P56389 (CDD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytidine deaminase
EC=3.5.4.5

Alternative name(s):
Cytidine aminohydrolase

Gene names

Name:	Cda
Synonyms:	Cdd

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	146 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of nucleotide metabolic process Inferred from sequence or structural similarity. Source: UniProtKB protein homotetramerization Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	cytidine deaminase activity Inferred from sequence or structural similarity. Source: UniProtKB nucleoside binding Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 146

146

Cytidine deaminase

PRO_0000171683

Regions

Domain

16 – 117

102

CMP/dCMP deaminase zinc-binding

Region

54 – 56

3

Substrate binding

Sites

Active site

67

1

Proton donor Ref.3

Metal binding

65

1

Zinc; catalytic

Metal binding

99

1

Zinc; catalytic

Metal binding

102

1

Zinc; catalytic

Secondary structure

1

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146

Helix Strand Turn

Details...

Helix

13 – 26

14

Turn

32 – 34

3

Beta strand

38 – 44

7

Beta strand

49 – 53

5

Helix

60 – 62

3

Helix

66 – 76

11

Beta strand

82 – 90

9

Beta strand

92 – 94

3

Helix

100 – 108

9

Beta strand

114 – 118

5

Beta strand

124 – 128

5

Helix

129 – 132

4

Helix

139 – 142

4

Sequences

	Sequence		Length	Mass (Da)
	P56389 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: D4181CE6BA9CD794	FASTA	146	16,131
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00110866.

RefSeq

NP_082452.1. NM_028176.1.

UniGene

Mm.46182.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZAB	X-ray	2.36	A/B/C/D	1-146	[»]
2FR5	X-ray	1.48	A/B/C/D	1-146	[»]
2FR6	X-ray	2.07	A/B/C/D	1-146	[»]

ProteinModelPortal

P56389.

SMR

P56389. Positions 10-146.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-218728.

PTM databases

PhosphoSite

P56389.

Proteomic databases

PaxDb

P56389.

PRIDE

P56389.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000030535; ENSMUSP00000030535; ENSMUSG00000028755.

GeneID

72269.

KEGG

mmu:72269.

Organism-specific databases

CTD

978.

MGI

MGI:1919519. Cda.

Phylogenomic databases

eggNOG

COG0295.

GeneTree

ENSGT00390000000911.

HOGENOM

HOG000014707.

HOVERGEN

HBG005294.

InParanoid

P56389.

KO

K01489.

OMA

KLVKMAL.

OrthoDB

EOG4WSWBW.

Gene expression databases

ArrayExpress

P56389.

Bgee

P56389.

CleanEx

MM_CDA.

Genevestigator

P56389.

GermOnline

ENSMUSG00000028755. Mus musculus.

Family and domain databases

InterPro

IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR006262. Cyt_deam_tetra.
IPR016193. Cytidine_deaminase-like.
[Graphical view]

Pfam

PF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]

SUPFAM

SSF53927. Cytidine_deaminase-like. 1 hit.

TIGRFAMs

TIGR01354. cyt_deam_tetra. 1 hit.

PROSITE

PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P56389.

ChEMBL

CHEMBL2110.

EvolutionaryTrace

P56389.

NextBio

335863.

SOURCE

Search...

Entry information

Entry name

CDD_MOUSE

Accession

Primary (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 3, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program