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Reviewed, UniProtKB/Swiss-Prot P32320 (CDD_HUMAN)

Last modified July 7, 2009. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 146146Cytidine deaminase
PRO_0000171682

Regions

Region54 – 607Substrate binding

Sites

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

Natural variations

Natural variant271K → Q: dbSNP rs2072671. Ref.5 Ref.6
VAR_021559

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P32320-1 [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: 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. 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: 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

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.
IPIIPI00027983.
PIRI52710.
RefSeqNP_001776.1.
UniGeneHs.466910

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1MQ0X-ray2.40A/B11-146[»]
ModBaseSearch...

Proteomic databases

PeptideAtlasP32320.
PRIDEP32320.

Genome annotation databases

EnsemblENSG00000158825. Homo sapiens. [Contig view]
GeneID978.
KEGGhsa:978.
UCSCuc001bdk.1. human.

Organism-specific databases

GeneCardsGC01P020788.
H-InvDBHIX0023648.
HGNCHGNC:1712. CDA.
MIM123920. gene.
PharmGKBPA24644.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP32320.
HOVERGENP32320.
OMAP32320. YMTKLDG.

Enzyme and pathway databases

BRENDA3.5.4.5. 247.
ReactomeREACT_1698. Metablism of nucleotides.

Gene expression databases

ArrayExpressP32320.
BgeeP32320.
CleanExHS_CDA.
GermOnlineENSG00000158825. Homo sapiens.

Family and domain databases

InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn_bd.
IPR006262. Cyt_deam_tetra.
[Graphical view]
PANTHERPTHR11644:SF2. Cyt_deam_tetra. 1 hit.
PfamPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01354. cyt_deam_tetra. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00928. Azacitidine.
DB01101. Capecitabine.
DB00987. Cytarabine.
DB00441. Gemcitabine.
NextBio4112.
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 7, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 1

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents