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P32320 (CDD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytidine deaminase

EC=3.5.4.5
Alternative name(s):
Cytidine aminohydrolase
Gene names
Name:CDA
Synonyms:CDD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.

Catalytic activity

Cytidine + H2O = uridine + NH3.

2'deoxycytidine + H2O = 2'-deoxyuridine + 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 diversityPolymorphism
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell surface receptor signaling pathway

Non-traceable author statement Ref.3. Source: UniProtKB

cytidine deamination

Inferred from direct assay 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

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

protein homotetramerization

Inferred from direct assay Ref.7Ref.3. Source: UniProtKB

pyrimidine nucleobase metabolic process

Traceable author statement. Source: Reactome

pyrimidine nucleoside salvage

Traceable author statement. Source: Reactome

pyrimidine-containing compound salvage

Non-traceable author statement Ref.3. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Non-traceable author statement PubMed 16303324. Source: UniProtKB

extracellular region

Traceable author statement Ref.3. Source: UniProtKB

   Molecular_functioncytidine 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 146146Cytidine deaminase
PRO_0000171682

Regions

Domain16 – 116101CMP/dCMP deaminase zinc-binding
Region54 – 607Substrate binding

Sites

Active site671Proton donor
Metal binding651Zinc; catalytic
Metal binding991Zinc; catalytic
Metal binding1021Zinc; catalytic

Natural variations

Natural variant271K → Q. Ref.5 Ref.6
Corresponds to variant rs2072671 [ dbSNP | Ensembl ].
VAR_021559

Secondary structure

......................... 146
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32320 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: AF33D09EE4E176B3

FASTA14616,185
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 expand/collapse EMBL AC list , 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.
CCDSCCDS210.1.
PIRI52710.
RefSeqNP_001776.1. NM_001785.2.
UniGeneHs.466910.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MQ0X-ray2.40A/B11-146[»]
ProteinModelPortalP32320.
SMRP32320. Positions 13-142.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107416. 2 interactions.
STRING9606.ENSP00000364212.

Chemistry

BindingDBP32320.
ChEMBLCHEMBL4502.
DrugBankDB00928. Azacitidine.
DB01101. Capecitabine.
DB00987. Cytarabine.
DB00441. Gemcitabine.

PTM databases

PhosphoSiteP32320.

Polymorphism databases

DMDM1705718.

Proteomic databases

MaxQBP32320.
PaxDbP32320.
PeptideAtlasP32320.
PRIDEP32320.

Protocols and materials databases

DNASU978.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375071; ENSP00000364212; ENSG00000158825.
GeneID978.
KEGGhsa:978.
UCSCuc001bdk.3. human.

Organism-specific databases

CTD978.
GeneCardsGC01P020915.
HGNCHGNC:1712. CDA.
MIM123920. gene.
neXtProtNX_P32320.
PharmGKBPA98.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0295.
HOGENOMHOG000014707.
HOVERGENHBG005294.
InParanoidP32320.
KOK01489.
OMATDWAVYM.
OrthoDBEOG75B872.
PhylomeDBP32320.
TreeFamTF314486.

Enzyme and pathway databases

BioCycMetaCyc:HS08334-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP32320.

Gene expression databases

ArrayExpressP32320.
BgeeP32320.
CleanExHS_CDA.
GenevestigatorP32320.

Family and domain databases

InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR006262. Cyt_deam_tetra.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMSSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR01354. cyt_deam_tetra. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDA. human.
EvolutionaryTraceP32320.
GeneWikiCytidine_deaminase.
GenomeRNAi978.
NextBio4112.
PROP32320.
SOURCESearch...

Entry information

Entry nameCDD_HUMAN
AccessionPrimary (citable) accession number: P32320
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM