Reviewed, UniProtKB/Swiss-Prot P32320 (CDD_HUMAN)

Names and origin

Protein names

Recommended name:
    Cytidine deaminase
    EC=3.5.4.5
Alternative name(s):
    Cytidine aminohydrolase

Gene names

Name:	CDA
Synonyms:	CDD

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	146 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This enzyme scavenge exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Catalytic activity	Cytidine + H2O = uridine + NH3.
Cofactor	Zinc.
Subunit structure	Homotetramer. Ref.7
Tissue specificity	Highly expressed in granulocytes while expression is very low in fibroblasts, chondrocytes, monocytes, and T- as well as B-cell lines.
Sequence similarities	Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell surface receptor linked signal transduction Ref.3 Non-traceable author statement. Source: UniProtKB cytidine deamination Ref.3 Inferred from direct assay. Source: UniProtKB cytosine metabolic process Ref.1 Traceable author statement. Source: UniProtKB negative regulation of cell growth Ref.3 Inferred from direct assay. Source: UniProtKB negative regulation of nucleotide metabolic process Ref.3 Inferred from direct assay. Source: UniProtKB protein homotetramerization Ref.3 Ref.7 Inferred from direct assay. Source: UniProtKB pyrimidine salvage Ref.3 Non-traceable author statement. Source: UniProtKB
Cellular component	cytosol Ref.1 Ref.3 Traceable author statement. Source: UniProtKB extracellular region Ref.3 Traceable author statement. Source: UniProtKB
Molecular function	cytidine deaminase activity Ref.1 Ref.3 Inferred from direct assay. Source: UniProtKB nucleoside binding Ref.7 Inferred from direct assay. Source: UniProtKB protein homodimerization activity Ref.7 Inferred from direct assay. Source: UniProtKB zinc ion binding Ref.3 Ref.7 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 146

146

Cytidine deaminase

PRO_0000171682

Regions

Region

54 – 60

7

Substrate binding

Sites

Active site

67

1

Proton donor

Metal binding

65

1

Zinc; catalytic

Metal binding

99

1

Zinc; catalytic

Metal binding

102

1

Zinc; catalytic

Natural variations

Natural variant

27

1

K → Q: dbSNP rs2072671. Ref.5 Ref.6

VAR_021559

Secondary structure

1

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146

Helix Strand Turn

Details...

Helix

15 – 25

11

Helix

26 – 28

3

Turn

32 – 34

3

Beta strand

38 – 43

6

Beta strand

49 – 53

5

Helix

60 – 62

3

Helix

66 – 76

11

Beta strand

83 – 90

8

Helix

100 – 107

8

Beta strand

111 – 118

8

Beta strand

124 – 128

5

Helix

129 – 132

4

Helix

139 – 141

3

Sequences

	Sequence		Length	Mass (Da)
	P32320-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: AF33D09EE4E176B3	FASTA	146	16,185
	10 20 30 40 50 60 MAQKRPACTL KPECVQQLLV CSQEAKKSAY CPYSHFPVGA ALLTQEGRIF KGCNIENACY 70 80 90 100 110 120 PLGICAERTA IQKAVSEGYK DFRAIAIASD MQDDFISPCG ACRQVMREFG TNWPVYMTKP 130 140 DGTYIVMTVQ ELLPSSFGPE DLQKTQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human cytidine deaminase: purification of enzyme, cloning, and expression of its complementary DNA." Laliberte J., Momparler R.L. Cancer Res. 54:5401-5407(1994) [PubMed: 7923172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Isolation and characterization of the gene coding for human cytidine deaminase." Demontis S., Terao M., Brivio M., Zanotta S., Bruschi M., Garattini E. Biochim. Biophys. Acta 1443:323-333(1998) [PubMed: 9878810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Growth inhibition of granulocyte-macrophage colony forming cells by human cytidine deaminase requires the catalytic function of the protein." Gran C., Boyum A., Johansen R.F., Lovhaug D., Seeberg E.C. Blood 91:4127-4135(1998) [PubMed: 9596658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Blood.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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], VARIANT GLN-27. Tissue: Liver.
[6]	"Cloning of a functional cDNA for human cytidine deaminase (CDD) and its use as a marker of monocyte/macrophage differentiation." Kuhn K., Bertling W.M., Emmrich F. Biochem. Biophys. Res. Commun. 190:1-7(1993) [PubMed: 8422236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-146, VARIANT GLN-27.
[7]	"Structure of human cytidine deaminase bound to a potent inhibitor." Chung S.J., Fromme J.C., Verdine G.L. J. Med. Chem. 48:658-660(2005) [PubMed: 15689149] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 7-146 IN COMPLEX WITH SUBSTRATE ANALOG AND ZINC IONS, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L27943 mRNA. Translation: AAA57254.1.
AF061658 , AF061655, AF061656, AF061657 Genomic DNA. Translation: AAD15828.1.
AJ000474 mRNA. Translation: CAA04113.1.
AL391357 Genomic DNA. Translation: CAH73474.1.
BC054036 mRNA. Translation: AAH54036.1.
S52873 mRNA. Translation: AAB24946.1.

IPI

IPI00027983.

PIR

I52710.

RefSeq

NP_001776.1.

UniGene

Hs.466910

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MQ0	X-ray	2.40	A/B	11-146	[»]

ModBase

Search...

Proteomic databases

PeptideAtlas

P32320.

PRIDE

P32320.

Genome annotation databases

Ensembl

ENSG00000158825. Homo sapiens. [Contig view]

GeneID

978.

KEGG

hsa:978.

UCSC

uc001bdk.1. human.

Organism-specific databases

GeneCards

GC01P020788.

H-InvDB

HIX0023648.

HGNC

HGNC:1712. CDA.

MIM

123920. gene.

PharmGKB

PA24644.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P32320.

HOVERGEN

P32320.

OMA

P32320. YMTKLDG.

Enzyme and pathway databases

BRENDA

3.5.4.5. 247.

Reactome

REACT_1698. Metablism of nucleotides.

Gene expression databases

ArrayExpress

P32320.

Bgee

P32320.

CleanEx

HS_CDA.

GermOnline

ENSG00000158825. Homo sapiens.

Family and domain databases

InterPro

IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn_bd.
IPR006262. Cyt_deam_tetra.
[Graphical view]

PANTHER

PTHR11644:SF2. Cyt_deam_tetra. 1 hit.

Pfam

PF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01354. cyt_deam_tetra. 1 hit.

PROSITE

PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00928. Azacitidine.
DB01101. Capecitabine.
DB00987. Cytarabine.
DB00441. Gemcitabine.

NextBio

4112.

SOURCE

Search...

Entry information

Entry name

CDD_HUMAN

Accession

Primary (citable) accession number: P32320

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1996
Last modified:	July 7, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)