DCTD_MOUSE
ID DCTD_MOUSE Reviewed; 178 AA.
AC Q8K2D6; Q8BP55;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Deoxycytidylate deaminase;
DE EC=3.5.4.12;
DE AltName: Full=dCMP deaminase;
GN Name=Dctd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Supplies the nucleotide substrate for thymidylate synthetase.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dCMP + H(+) + H2O = dUMP + NH4(+); Xref=Rhea:RHEA:22924,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57566, ChEBI:CHEBI:246422; EC=3.5.4.12;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Allosteric enzyme whose activity is greatly
CC influenced by the end products of its metabolic pathway, dCTP and dTTP.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK031645; BAC27492.1; -; mRNA.
DR EMBL; AK039066; BAC30229.1; -; mRNA.
DR EMBL; AK077663; BAC36937.1; -; mRNA.
DR EMBL; BC031719; AAH31719.1; -; mRNA.
DR CCDS; CCDS22302.2; -.
DR RefSeq; NP_001154987.1; NM_001161515.1.
DR RefSeq; NP_001154988.1; NM_001161516.1.
DR RefSeq; NP_848903.2; NM_178788.4.
DR AlphaFoldDB; Q8K2D6; -.
DR SMR; Q8K2D6; -.
DR STRING; 10090.ENSMUSP00000126733; -.
DR PhosphoSitePlus; Q8K2D6; -.
DR EPD; Q8K2D6; -.
DR MaxQB; Q8K2D6; -.
DR PaxDb; Q8K2D6; -.
DR PRIDE; Q8K2D6; -.
DR ProteomicsDB; 279508; -.
DR DNASU; 320685; -.
DR Ensembl; ENSMUST00000033966; ENSMUSP00000033966; ENSMUSG00000031562.
DR Ensembl; ENSMUST00000170263; ENSMUSP00000126733; ENSMUSG00000031562.
DR Ensembl; ENSMUST00000174278; ENSMUSP00000133445; ENSMUSG00000031562.
DR GeneID; 320685; -.
DR KEGG; mmu:320685; -.
DR UCSC; uc012gdt.1; mouse.
DR CTD; 1635; -.
DR MGI; MGI:2444529; Dctd.
DR eggNOG; KOG3127; Eukaryota.
DR GeneTree; ENSGT00940000153676; -.
DR InParanoid; Q8K2D6; -.
DR OrthoDB; 1569973at2759; -.
DR PhylomeDB; Q8K2D6; -.
DR Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR BioGRID-ORCS; 320685; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Dctd; mouse.
DR PRO; PR:Q8K2D6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8K2D6; protein.
DR GO; GO:0004132; F:dCMP deaminase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006231; P:dTMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central.
DR CDD; cd01286; deoxycytidylate_deaminase; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR016473; dCMP_deaminase.
DR InterPro; IPR015517; dCMP_deaminase-rel.
DR InterPro; IPR035105; Deoxycytidylate_deaminase_dom.
DR PANTHER; PTHR11086; PTHR11086; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR PIRSF; PIRSF006019; dCMP_deaminase; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme; Hydrolase; Metal-binding; Nucleotide biosynthesis;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..178
FT /note="Deoxycytidylate deaminase"
FT /id="PRO_0000171692"
FT DOMAIN 14..145
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 86
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32321"
FT CONFLICT 35
FT /note="S -> F (in Ref. 1; BAC36937)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 20059 MW; A53ED5C676965029 CRC64;
MSDISCKKRD DYLEWPEYFM AVAFLSAQRS KDPSSQVGAC IVNTENKIVG IGYNGMPNGC
SDDLLPWRRT AENKLDTKYP YVCHAELNAI MNKNSADVKG CSMYVALFPC NECAKLIIQA
GIKEVIFMSD KYHDSEETTA ARLLFKLAGV TFRKFTPKYS KIVIDFDSIN SRPSQKPQ
