[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. PubMed=7685356 [NCBI, ExPASy, EBI, Israel, Japan] Weiner K.X., Weiner R.S., Maley F., Maley G.F.; "Primary structure of human deoxycytidylate deaminase and overexpression of its functional protein in Escherichia coli."; J. Biol. Chem. 268:12983-12989(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Lung; DOI=10.1074/jbc.270.32.18727; PubMed=7642519 [NCBI, ExPASy, EBI, Israel, Japan] Weiner K.X., Ciesla J., Jaffe A.B., Ketring R., Maley F., Maley G.F.; "Chromosomal location and structural organization of the human deoxycytidylate deaminase gene."; J. Biol. Chem. 270:18727-18729(1995).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Cervix; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-79, AND MASS SPECTROMETRY. DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan] Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.; "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; Nat. Biotechnol. 23:94-101(2005).

Comments

FUNCTION: Supplies the nucleotide substrate for thymidylate synthetase.
CATALYTIC ACTIVITY: dCMP + H₂O = dUMP + NH₃.
COFACTOR: Zinc.
ENZYME REGULATION: Allosteric enzyme whose activity is greatly influenced by the end products of its metabolic pathway, dCTP and dTTP.
SUBUNIT: Homohexamer.
SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L12136; AAA35755.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L39874; AAC37579.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001286; AAH01286.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A47288; A47288.
I55434; I55434.

RefSeq

NP_001912.2; -.

UniGene

Hs.183850

3D structure databases

ModBase

P32321.

Protein-protein interaction databases

IntAct

P32321; -.

PTM databases

PhosphoSite

P32321; -.

Enzyme and pathway databases

Reactome

REACT_1698; Nucleotide metabolism.

Organism-specific databases

HIX0004657; -.

HGNC:2710; DCTD.

607638; gene. [NCBI / EBI]

PharmGKB

PA138; -.

GeneCards

P32321.

Gene expression databases

ArrayExpress

P32321; -.

CleanEx

HS_DCTD; -.

GermOnline

ENSG00000129187; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0004132;	Molecular function: dCMP deaminase activity (traceable author statement from ProtInc).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0009165;	Biological process: nucleotide biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006220;	Biological process: pyrimidine nucleotide metabolic process (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR016192; APOBEC/CMP_deaminase_Zn-bd.
IPR002125; CMP_dCMP_Zn_bd.
IPR015517; Cyt_deaminase.
IPR016473; dCMP_deaminase.
Graphical view of domain structure.

PANTHER

PTHR11086; Cyt_deaminase; 1.

Pfam

PF00383; dCMP_cyt_deam_1; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF006019; dCMP_deaminase; 1.

PROSITE

PS00903; CYT_DCMP_DEAMINASES; 1.

Genome annotation databases

Ensembl

ENSG00000129187; Homo sapiens. [Contig view]

GeneID

1635; -.

Phylogenomic databases

HOVERGEN

P32321; -.

Other

NextBio

6716; -.

SOURCE

DCTD; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Allosteric enzyme; Direct protein sequencing; Hydrolase; Metal-binding; Nucleotide biosynthesis; Phosphoprotein; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 178`	`178`	`Deoxycytidylate deaminase.`	`PRO_0000171691`
`ACT_SITE`	`86 86`		`Proton donor (By similarity).`
`METAL`	`84 84`		`Zinc; catalytic (By similarity).`
`METAL`	`110 110`		`Zinc; catalytic (By similarity).`
`METAL`	`113 113`		`Zinc; catalytic (By similarity).`
`MOD_RES`	`79 79`		`Phosphotyrosine.`
`CONFLICT`	`95 95`		`S -> L (in Ref. 3; AAH01286).`
`CONFLICT`	`128 128`		`M -> T (in Ref. 1; AAA35755).`

Sequence information

Length: 178 AA [This is the length of the unprocessed precursor]

Molecular weight: 20016 Da [This is the MW of the unprocessed precursor]

CRC64: 2B8DA5EAC85F3666 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSEVSCKKRD DYLEWPEYFM AVAFLSAQRS KDPNSQVGAC IVNSENKIVG IGYNGMPNGC 

        70         80         90        100        110        120 
SDDVLPWRRT AENKLDTKYP YVCHAELNAI MNKNSTDVKG CSMYVALFPC NECAKLIIQA 

       130        140        150        160        170 
GIKEVIFMSD KYHDSDEATA ARLLFNMAGV TFRKFIPKCS KIVIDFDSIN SRPSQKLQ

P32321 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools