P32320 (CDD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	146 AA.
Sequence status	Complete.
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. Contains 1 CMP/dCMP deaminase zinc-binding domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell surface receptor signaling pathway Non-traceable author statement Ref.3. Source: UniProtKB cytosine metabolic process Traceable author statement Ref.1. Source: UniProtKB negative regulation of cell growth Inferred from direct assay Ref.3. Source: UniProtKB negative regulation of nucleotide metabolic process Inferred from direct assay Ref.3. Source: UniProtKB protein homotetramerization Inferred from direct assay Ref.7Ref.3. Source: UniProtKB pyrimidine nucleoside salvage Traceable author statement. Source: Reactome
Cellular_component	cytosol Non-traceable author statement PubMed 16303324. Source: UniProtKB extracellular region Traceable author statement Ref.3. Source: UniProtKB
Molecular_function	cytidine deaminase activity Inferred from direct assay Ref.1Ref.3. Source: UniProtKB nucleoside binding Inferred from direct assay Ref.7. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.7. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.7. 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

Domain

16 – 116

101

CMP/dCMP deaminase zinc-binding

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. Ref.5 Ref.6
Corresponds to variant rs2072671 [ dbSNP | Ensembl ].

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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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

EMBL
GenBank
DDBJ

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. NM_001785.2.

UniGene

Hs.466910.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P32320.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000364212.

PTM databases

PhosphoSite

P32320.

Polymorphism databases

DMDM

1705718.

Proteomic databases

PaxDb

P32320.

PeptideAtlas

P32320.

PRIDE

P32320.

Protocols and materials databases

DNASU

978.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375071; ENSP00000364212; ENSG00000158825.

GeneID

978.

KEGG

hsa:978.

UCSC

uc001bdk.3. human.

Organism-specific databases

CTD

978.

GeneCards

GC01P020915.

HGNC

HGNC:1712. CDA.

MIM

123920. gene.

neXtProt

NX_P32320.

PharmGKB

PA98.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0295.

HOGENOM

HOG000014707.

HOVERGEN

HBG005294.

InParanoid

P32320.

KO

K01489.

OMA

KLVKMAL.

OrthoDB

EOG4WSWBW.

PhylomeDB

P32320.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P32320.

Gene expression databases

ArrayExpress

P32320.

Bgee

P32320.

CleanEx

HS_CDA.

Genevestigator

P32320.

GermOnline

ENSG00000158825. Homo sapiens.

Family and domain databases

InterPro

IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR006262. Cyt_deam_tetra.
IPR016193. Cytidine_deaminase-like.
[Graphical view]

Pfam

PF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]

SUPFAM

SSF53927. Cytidine_deaminase-like. 1 hit.

TIGRFAMs

TIGR01354. cyt_deam_tetra. 1 hit.

PROSITE

PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P32320.

ChEMBL

CHEMBL4502.

ChiTaRS

CDA. human.

DrugBank

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

EvolutionaryTrace

P32320.

GenomeRNAi

978.

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:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.