DGUOK_MOUSE
ID DGUOK_MOUSE Reviewed; 277 AA.
AC Q9QX60; Q8CBU2; Q9R0Y2; Q9WUT9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Deoxyguanosine kinase, mitochondrial;
DE EC=2.7.1.113 {ECO:0000269|PubMed:10455141};
DE AltName: Full=Deoxyadenosine kinase, mitochondrial;
DE EC=2.7.1.76 {ECO:0000269|PubMed:10455141};
DE Flags: Precursor;
GN Name=Dguok; Synonyms=Dgk;
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=10455141; DOI=10.1074/jbc.274.35.24726;
RA Petrakis T.G., Ktistaki E., Wang L., Eriksson S., Talianidis I.;
RT "Cloning and characterization of mouse deoxyguanosine kinase. Evidence for
RT a cytoplasmic isoform.";
RL J. Biol. Chem. 274:24726-24730(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Johansson M., Holmdahl L., Karlsson A.;
RT "Cloning of mouse deoxyguanosine kinase cDNA.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Phosphorylates deoxyguanosine and deoxyadenosine in the
CC mitochondrial matrix, with the highest efficiency for deoxyguanosine
CC (PubMed:10455141). In non-replicating cells, where cytosolic dNTP
CC synthesis is down-regulated, mtDNA synthesis depends solely on DGUOK
CC and TK2. Phosphorylates certain nucleoside analogs (PubMed:10455141).
CC Widely used as target of antiviral and chemotherapeutic agents.
CC {ECO:0000250|UniProtKB:Q16854, ECO:0000269|PubMed:10455141}.
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:0000269|PubMed:10455141};
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:0000269|PubMed:10455141};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q16854}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000269|PubMed:10455141}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:10455141}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QX60-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QX60-2; Sequence=VSP_003027;
CC -!- TISSUE SPECIFICITY: Spleen and thymus. Expressed at much lower levels
CC in the brain and liver. {ECO:0000269|PubMed:10455141}.
CC -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR EMBL; AJ133749; CAB43121.1; -; mRNA.
DR EMBL; AJ133750; CAB43122.1; -; mRNA.
DR EMBL; U90524; AAF14342.1; -; mRNA.
DR EMBL; AK035281; BAC29014.1; -; mRNA.
DR EMBL; AC090648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466523; EDK99082.1; -; Genomic_DNA.
DR CCDS; CCDS20279.1; -. [Q9QX60-1]
DR RefSeq; NP_038792.2; NM_013764.2. [Q9QX60-1]
DR AlphaFoldDB; Q9QX60; -.
DR SMR; Q9QX60; -.
DR STRING; 10090.ENSMUSP00000014698; -.
DR iPTMnet; Q9QX60; -.
DR PhosphoSitePlus; Q9QX60; -.
DR SwissPalm; Q9QX60; -.
DR EPD; Q9QX60; -.
DR MaxQB; Q9QX60; -.
DR PaxDb; Q9QX60; -.
DR PeptideAtlas; Q9QX60; -.
DR PRIDE; Q9QX60; -.
DR ProteomicsDB; 279525; -. [Q9QX60-1]
DR ProteomicsDB; 279526; -. [Q9QX60-2]
DR Antibodypedia; 31404; 216 antibodies from 25 providers.
DR DNASU; 27369; -.
DR Ensembl; ENSMUST00000014698; ENSMUSP00000014698; ENSMUSG00000014554. [Q9QX60-1]
DR GeneID; 27369; -.
DR KEGG; mmu:27369; -.
DR UCSC; uc009cnn.2; mouse. [Q9QX60-1]
DR CTD; 1716; -.
DR MGI; MGI:1351602; Dguok.
DR VEuPathDB; HostDB:ENSMUSG00000014554; -.
DR eggNOG; KOG4235; Eukaryota.
DR GeneTree; ENSGT00940000159627; -.
DR InParanoid; Q9QX60; -.
DR OMA; LMIYLRC; -.
DR OrthoDB; 1505356at2759; -.
DR PhylomeDB; Q9QX60; -.
DR TreeFam; TF324413; -.
DR BRENDA; 2.7.1.113; 3474.
DR Reactome; R-MMU-74217; Purine salvage.
DR SABIO-RK; Q9QX60; -.
DR BioGRID-ORCS; 27369; 5 hits in 74 CRISPR screens.
DR PRO; PR:Q9QX60; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9QX60; protein.
DR Bgee; ENSMUSG00000014554; Expressed in retinal neural layer and 253 other tissues.
DR ExpressionAtlas; Q9QX60; baseline and differential.
DR Genevisible; Q9QX60; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004136; F:deoxyadenosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004138; F:deoxyguanosine kinase activity; IDA:MGI.
DR GO; GO:0019136; F:deoxynucleoside kinase activity; IDA:MGI.
DR GO; GO:0006754; P:ATP biosynthetic process; ISO:MGI.
DR GO; GO:0106383; P:dAMP salvage; IEA:Ensembl.
DR GO; GO:0046070; P:dGTP metabolic process; IDA:MGI.
DR GO; GO:0106385; P:dIMP salvage; TAS:MGI.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; ISO:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0046122; P:purine deoxyribonucleoside metabolic process; ISO:MGI.
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 Alternative splicing; ATP-binding; Cytoplasm; Kinase; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..277
FT /note="Deoxyguanosine kinase, mitochondrial"
FT /id="PRO_0000016841"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 45..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q16854"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16854"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16854"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16854"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16854"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16854"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 206..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q16854"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16854"
FT BINDING 254..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305|PubMed:10455141"
FT /id="VSP_003027"
FT CONFLICT 22..23
FT /note="AL -> CF (in Ref. 2; AAF14342)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="E -> A (in Ref. 1; CAB43121/CAB43122)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 32281 MW; 021C3B3335510279 CRC64;
MAAGRFLLRR LRASFRSPLR NALVDAPHAR AMHDGGGPRR LCIEGNIAVG KSTFVKLLMK
THPEWQVATE PIAEWQNIQA AGAQKDGTSK RLGNLLEMMY QEPARWSYTF QTLSFMSRLK
VQLEPIPGRL LQAEKSVRVF ERSVYSDRYI FAKNLFENGS LSDIEWHIYQ DWHSFLLQEF
ANRLLLHGFI YLQASPQVCM ERLYQRDREE EKGIELAYLQ QLHSQHEDWF INKTTKLHFE
ALQHVPVLVL DVTEDFSENA ARQEELMGQV NTFMRNL
