DCK_RAT
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 03-AUG-2022, entry version 126.
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; P48769; -.
DR PRIDE; P48769; -.
DR GeneID; 79127; -.
DR KEGG; rno:79127; -.
DR UCSC; RGD:620667; rat.
DR CTD; 1633; -.
DR RGD; 620667; Dck.
DR eggNOG; KOG4235; Eukaryota.
DR InParanoid; P48769; -.
DR OrthoDB; 1505356at2759; -.
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:0005829; C:cytosol; IDA:RGD.
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: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:0019136; F:deoxynucleoside kinase activity; IBA:GO_Central.
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:0046939; P:nucleotide phosphorylation; IDA:RGD.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; ISS:UniProtKB.
DR CDD; cd01673; dNK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002624; DCK/DGK.
DR InterPro; IPR031314; DNK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01712; dNK; 1.
DR PIRSF; PIRSF000705; DNK; 1.
DR SUPFAM; SSF52540; SSF52540; 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
