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P56389 (CDD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

General annotation (Comments)

Function

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

Catalytic activity

Cytidine + H2O = uridine + NH3.

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

Cofactor

Zinc. Ref.3

Subunit structure

Homotetramer. Ref.3

Sequence similarities

Belongs to the cytidine and deoxycytidylate deaminase family.

Contains 1 CMP/dCMP deaminase zinc-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 146146Cytidine deaminase
PRO_0000171683

Regions

Domain16 – 117102CMP/dCMP deaminase zinc-binding
Region54 – 563Substrate binding

Sites

Active site671Proton donor Ref.3
Metal binding651Zinc; catalytic
Metal binding991Zinc; catalytic
Metal binding1021Zinc; catalytic

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P56389 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: D4181CE6BA9CD794

FASTA14616,131
        10         20         30         40         50         60 
MAQERPSCAV EPEHVQRLLL SSREAKKSAY CPYSRFPVGA ALLTGDGRIF SGCNIENACY 

        70         80         90        100        110        120 
PLGVCAERTA IQKAISEGYK DFRAIAISSD LQEEFISPCG ACRQVMREFG TDWAVYMTKP 

       130        140 
DGTFVVRTVQ ELLPASFGPE DLQKIQ 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Stomach.
[2]"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].
Tissue: Pancreas.
[3]"The 1.48 A resolution crystal structure of the homotetrameric cytidine deaminase from mouse."
Teh A.H., Kimura M., Yamamoto M., Tanaka N., Yamaguchi I., Kumasaka T.
Biochemistry 45:7825-7833(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH CYTIDINE, SUBUNIT, COFACTOR, ACTIVE SITE, SUBSTRATE-BINDING REGION, ZINC-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK008793 mRNA. Translation: BAB25898.1.
BC050114 mRNA. Translation: AAH50114.1.
RefSeqNP_082452.1. NM_028176.1.
UniGeneMm.46182.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZABX-ray2.36A/B/C/D1-146[»]
2FR5X-ray1.48A/B/C/D1-146[»]
2FR6X-ray2.07A/B/C/D1-146[»]
ProteinModelPortalP56389.
SMRP56389. Positions 10-146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-218728.

Chemistry

BindingDBP56389.
ChEMBLCHEMBL2110.

PTM databases

PhosphoSiteP56389.

Proteomic databases

PaxDbP56389.
PRIDEP56389.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030535; ENSMUSP00000030535; ENSMUSG00000028755.
GeneID72269.
KEGGmmu:72269.
UCSCuc008vkw.1. mouse.

Organism-specific databases

CTD978.
MGIMGI:1919519. Cda.

Phylogenomic databases

eggNOGCOG0295.
GeneTreeENSGT00390000000911.
HOGENOMHOG000014707.
HOVERGENHBG005294.
InParanoidP56389.
KOK01489.
OMADLHDERK.
OrthoDBEOG75B872.
PhylomeDBP56389.
TreeFamTF314486.

Gene expression databases

ArrayExpressP56389.
BgeeP56389.
CleanExMM_CDA.
GenevestigatorP56389.

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

EvolutionaryTraceP56389.
NextBio335863.
PROP56389.
SOURCESearch...

Entry information

Entry nameCDD_MOUSE
AccessionPrimary (citable) accession number: P56389
Secondary accession number(s): Q9D7V3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: March 29, 2005
Last modified: April 16, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot