NT5C_MOUSE
ID NT5C_MOUSE Reviewed; 200 AA.
AC Q9JM14;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=5'(3')-deoxyribonucleotidase, cytosolic type;
DE EC=3.1.3.- {ECO:0000269|PubMed:10681516};
DE AltName: Full=Cytosolic 5',3'-pyrimidine nucleotidase;
DE AltName: Full=Deoxy-5'-nucleotidase 1;
DE Short=dNT-1;
GN Name=Nt5c; Synonyms=Dnt1;
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], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J;
RX PubMed=10681516; DOI=10.1074/jbc.275.8.5409;
RA Rampazzo C., Johansson M., Gallinaro L., Ferraro P., Hellman U.,
RA Karlsson A., Reichard P., Bianchi V.;
RT "Mammalian 5'(3')-deoxyribonucleotidase, cDNA cloning, and overexpression
RT of the enzyme in Escherichia coli and mammalian cells.";
RL J. Biol. Chem. 275:5409-5415(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP GENE STRUCTURE.
RX PubMed=12234672; DOI=10.1016/s0378-1119(02)00651-0;
RA Rampazzo C., Kost-Alimova M., Ruzzenente B., Dumanski J.P., Bianchi V.;
RT "Mouse cytosolic and mitochondrial deoxyribonucleotidases: cDNA cloning of
RT the mitochondrial enzyme, gene structures, chromosomal mapping and
RT comparison with the human orthologs.";
RL Gene 294:109-117(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-102 AND SER-184, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM IONS;
RP 2'-DEOXYURIDINE 5'-MONOPHOSPHATE AND 2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE,
RP COFACTOR, AND SUBUNIT.
RX PubMed=17985935; DOI=10.1021/bi7014794;
RA Wallden K., Rinaldo-Matthis A., Ruzzenente B., Rampazzo C., Bianchi V.,
RA Nordlund P.;
RT "Crystal structures of human and murine deoxyribonucleotidases: insights
RT into recognition of substrates and nucleotide analogues.";
RL Biochemistry 46:13809-13818(2007).
CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of
CC deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate
CC activity towards dGMP, and low activity towards dCMP and dAMP.
CC {ECO:0000269|PubMed:10681516}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17985935};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.42 mM for dUMP-5' {ECO:0000269|PubMed:10681516};
CC KM=1.25 mM for dTMP-5' {ECO:0000269|PubMed:10681516};
CC KM=1.2 mM for dGMP-5' {ECO:0000269|PubMed:10681516};
CC KM=1.0 mM for dAMP-5' {ECO:0000269|PubMed:10681516};
CC KM=3.6 mM for dCMP-5' {ECO:0000269|PubMed:10681516};
CC KM=0.4 mM for UMP-3 {ECO:0000269|PubMed:10681516};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17985935}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10681516}.
CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF078840; AAF36421.1; -; mRNA.
DR EMBL; AK007418; BAB25027.1; -; mRNA.
DR EMBL; BC024368; AAH24368.1; -; mRNA.
DR EMBL; BK000208; DAA00069.1; -; Genomic_DNA.
DR CCDS; CCDS25637.1; -.
DR RefSeq; NP_056622.1; NM_015807.1.
DR PDB; 2JAO; X-ray; 2.00 A; A=1-200.
DR PDB; 2JAR; X-ray; 1.94 A; A=1-200.
DR PDBsum; 2JAO; -.
DR PDBsum; 2JAR; -.
DR AlphaFoldDB; Q9JM14; -.
DR SMR; Q9JM14; -.
DR BioGRID; 206105; 1.
DR STRING; 10090.ENSMUSP00000021082; -.
DR iPTMnet; Q9JM14; -.
DR PhosphoSitePlus; Q9JM14; -.
DR REPRODUCTION-2DPAGE; IPI00124639; -.
DR EPD; Q9JM14; -.
DR jPOST; Q9JM14; -.
DR MaxQB; Q9JM14; -.
DR PaxDb; Q9JM14; -.
DR PeptideAtlas; Q9JM14; -.
DR PRIDE; Q9JM14; -.
DR ProteomicsDB; 252862; -.
DR Antibodypedia; 19500; 78 antibodies from 18 providers.
DR DNASU; 50773; -.
DR Ensembl; ENSMUST00000021082; ENSMUSP00000021082; ENSMUSG00000020736.
DR GeneID; 50773; -.
DR KEGG; mmu:50773; -.
DR UCSC; uc007mhu.1; mouse.
DR CTD; 30833; -.
DR MGI; MGI:1354954; Nt5c.
DR VEuPathDB; HostDB:ENSMUSG00000020736; -.
DR eggNOG; ENOG502QZUW; Eukaryota.
DR GeneTree; ENSGT00390000011596; -.
DR HOGENOM; CLU_100259_0_0_1; -.
DR InParanoid; Q9JM14; -.
DR OMA; GPKFVER; -.
DR OrthoDB; 1316201at2759; -.
DR PhylomeDB; Q9JM14; -.
DR TreeFam; TF331117; -.
DR BRENDA; 3.1.3.34; 3474.
DR Reactome; R-MMU-73621; Pyrimidine catabolism.
DR Reactome; R-MMU-74259; Purine catabolism.
DR SABIO-RK; Q9JM14; -.
DR BioGRID-ORCS; 50773; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Nt5c; mouse.
DR EvolutionaryTrace; Q9JM14; -.
DR PRO; PR:Q9JM14; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JM14; protein.
DR Bgee; ENSMUSG00000020736; Expressed in dorsal pancreas and 249 other tissues.
DR ExpressionAtlas; Q9JM14; baseline and differential.
DR Genevisible; Q9JM14; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0050483; F:IMP 5'-nucleotidase activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008252; F:nucleotidase activity; ISO:MGI.
DR GO; GO:0016791; F:phosphatase activity; IDA:MGI.
DR GO; GO:0019103; F:pyrimidine nucleotide binding; ISO:MGI.
DR GO; GO:0000255; P:allantoin metabolic process; IDA:MGI.
DR GO; GO:0006249; P:dCMP catabolic process; IDA:MGI.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IDA:MGI.
DR GO; GO:0016311; P:dephosphorylation; ISO:MGI.
DR GO; GO:0046055; P:dGMP catabolic process; IDA:MGI.
DR GO; GO:0046074; P:dTMP catabolic process; IDA:MGI.
DR GO; GO:0046079; P:dUMP catabolic process; IDA:MGI.
DR GO; GO:0006204; P:IMP catabolic process; IDA:MGI.
DR GO; GO:0009223; P:pyrimidine deoxyribonucleotide catabolic process; ISO:MGI.
DR GO; GO:0046050; P:UMP catabolic process; IDA:MGI.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR010708; 5'(3')-deoxyribonucleotidase.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF06941; NT5C; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..200
FT /note="5'(3')-deoxyribonucleotidase, cytosolic type"
FT /id="PRO_0000164372"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 14
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 20
FT /ligand="substrate"
FT BINDING 46
FT /ligand="substrate"
FT BINDING 67
FT /ligand="substrate"
FT BINDING 101
FT /ligand="substrate"
FT BINDING 136
FT /ligand="substrate"
FT BINDING 147
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:2JAR"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:2JAR"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:2JAR"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2JAR"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:2JAR"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:2JAR"
FT TURN 70..75
FT /evidence="ECO:0007829|PDB:2JAR"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:2JAR"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:2JAR"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:2JAR"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:2JAR"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:2JAR"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2JAR"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2JAR"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:2JAR"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:2JAR"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:2JAR"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:2JAR"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:2JAR"
SQ SEQUENCE 200 AA; 23076 MW; 5E5A3AFB0A214082 CRC64;
MAVKRPVRVL VDMDGVLADF ESGLLQGFRR RFPEEPHVPL EQRRGFLANE QYGALRPDLA
EKVASVYESP GFFLNLEPIP GALDALREMN DMKDTEVFIC TTPLLKYDHC VGEKYRWVEQ
NLGPEFVERI ILTRDKTVVM GDLLIDDKDN IQGLEETPSW EHILFTCCHN QHLALPPTRR
RLLSWSDNWR GIIESKRASL
