NT5M_MOUSE
ID NT5M_MOUSE Reviewed; 220 AA.
AC Q8VCE6;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=5'(3')-deoxyribonucleotidase, mitochondrial;
DE Short=5',3'-nucleotidase, mitochondrial;
DE EC=3.1.3.-;
DE AltName: Full=Deoxy-5'-nucleotidase 2;
DE Short=dNT-2;
DE Flags: Precursor;
GN Name=Nt5m; Synonyms=Dnt2;
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], AND FUNCTION.
RC TISSUE=Diaphragm;
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 [2]
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Dephosphorylates specifically the 5' and 2'(3')-phosphates of
CC uracil and thymine deoxyribonucleotides, and so protects mitochondrial
CC DNA replication from excess dTTP. Has only marginal activity towards
CC dIMP and dGMP. {ECO:0000269|PubMed:12234672}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC {ECO:0000305}.
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DR EMBL; AY061970; AAL35749.1; -; mRNA.
DR EMBL; BK000190; DAA00068.1; -; mRNA.
DR EMBL; BC020084; AAH20084.1; -; mRNA.
DR CCDS; CCDS24779.1; -.
DR RefSeq; NP_598790.1; NM_134029.2.
DR AlphaFoldDB; Q8VCE6; -.
DR SMR; Q8VCE6; -.
DR STRING; 10090.ENSMUSP00000099756; -.
DR PhosphoSitePlus; Q8VCE6; -.
DR EPD; Q8VCE6; -.
DR MaxQB; Q8VCE6; -.
DR PaxDb; Q8VCE6; -.
DR PeptideAtlas; Q8VCE6; -.
DR PRIDE; Q8VCE6; -.
DR ProteomicsDB; 253030; -.
DR Antibodypedia; 25442; 94 antibodies from 20 providers.
DR DNASU; 103850; -.
DR Ensembl; ENSMUST00000102695; ENSMUSP00000099756; ENSMUSG00000032615.
DR GeneID; 103850; -.
DR KEGG; mmu:103850; -.
DR UCSC; uc007jfb.1; mouse.
DR CTD; 56953; -.
DR MGI; MGI:1917127; Nt5m.
DR VEuPathDB; HostDB:ENSMUSG00000032615; -.
DR eggNOG; ENOG502QPWJ; Eukaryota.
DR GeneTree; ENSGT00390000011596; -.
DR HOGENOM; CLU_100259_0_0_1; -.
DR InParanoid; Q8VCE6; -.
DR OMA; YAWIEKH; -.
DR OrthoDB; 1316201at2759; -.
DR PhylomeDB; Q8VCE6; -.
DR TreeFam; TF331117; -.
DR Reactome; R-MMU-73621; Pyrimidine catabolism.
DR SABIO-RK; Q8VCE6; -.
DR BioGRID-ORCS; 103850; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Nt5m; mouse.
DR PRO; PR:Q8VCE6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VCE6; protein.
DR Bgee; ENSMUSG00000032615; Expressed in spermatocyte and 254 other tissues.
DR Genevisible; Q8VCE6; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0046079; P:dUMP catabolic process; IDA:MGI.
DR GO; GO:0009223; P:pyrimidine deoxyribonucleotide catabolic process; IBA:GO_Central.
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 Hydrolase; Magnesium; Metal-binding; Mitochondrion; Nucleotide metabolism;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 24..220
FT /note="5'(3')-deoxyribonucleotidase, mitochondrial"
FT /id="PRO_0000000012"
FT ACT_SITE 33
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 35
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 220 AA; 25602 MW; 4EB6627803AD9993 CRC64;
MHRLRGCCAR PRGAPLRAER SRASSRALRV LVDMDGVLAD FEGGFLRKFR ARFPDLPFVA
LEDRRGFWVS EQYGRLQPGL SEKAISIWES KDFFFELEPL PGAVEAVKQM ANLQNTDVFI
CTSPIKMFKY CPYEKYAWVE KHFGPDFLEQ IVLTRDKTVI SADLLIDDRP DITGAEPHPS
WEHILFTSCH NYHLQLQPPR RRLHSWADDW KAILDSKRLR
