ID   DCTD_HUMAN              Reviewed;         178 AA.
AC   P32321; Q9BVD8;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 2.
DT   07-JUL-2009, entry version 83.
DE   RecName: Full=Deoxycytidylate deaminase;
DE            EC=3.5.4.12;
DE   AltName: Full=dCMP deaminase;
GN   Name=DCTD;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=93286150; PubMed=7685356;
RA   Weiner K.X., Weiner R.S., Maley F., Maley G.F.;
RT   "Primary structure of human deoxycytidylate deaminase and
RT   overexpression of its functional protein in Escherichia coli.";
RL   J. Biol. Chem. 268:12983-12989(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Lung;
RX   MEDLINE=95370171; PubMed=7642519; DOI=10.1074/jbc.270.32.18727;
RA   Weiner K.X., Ciesla J., Jaffe A.B., Ketring R., Maley F., Maley G.F.;
RT   "Chromosomal location and structural organization of the human
RT   deoxycytidylate deaminase gene.";
RL   J. Biol. Chem. 270:18727-18729(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cervix;
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).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-79, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [5]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: Supplies the nucleotide substrate for thymidylate
CC       synthetase.
CC   -!- CATALYTIC ACTIVITY: dCMP + H(2)O = dUMP + NH(3).
CC   -!- COFACTOR: Zinc.
CC   -!- ENZYME REGULATION: Allosteric enzyme whose activity is greatly
CC       influenced by the end products of its metabolic pathway, dCTP and
CC       dTTP.
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family.
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DR   EMBL; L12136; AAA35755.1; -; mRNA.
DR   EMBL; L39874; AAC37579.1; -; Genomic_DNA.
DR   EMBL; BC001286; AAH01286.1; -; mRNA.
DR   IPI; IPI00296863; -.
DR   PIR; A47288; A47288.
DR   PIR; I55434; I55434.
DR   RefSeq; NP_001912.2; -.
DR   UniGene; Hs.183850; -.
DR   PDB; 2W4L; X-ray; 2.10 A; A/B/C/D/E/F=5-173.
DR   PDBsum; 2W4L; -.
DR   IntAct; P32321; 5.
DR   PhosphoSite; P32321; -.
DR   PRIDE; P32321; -.
DR   Ensembl; ENSG00000129187; Homo sapiens.
DR   GeneID; 1635; -.
DR   UCSC; uc003ivf.1; human.
DR   GeneCards; GC04M184048; -.
DR   H-InvDB; HIX0004657; -.
DR   HGNC; HGNC:2710; DCTD.
DR   MIM; 607638; gene.
DR   PharmGKB; PA138; -.
DR   HOVERGEN; P32321; -.
DR   BRENDA; 3.5.4.12; 247.
DR   Reactome; REACT_1698; Metablism of nucleotides.
DR   NextBio; 6716; -.
DR   ArrayExpress; P32321; -.
DR   Bgee; P32321; -.
DR   CleanEx; HS_DCTD; -.
DR   GermOnline; ENSG00000129187; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0004132; F:dCMP deaminase activity; EXP:Reactome.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; TAS:ProtInc.
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   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; Complete proteome;
KW   Direct protein sequencing; Hydrolase; Metal-binding;
KW   Nucleotide biosynthesis; Phosphoprotein; Zinc.
FT   CHAIN         1    178       Deoxycytidylate deaminase.
FT                                /FTId=PRO_0000171691.
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.
FT   CONFLICT     95     95       S -> L (in Ref. 3; AAH01286).
FT   CONFLICT    128    128       M -> T (in Ref. 1; AAA35755).
SQ   SEQUENCE   178 AA;  20016 MW;  2B8DA5EAC85F3666 CRC64;
     MSEVSCKKRD DYLEWPEYFM AVAFLSAQRS KDPNSQVGAC IVNSENKIVG IGYNGMPNGC
     SDDVLPWRRT AENKLDTKYP YVCHAELNAI MNKNSTDVKG CSMYVALFPC NECAKLIIQA
     GIKEVIFMSD KYHDSDEATA ARLLFNMAGV TFRKFIPKCS KIVIDFDSIN SRPSQKLQ
//