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Protein

Cytidine deaminase

Gene

Cda

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Zn2+1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi65Zinc; catalytic1
Active sitei67Proton donor1 Publication1
Metal bindingi99Zinc; catalytic1
Metal bindingi102Zinc; catalytic1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.4.5 3474
ReactomeiR-MMU-6798695 Neutrophil degranulation
R-MMU-73614 Pyrimidine salvage

Names & Taxonomyi

Protein namesi
Recommended name:
Cytidine deaminase (EC:3.5.4.5)
Alternative name(s):
Cytidine aminohydrolase
Gene namesi
Name:Cda
Synonyms:Cdd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1919519 Cda

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2110

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001716831 – 146Cytidine deaminaseAdd BLAST146

Proteomic databases

MaxQBiP56389
PaxDbiP56389
PeptideAtlasiP56389
PRIDEiP56389

PTM databases

iPTMnetiP56389
PhosphoSitePlusiP56389

Expressioni

Gene expression databases

BgeeiENSMUSG00000028755
CleanExiMM_CDA
GenevisibleiP56389 MM

Interactioni

Subunit structurei

Homotetramer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: MGI
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

MINTiP56389
STRINGi10090.ENSMUSP00000030535

Chemistry databases

BindingDBiP56389

Structurei

Secondary structure

1146
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 26Combined sources14
Turni32 – 34Combined sources3
Beta strandi38 – 44Combined sources7
Beta strandi49 – 53Combined sources5
Helixi60 – 62Combined sources3
Helixi66 – 76Combined sources11
Beta strandi82 – 90Combined sources9
Beta strandi92 – 94Combined sources3
Helixi100 – 108Combined sources9
Beta strandi114 – 118Combined sources5
Beta strandi124 – 128Combined sources5
Helixi129 – 132Combined sources4
Helixi139 – 142Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZABX-ray2.36A/B/C/D1-146[»]
2FR5X-ray1.48A/B/C/D1-146[»]
2FR6X-ray2.07A/B/C/D1-146[»]
ProteinModelPortaliP56389
SMRiP56389
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56389

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 140CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd BLAST128

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni54 – 56Substrate binding3

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0833 Eukaryota
COG0295 LUCA
GeneTreeiENSGT00390000000911
HOGENOMiHOG000014707
HOVERGENiHBG005294
InParanoidiP56389
KOiK01489
OMAiAVYMTKP
OrthoDBiEOG091G09D3
PhylomeDBiP56389
TreeFamiTF314486

Family and domain databases

InterProiView protein in InterPro
IPR016192 APOBEC/CMP_deaminase_Zn-bd
IPR002125 CMP_dCMP_dom
IPR006262 Cyt_deam_tetra
IPR016193 Cytidine_deaminase-like
PfamiView protein in Pfam
PF00383 dCMP_cyt_deam_1, 1 hit
SUPFAMiSSF53927 SSF53927, 1 hit
TIGRFAMsiTIGR01354 cyt_deam_tetra, 1 hit
PROSITEiView protein in PROSITE
PS00903 CYT_DCMP_DEAMINASES_1, 1 hit
PS51747 CYT_DCMP_DEAMINASES_2, 1 hit

Sequencei

Sequence statusi: Complete.

P56389-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQERPSCAV EPEHVQRLLL SSREAKKSAY CPYSRFPVGA ALLTGDGRIF
60 70 80 90 100
SGCNIENACY PLGVCAERTA IQKAISEGYK DFRAIAISSD LQEEFISPCG
110 120 130 140
ACRQVMREFG TDWAVYMTKP DGTFVVRTVQ ELLPASFGPE DLQKIQ
Length:146
Mass (Da):16,131
Last modified:March 29, 2005 - v2
Checksum:iD4181CE6BA9CD794
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008793 mRNA Translation: BAB25898.1
BC050114 mRNA Translation: AAH50114.1
CCDSiCCDS18826.1
RefSeqiNP_082452.1, NM_028176.1
UniGeneiMm.46182

Genome annotation databases

EnsembliENSMUST00000030535; ENSMUSP00000030535; ENSMUSG00000028755
GeneIDi72269
KEGGimmu:72269
UCSCiuc008vkw.1 mouse

Similar proteinsi

Entry informationi

Entry nameiCDD_MOUSE
AccessioniPrimary (citable) accession number: P56389
Secondary accession number(s): Q9D7V3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: March 29, 2005
Last modified: June 20, 2018
This is version 137 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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