ID   DCK_RAT                 Reviewed;         260 AA.
AC   P48769;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-NOV-2023, entry version 132.
DE   RecName: Full=Deoxycytidine kinase;
DE            Short=dCK;
DE            EC=2.7.1.74 {ECO:0000250|UniProtKB:P27707};
DE   AltName: Full=Deoxyadenosine kinase;
DE            EC=2.7.1.76 {ECO:0000250|UniProtKB:P27707};
DE   AltName: Full=Deoxyguanosine kinase;
DE            EC=2.7.1.113 {ECO:0000250|UniProtKB:P27707};
GN   Name=Dck;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7821805; DOI=10.1016/0378-1119(94)90451-0;
RA   Stegmann A.P., Honders M.W., Willemze R., Landegent J.E.;
RT   "Cloning of the Dck gene encoding rat deoxycytidine kinase.";
RL   Gene 150:351-354(1994).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Phosphorylates the deoxyribonucleosides deoxycytidine,
CC       deoxyguanosine and deoxyadenosine. {ECO:0000250|UniProtKB:P27707}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxycytidine + a ribonucleoside 5'-triphosphate = a
CC         ribonucleoside 5'-diphosphate + dCMP + H(+); Xref=Rhea:RHEA:20061,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:57566,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=2.7.1.74;
CC         Evidence={ECO:0000250|UniProtKB:P27707};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyadenosine + ATP = ADP + dAMP + H(+);
CC         Xref=Rhea:RHEA:23452, ChEBI:CHEBI:15378, ChEBI:CHEBI:17256,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58245, ChEBI:CHEBI:456216;
CC         EC=2.7.1.76; Evidence={ECO:0000250|UniProtKB:P27707};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyguanosine + ATP = ADP + dGMP + H(+);
CC         Xref=Rhea:RHEA:19201, ChEBI:CHEBI:15378, ChEBI:CHEBI:17172,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57673, ChEBI:CHEBI:456216;
CC         EC=2.7.1.113; Evidence={ECO:0000250|UniProtKB:P27707};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P27707}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27707}.
CC   -!- PTM: Phosphorylated and activated in vitro upon phosphorylation at Ser-
CC       74 by CSNK1D/CK1. {ECO:0000250|UniProtKB:P27707}.
CC   -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR   EMBL; L33894; AAA65098.1; -; mRNA.
DR   RefSeq; NP_077072.1; NM_024158.1.
DR   AlphaFoldDB; P48769; -.
DR   SMR; P48769; -.
DR   STRING; 10116.ENSRNOP00000004440; -.
DR   ChEMBL; CHEMBL3271929; -.
DR   iPTMnet; P48769; -.
DR   PhosphoSitePlus; P48769; -.
DR   PaxDb; 10116-ENSRNOP00000004440; -.
DR   GeneID; 79127; -.
DR   KEGG; rno:79127; -.
DR   UCSC; RGD:620667; rat.
DR   AGR; RGD:620667; -.
DR   CTD; 1633; -.
DR   RGD; 620667; Dck.
DR   eggNOG; KOG4235; Eukaryota.
DR   InParanoid; P48769; -.
DR   OrthoDB; 315858at2759; -.
DR   PhylomeDB; P48769; -.
DR   Reactome; R-RNO-73614; Pyrimidine salvage.
DR   Reactome; R-RNO-74217; Purine salvage.
DR   SABIO-RK; P48769; -.
DR   PRO; PR:P48769; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0043771; F:cytidine kinase activity; ISO:RGD.
DR   GO; GO:0004136; F:deoxyadenosine kinase activity; ISO:RGD.
DR   GO; GO:0004137; F:deoxycytidine kinase activity; IDA:RGD.
DR   GO; GO:0004138; F:deoxyguanosine kinase activity; ISO:RGD.
DR   GO; GO:0032546; F:deoxyribonucleoside binding; IPI:RGD.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0032548; F:pyrimidine deoxyribonucleoside binding; IDA:RGD.
DR   GO; GO:0106383; P:dAMP salvage; ISO:RGD.
DR   GO; GO:0046092; P:deoxycytidine metabolic process; IDA:RGD.
DR   GO; GO:1901293; P:nucleoside phosphate biosynthetic process; ISO:RGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; ISS:UniProtKB.
DR   CDD; cd01673; dNK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR002624; DCK/DGK.
DR   InterPro; IPR031314; DNK_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10513:SF19; DEOXYCYTIDINE KINASE; 1.
DR   PANTHER; PTHR10513; DEOXYNUCLEOSIDE KINASE; 1.
DR   Pfam; PF01712; dNK; 1.
DR   PIRSF; PIRSF000705; DNK; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..260
FT                   /note="Deoxycytidine kinase"
FT                   /id="PRO_0000175092"
FT   ACT_SITE        127
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         28..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         188..192
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         240..242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="Phosphoserine; by CK1"
FT                   /evidence="ECO:0000250|UniProtKB:P27707"
FT   MOD_RES         15
FT                   /note="Phosphoserine; by CK1"
FT                   /evidence="ECO:0000250|UniProtKB:P27707"
FT   MOD_RES         72
FT                   /note="Phosphothreonine; by CK1"
FT                   /evidence="ECO:0000250|UniProtKB:P27707"
FT   MOD_RES         74
FT                   /note="Phosphoserine; by CK1"
FT                   /evidence="ECO:0000250|UniProtKB:P27707"
SQ   SEQUENCE   260 AA;  30406 MW;  4F6C9FAAC09EDBB7 CRC64;
     MATPPKRFCS SPSTSSEGTR IKKISIEGNI AAGKSTFVNI LKQVCEDWEV VPEPVARWCN
     VQSTQDEFEE LTTSQKSGGN VLQMMYEKPE RWSFIFQSYA CLSRIRAQLA SLNGSLRDAE
     KPVLFFERSV YSDRYIFASN LYESDCMNET EWTIYQDWHD WMNSQFGQSL ELDGIIYLRA
     TPEKCLNRIY IRGRDEEQGI PLEYLEKLHY KHESWLLHRT LKTNFEYLQE VPILTLDVNL
     DFKDKEESLV EKVKEFLSTT
//