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Q8K2D6 (DCTD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Deoxycytidylate deaminase

EC=3.5.4.12
Alternative name(s):
dCMP deaminase
Gene names
Name:Dctd
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Supplies the nucleotide substrate for thymidylate synthetase By similarity.

Catalytic activity

dCMP + H2O = dUMP + NH3.

Cofactor

Zinc By similarity.

Enzyme regulation

Allosteric enzyme whose activity is greatly influenced by the end products of its metabolic pathway, dCTP and dTTP By similarity.

Subunit structure

Homohexamer By similarity.

Sequence similarities

Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiondCMP deaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 178178Deoxycytidylate deaminase
PRO_0000171692

Sites

Active site861Proton donor By similarity
Metal binding841Zinc; catalytic By similarity
Metal binding1101Zinc; catalytic By similarity
Metal binding1131Zinc; catalytic By similarity

Experimental info

Sequence conflict351S → F in BAC36937. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8K2D6 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: A53ED5C676965029

FASTA17820,059
        10         20         30         40         50         60 
MSDISCKKRD DYLEWPEYFM AVAFLSAQRS KDPSSQVGAC IVNTENKIVG IGYNGMPNGC 

        70         80         90        100        110        120 
SDDLLPWRRT AENKLDTKYP YVCHAELNAI MNKNSADVKG CSMYVALFPC NECAKLIIQA 

       130        140        150        160        170 
GIKEVIFMSD KYHDSEETTA ARLLFKLAGV TFRKFTPKYS KIVIDFDSIN SRPSQKPQ 

« Hide

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: Hypothalamus and Testis.
[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].
Strain: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK031645 mRNA. Translation: BAC27492.1.
AK039066 mRNA. Translation: BAC30229.1.
AK077663 mRNA. Translation: BAC36937.1.
BC031719 mRNA. Translation: AAH31719.1.
RefSeqNP_001154987.1. NM_001161515.1.
NP_001154988.1. NM_001161516.1.
NP_848903.2. NM_178788.4.
UniGeneMm.121549.

3D structure databases

ProteinModelPortalQ8K2D6.
SMRQ8K2D6. Positions 12-173.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8K2D6.

Proteomic databases

PRIDEQ8K2D6.

Protocols and materials databases

DNASU320685.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID320685.
KEGGmmu:320685.
UCSCuc012gdt.1. mouse.

Organism-specific databases

CTD1635.
MGIMGI:2444529. Dctd.

Phylogenomic databases

eggNOGCOG2131.
HOGENOMHOG000015715.
HOVERGENHBG025823.
InParanoidQ8K2D6.
KOK01493.
PhylomeDBQ8K2D6.

Gene expression databases

ArrayExpressQ8K2D6.
BgeeQ8K2D6.
CleanExMM_DCTD.
GenevestigatorQ8K2D6.

Family and domain databases

InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR015517. Cyt_deaminase.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
[Graphical view]
PANTHERPTHR11086. PTHR11086. 1 hit.
PfamPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
PIRSFPIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMSSF53927. SSF53927. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDCTD. mouse.
NextBio397213.
PROQ8K2D6.
SOURCESearch...

Entry information

Entry nameDCTD_MOUSE
AccessionPrimary (citable) accession number: Q8K2D6
Secondary accession number(s): Q8BP55
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 87 of the entry and version 1 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

MGD cross-references

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