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   16-JUN-2009, entry version 52.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Supplies the nucleotide substrate for thymidylate
CC       synthetase (By similarity).
CC   -!- CATALYTIC ACTIVITY: dCMP + H(2)O = dUMP + NH(3).
CC   -!- COFACTOR: Zinc (By similarity).
CC   -!- ENZYME REGULATION: Allosteric enzyme whose activity is greatly
CC       influenced by the end products of its metabolic pathway, dCTP and
CC       dTTP (By similarity).
CC   -!- SUBUNIT: Homohexamer (By similarity).
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family.
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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   IPI; IPI00267960; -.
DR   RefSeq; NP_848903.1; -.
DR   UniGene; Mm.121549; -.
DR   PhosphoSite; Q8K2D6; -.
DR   Ensembl; ENSMUSG00000031562; Mus musculus.
DR   GeneID; 320685; -.
DR   KEGG; mmu:320685; -.
DR   MGI; MGI:2444529; Dctd.
DR   HOGENOM; Q8K2D6; -.
DR   HOVERGEN; Q8K2D6; -.
DR   OMA; Q8K2D6; ARRSTCL.
DR   BRENDA; 3.5.4.12; 244.
DR   NextBio; 397213; -.
DR   ArrayExpress; Q8K2D6; -.
DR   Bgee; Q8K2D6; -.
DR   CleanEx; MM_DCTD; -.
DR   GO; GO:0004132; F:dCMP deaminase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_Zn_bd.
DR   InterPro; IPR015517; Cyt_deaminase.
DR   InterPro; IPR016473; dCMP_deaminase.
DR   PANTHER; PTHR11086; Cyt_deaminase; 1.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   PIRSF; PIRSF006019; dCMP_deaminase; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Hydrolase; Metal-binding; Nucleotide biosynthesis;
KW   Phosphoprotein; Zinc.
FT   CHAIN         1    178       Deoxycytidylate deaminase.
FT                                /FTId=PRO_0000171692.
FT   ACT_SITE     86     86       Proton donor (By similarity).
FT   METAL        84     84       Zinc; catalytic (By similarity).
FT   METAL       110    110       Zinc; catalytic (By similarity).
FT   METAL       113    113       Zinc; catalytic (By similarity).
FT   MOD_RES      79     79       Phosphotyrosine (By similarity).
FT   CONFLICT     35     35       S -> F (in Ref. 1; BAC36937).
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
//