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P56389

- CDD_MOUSE

UniProt

P56389 - CDD_MOUSE

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Protein

Cytidine deaminase

Gene
Cda, Cdd
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Zinc.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

  1. cytidine deaminase activity Source: UniProtKB
  2. identical protein binding Source: MGI
  3. nucleoside binding Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB
  5. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cytidine deamination Source: UniProtKB
  2. negative regulation of cell growth Source: UniProtKB
  3. negative regulation of nucleotide metabolic process Source: UniProtKB
  4. protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

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: 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

ArrayExpressiP56389.
BgeeiP56389.
CleanExiMM_CDA.
GenevestigatoriP56389.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

MINTiMINT-218728.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP56389.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 117102CMP/dCMP deaminase zinc-bindingAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 563Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0295.
GeneTreeiENSGT00390000000911.
HOGENOMiHOG000014707.
HOVERGENiHBG005294.
InParanoidiP56389.
KOiK01489.
OMAiTDWAVYM.
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 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56389-1 [UniParc]FASTAAdd to Basket

« Hide

MAQERPSCAV EPEHVQRLLL SSREAKKSAY CPYSRFPVGA ALLTGDGRIF    50
SGCNIENACY PLGVCAERTA IQKAISEGYK DFRAIAISSD LQEEFISPCG 100
ACRQVMREFG TDWAVYMTKP DGTFVVRTVQ ELLPASFGPE DLQKIQ 146
Length:146
Mass (Da):16,131
Last modified:March 29, 2005 - v2
Checksum:iD4181CE6BA9CD794
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK008793 mRNA. Translation: BAB25898.1 .
BC050114 mRNA. Translation: AAH50114.1 .
CCDSi CCDS18826.1.
RefSeqi NP_082452.1. NM_028176.1.
UniGenei Mm.46182.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P56389.
SMRi P56389. Positions 10-146.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-218728.

Chemistry

BindingDBi P56389.
ChEMBLi CHEMBL2110.

PTM databases

PhosphoSitei P56389.

Proteomic databases

MaxQBi P56389.
PaxDbi P56389.
PRIDEi P56389.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030535 ; ENSMUSP00000030535 ; ENSMUSG00000028755 .
GeneIDi 72269.
KEGGi mmu:72269.
UCSCi uc008vkw.1. mouse.

Organism-specific databases

CTDi 978.
MGIi MGI:1919519. Cda.

Phylogenomic databases

eggNOGi COG0295.
GeneTreei ENSGT00390000000911.
HOGENOMi HOG000014707.
HOVERGENi HBG005294.
InParanoidi P56389.
KOi K01489.
OMAi TDWAVYM.
OrthoDBi EOG75B872.
PhylomeDBi P56389.
TreeFami TF314486.

Miscellaneous databases

EvolutionaryTracei P56389.
NextBioi 335863.
PROi P56389.
SOURCEi Search...

Gene expression databases

ArrayExpressi P56389.
Bgeei P56389.
CleanExi MM_CDA.
Genevestigatori P56389.

Family and domain databases

InterProi IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR006262. Cyt_deam_tetra.
IPR016193. Cytidine_deaminase-like.
[Graphical view ]
Pfami PF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view ]
SUPFAMi SSF53927. SSF53927. 1 hit.
TIGRFAMsi TIGR01354. cyt_deam_tetra. 1 hit.
PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 9, 2014
This is version 112 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

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