFVF STHEKREQKI QPRIVERLE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of the Caenorhabditis elegans CeCRMP/DHP-1 and -2; common ancestors of CRMP and dihydropyrimidinase?" Takemoto T., Sasaki Y., Hamajima N., Goshima Y., Nonaka M., Kimura H. Gene 261:259-267(2000) [PubMed: 11167013] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"The Ulip family phosphoproteins -- common and specific properties." Byk T., Ozon S., Sobel A. Eur. J. Biochem. 254:14-24(1998) [PubMed: 9652388] [Abstract] Cited for: IDENTIFICATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB040992 mRNA. Translation: BAB21560.1. Z71266 Genomic DNA. Translation: CAD24483.1.
PIR	T23968.
RefSeq	NP_001021583.1.
UniGene	Cel.19394
3D structure databases
HSSP	HSSP built from PDB template 1K1D based on UniProtKB Q45515.
ModBase	Search...
Genome annotation databases
Ensembl	R06C7.3. Caenorhabditis elegans. [Contig view]
GeneID	172464.
KEGG	cel:R06C7.3.
Organism-specific databases
WormBase	WBGene00000963. dhp-1.
WormPep	R06C7.3. CE30293. [WorfDB]
Phylogenomic databases
OMA	Q21773. GINGVED.
Enzyme and pathway databases
BRENDA	3.5.2.2. 672.
Gene expression databases
ArrayExpress	Q21773.
Family and domain databases
InterPro	IPR006680. Amidohydro_1. IPR011778. D-hydantoinase. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
ProDom	PD000518. DHOase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR02033. D-hydantoinase. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	875623.

Entry information

Entry name

DHP1_CAEEL

Accession

Primary (citable) accession number: Q21773
Secondary accession number(s): Q9BPU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project