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Protein

Cytidine deaminase

Gene

CDA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Cytidine + H2O = uridine + NH3.
2'deoxycytidine + H2O = 2'-deoxyuridine + NH3.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi65 – 651Zinc; catalytic
Active sitei67 – 671Proton donor
Metal bindingi99 – 991Zinc; catalytic
Metal bindingi102 – 1021Zinc; catalytic

GO - Molecular functioni

  • cytidine deaminase activity Source: UniProtKB
  • nucleoside binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cell surface receptor signaling pathway Source: UniProtKB
  • cytidine deamination Source: UniProtKB
  • cytosine metabolic process Source: UniProtKB
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of nucleotide metabolic process Source: UniProtKB
  • nucleobase-containing small molecule metabolic process Source: Reactome
  • protein homotetramerization Source: UniProtKB
  • pyrimidine-containing compound salvage Source: UniProtKB
  • pyrimidine nucleobase metabolic process Source: Reactome
  • pyrimidine nucleoside salvage Source: Reactome
  • small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS08334-MONOMER.
BRENDAi3.5.4.5. 2681.
ReactomeiREACT_655. Pyrimidine salvage reactions.
SABIO-RKP32320.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytidine deaminase (EC:3.5.4.5)
Alternative name(s):
Cytidine aminohydrolase
Gene namesi
Name:CDA
Synonyms:CDD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1712. CDA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extracellular region Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA98.

Chemistry

DrugBankiDB00928. Azacitidine.
DB01101. Capecitabine.
DB00987. Cytarabine.
DB00441. Gemcitabine.

Polymorphism and mutation databases

BioMutaiCDA.
DMDMi1705718.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 146146Cytidine deaminasePRO_0000171682Add
BLAST

Proteomic databases

MaxQBiP32320.
PaxDbiP32320.
PeptideAtlasiP32320.
PRIDEiP32320.

PTM databases

PhosphoSiteiP32320.

Expressioni

Tissue specificityi

Highly expressed in granulocytes while expression is very low in fibroblasts, chondrocytes, monocytes, and T- as well as B-cell lines.

Gene expression databases

BgeeiP32320.
CleanExiHS_CDA.
GenevisibleiP32320. HS.

Organism-specific databases

HPAiHPA064202.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
C20orf195Q9BVV23EBI-9250559,EBI-744935
LNX1Q8TBB13EBI-9250559,EBI-739832
PLEKHB2Q96CS73EBI-9250559,EBI-373552
PSMA1P257863EBI-9250559,EBI-359352
PTGER3Q147X83EBI-9250559,EBI-10234038
SDCBPO005603EBI-9250559,EBI-727004
WDYHV1Q96HA83EBI-9250559,EBI-741158
ZBTB24O431673EBI-9250559,EBI-744471

Protein-protein interaction databases

BioGridi107416. 10 interactions.
IntActiP32320. 8 interactions.
STRINGi9606.ENSP00000364212.

Structurei

Secondary structure

1
146
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 2511Combined sources
Helixi26 – 283Combined sources
Turni32 – 343Combined sources
Beta strandi38 – 436Combined sources
Beta strandi49 – 535Combined sources
Helixi60 – 623Combined sources
Helixi66 – 7611Combined sources
Beta strandi83 – 908Combined sources
Helixi100 – 1078Combined sources
Beta strandi111 – 1188Combined sources
Beta strandi124 – 1285Combined sources
Helixi129 – 1324Combined sources
Helixi139 – 1413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MQ0X-ray2.40A/B11-146[»]
ProteinModelPortaliP32320.
SMRiP32320. Positions 13-142.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32320.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 140128CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 607Substrate binding

Sequence similaritiesi

Contains 1 CMP/dCMP-type deaminase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0295.
GeneTreeiENSGT00390000000911.
HOGENOMiHOG000014707.
HOVERGENiHBG005294.
InParanoidiP32320.
KOiK01489.
OMAiGCRQRIR.
OrthoDBiEOG75B872.
PhylomeDBiP32320.
TreeFamiTF314486.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR006262. Cyt_deam_tetra.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR01354. cyt_deam_tetra. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32320-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQKRPACTL KPECVQQLLV CSQEAKKSAY CPYSHFPVGA ALLTQEGRIF
60 70 80 90 100
KGCNIENACY PLGICAERTA IQKAVSEGYK DFRAIAIASD MQDDFISPCG
110 120 130 140
ACRQVMREFG TNWPVYMTKP DGTYIVMTVQ ELLPSSFGPE DLQKTQ
Length:146
Mass (Da):16,185
Last modified:October 1, 1996 - v2
Checksum:iAF33D09EE4E176B3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271K → Q.2 Publications
Corresponds to variant rs2072671 [ dbSNP | Ensembl ].
VAR_021559

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS210.1.
PIRiI52710.
RefSeqiNP_001776.1. NM_001785.2.
UniGeneiHs.466910.

Genome annotation databases

EnsembliENST00000375071; ENSP00000364212; ENSG00000158825.
GeneIDi978.
KEGGihsa:978.
UCSCiuc001bdk.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS210.1.
PIRiI52710.
RefSeqiNP_001776.1. NM_001785.2.
UniGeneiHs.466910.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MQ0X-ray2.40A/B11-146[»]
ProteinModelPortaliP32320.
SMRiP32320. Positions 13-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107416. 10 interactions.
IntActiP32320. 8 interactions.
STRINGi9606.ENSP00000364212.

Chemistry

BindingDBiP32320.
ChEMBLiCHEMBL4502.
DrugBankiDB00928. Azacitidine.
DB01101. Capecitabine.
DB00987. Cytarabine.
DB00441. Gemcitabine.

PTM databases

PhosphoSiteiP32320.

Polymorphism and mutation databases

BioMutaiCDA.
DMDMi1705718.

Proteomic databases

MaxQBiP32320.
PaxDbiP32320.
PeptideAtlasiP32320.
PRIDEiP32320.

Protocols and materials databases

DNASUi978.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375071; ENSP00000364212; ENSG00000158825.
GeneIDi978.
KEGGihsa:978.
UCSCiuc001bdk.3. human.

Organism-specific databases

CTDi978.
GeneCardsiGC01P020915.
HGNCiHGNC:1712. CDA.
HPAiHPA064202.
MIMi123920. gene.
neXtProtiNX_P32320.
PharmGKBiPA98.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0295.
GeneTreeiENSGT00390000000911.
HOGENOMiHOG000014707.
HOVERGENiHBG005294.
InParanoidiP32320.
KOiK01489.
OMAiGCRQRIR.
OrthoDBiEOG75B872.
PhylomeDBiP32320.
TreeFamiTF314486.

Enzyme and pathway databases

BioCyciMetaCyc:HS08334-MONOMER.
BRENDAi3.5.4.5. 2681.
ReactomeiREACT_655. Pyrimidine salvage reactions.
SABIO-RKP32320.

Miscellaneous databases

ChiTaRSiCDA. human.
EvolutionaryTraceiP32320.
GeneWikiiCytidine_deaminase.
GenomeRNAii978.
NextBioi4112.
PROiP32320.
SOURCEiSearch...

Gene expression databases

BgeeiP32320.
CleanExiHS_CDA.
GenevisibleiP32320. HS.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR006262. Cyt_deam_tetra.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR01354. cyt_deam_tetra. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiCDD_HUMAN
AccessioniPrimary (citable) accession number: P32320
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.