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Protein

Cytidine deaminase

Gene

Cda

Organism
Mus musculus (Mouse)
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.By similarity

Catalytic activityi

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

Cofactori

Zn2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi65 – 651Zinc; catalytic
Active sitei67 – 671Proton donor1 Publication
Metal bindingi99 – 991Zinc; catalytic
Metal bindingi102 – 1021Zinc; catalytic

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.4.5. 3474.
ReactomeiREACT_295314. Pyrimidine salvage reactions.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1919519. Cda.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 146146Cytidine deaminasePRO_0000171683Add
BLAST

Proteomic databases

MaxQBiP56389.
PaxDbiP56389.
PRIDEiP56389.

PTM databases

PhosphoSiteiP56389.

Expressioni

Gene expression databases

BgeeiP56389.
CleanExiMM_CDA.
ExpressionAtlasiP56389. baseline and differential.
GenevisibleiP56389. MM.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

MINTiMINT-218728.
STRINGi10090.ENSMUSP00000030535.

Structurei

Secondary structure

1
146
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2614Combined sources
Turni32 – 343Combined sources
Beta strandi38 – 447Combined sources
Beta strandi49 – 535Combined sources
Helixi60 – 623Combined sources
Helixi66 – 7611Combined sources
Beta strandi82 – 909Combined sources
Beta strandi92 – 943Combined sources
Helixi100 – 1089Combined sources
Beta strandi114 – 1185Combined sources
Beta strandi124 – 1285Combined sources
Helixi129 – 1324Combined sources
Helixi139 – 1424Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 10-146.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56389.

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 – 563Substrate binding

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0295.
GeneTreeiENSGT00390000000911.
HOGENOMiHOG000014707.
HOVERGENiHBG005294.
InParanoidiP56389.
KOiK01489.
OMAiKLVKMAL.
OrthoDBiEOG75B872.
PhylomeDBiP56389.
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.

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 10-146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-218728.
STRINGi10090.ENSMUSP00000030535.

Chemistry

BindingDBiP56389.
ChEMBLiCHEMBL2110.

PTM databases

PhosphoSiteiP56389.

Proteomic databases

MaxQBiP56389.
PaxDbiP56389.
PRIDEiP56389.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi978.
MGIiMGI:1919519. Cda.

Phylogenomic databases

eggNOGiCOG0295.
GeneTreeiENSGT00390000000911.
HOGENOMiHOG000014707.
HOVERGENiHBG005294.
InParanoidiP56389.
KOiK01489.
OMAiKLVKMAL.
OrthoDBiEOG75B872.
PhylomeDBiP56389.
TreeFamiTF314486.

Enzyme and pathway databases

BRENDAi3.5.4.5. 3474.
ReactomeiREACT_295314. Pyrimidine salvage reactions.

Miscellaneous databases

EvolutionaryTraceiP56389.
NextBioi335863.
PROiP56389.
SOURCEiSearch...

Gene expression databases

BgeeiP56389.
CleanExiMM_CDA.
ExpressionAtlasiP56389. baseline and differential.
GenevisibleiP56389. MM.

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. "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.
    , 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.

Entry informationi

Entry nameiCDD_MOUSE
AccessioniPrimary (citable) accession number: P56389
Secondary accession number(s): Q9D7V3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: March 29, 2005
Last modified: July 22, 2015
This is version 120 of the entry and version 2 of the sequence. [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

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.