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Q8K2D6

- DCTD_MOUSE

UniProt

Q8K2D6 - DCTD_MOUSE

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Protein

Deoxycytidylate deaminase

Gene

Dctd

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Supplies the nucleotide substrate for thymidylate synthetase.By similarity

Catalytic activityi

dCMP + H2O = dUMP + NH3.

Cofactori

Zn2+By similarity

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi84 – 841Zinc; catalyticBy similarity
Active sitei86 – 861Proton donorBy similarity
Metal bindingi110 – 1101Zinc; catalyticBy similarity
Metal bindingi113 – 1131Zinc; catalyticBy similarity

GO - Molecular functioni

  1. dCMP deaminase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. nucleotide biosynthetic process Source: UniProtKB-KW
  2. pyrimidine nucleotide metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_238763. Pyrimidine biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxycytidylate deaminase (EC:3.5.4.12)
Alternative name(s):
dCMP deaminase
Gene namesi
Name:Dctd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:2444529. Dctd.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 178178Deoxycytidylate deaminasePRO_0000171692Add
BLAST

Proteomic databases

MaxQBiQ8K2D6.
PRIDEiQ8K2D6.

PTM databases

PhosphoSiteiQ8K2D6.

Expressioni

Gene expression databases

BgeeiQ8K2D6.
CleanExiMM_DCTD.
ExpressionAtlasiQ8K2D6. baseline and differential.
GenevestigatoriQ8K2D6.

Interactioni

Subunit structurei

Homohexamer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8K2D6.
SMRiQ8K2D6. Positions 12-173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2131.
HOGENOMiHOG000015715.
HOVERGENiHBG025823.
InParanoidiQ8K2D6.
KOiK01493.
PhylomeDBiQ8K2D6.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
IPR015517. dCMP_deaminase-rel.
[Graphical view]
PANTHERiPTHR11086. PTHR11086. 1 hit.
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
PIRSFiPIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K2D6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDISCKKRD DYLEWPEYFM AVAFLSAQRS KDPSSQVGAC IVNTENKIVG
60 70 80 90 100
IGYNGMPNGC SDDLLPWRRT AENKLDTKYP YVCHAELNAI MNKNSADVKG
110 120 130 140 150
CSMYVALFPC NECAKLIIQA GIKEVIFMSD KYHDSEETTA ARLLFKLAGV
160 170
TFRKFTPKYS KIVIDFDSIN SRPSQKPQ
Length:178
Mass (Da):20,059
Last modified:October 1, 2002 - v1
Checksum:iA53ED5C676965029
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351S → F in BAC36937. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031645 mRNA. Translation: BAC27492.1.
AK039066 mRNA. Translation: BAC30229.1.
AK077663 mRNA. Translation: BAC36937.1.
BC031719 mRNA. Translation: AAH31719.1.
RefSeqiNP_001154987.1. NM_001161515.1.
NP_001154988.1. NM_001161516.1.
NP_848903.2. NM_178788.4.
UniGeneiMm.121549.

Genome annotation databases

GeneIDi320685.
KEGGimmu:320685.
UCSCiuc012gdt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031645 mRNA. Translation: BAC27492.1 .
AK039066 mRNA. Translation: BAC30229.1 .
AK077663 mRNA. Translation: BAC36937.1 .
BC031719 mRNA. Translation: AAH31719.1 .
RefSeqi NP_001154987.1. NM_001161515.1.
NP_001154988.1. NM_001161516.1.
NP_848903.2. NM_178788.4.
UniGenei Mm.121549.

3D structure databases

ProteinModelPortali Q8K2D6.
SMRi Q8K2D6. Positions 12-173.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8K2D6.

Proteomic databases

MaxQBi Q8K2D6.
PRIDEi Q8K2D6.

Protocols and materials databases

DNASUi 320685.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 320685.
KEGGi mmu:320685.
UCSCi uc012gdt.1. mouse.

Organism-specific databases

CTDi 1635.
MGIi MGI:2444529. Dctd.

Phylogenomic databases

eggNOGi COG2131.
HOGENOMi HOG000015715.
HOVERGENi HBG025823.
InParanoidi Q8K2D6.
KOi K01493.
PhylomeDBi Q8K2D6.

Enzyme and pathway databases

Reactomei REACT_238763. Pyrimidine biosynthesis.

Miscellaneous databases

ChiTaRSi Dctd. mouse.
NextBioi 397213.
PROi Q8K2D6.
SOURCEi Search...

Gene expression databases

Bgeei Q8K2D6.
CleanExi MM_DCTD.
ExpressionAtlasi Q8K2D6. baseline and differential.
Genevestigatori Q8K2D6.

Family and domain databases

InterProi IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
IPR015517. dCMP_deaminase-rel.
[Graphical view ]
PANTHERi PTHR11086. PTHR11086. 1 hit.
Pfami PF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMi SSF53927. SSF53927. 1 hit.
PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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: 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.

Entry informationi

Entry nameiDCTD_MOUSE
AccessioniPrimary (citable) accession number: Q8K2D6
Secondary accession number(s): Q8BP55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: October 1, 2002
Last modified: November 26, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3