ID NT5C_HUMAN Reviewed; 201 AA. AC Q8TCD5; Q96HS6; Q9NP82; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2003, sequence version 2. DT 02-SEP-2026, entry version 185. DE RecName: Full=5'(3')-deoxyribonucleotidase, cytosolic type; DE EC=3.1.3.- {ECO:0000269|Ref.12}; DE AltName: Full=Cytosolic 5',3'-pyrimidine nucleotidase; DE AltName: Full=Deoxy-5'-nucleotidase 1; DE Short=dNT-1; GN Name=NT5C; Synonyms=DNT1, UMPH2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 52-66; 99-112; RP 114-121 AND 125-146, AND TISSUE SPECIFICITY. 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] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP LEU-68. RC TISSUE=Brain, Eye, and Lung; 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 [5] 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 3-195 IN COMPLEX WITH MAGNESIUM RP IONS AND THE SUBSTRATE ANALOG DEOXYURIDINE TETRAFLUOROALUMINATE, CATALYTIC RP ACTIVITY, 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). RN [11] {ECO:0007744|PDB:4L57} RP X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF 1-195 IN COMPLEX WITH MG(2+). RX PubMed=24531480; DOI=10.1107/s1399004713030502; RA Pachl P., Fabry M., Rosenberg I., Simak O., Rezacova P., Brynda J.; RT "Structures of human cytosolic and mitochondrial nucleotidases: RT implications for structure-based design of selective inhibitors."; RL Acta Crystallogr. D 70:461-470(2014). RN [12] {ECO:0007744|PDB:4YIH} RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 1-195 IN COMPLEX WITH MG(2+), RP FUNCTION, AND CATALYTIC ACTIVITY. RX DOI=10.1039/C5MD00235D; RA Pachl P., Simak O., Rezacova P., Fabry M., Budesinsky M., Rosenberg I., RA Brynda J.; RT "Structure-based design of a bisphosphonate 5'(3')-deoxyribonucleotidase RT inhibitor."; RL Med. Chem. Commun. 6:1635-1638(2015). CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of CC deoxyribonucleotides, with a preference for dUMP (Ref.12). Also CC dephosphsphorylates dTMP, exhibits intermediate activity towards dGMP, CC and low activity towards dCMP and dAMP (By similarity). CC {ECO:0000250|UniProtKB:Q9JM14, ECO:0000269|Ref.12}. CC -!- CATALYTIC ACTIVITY: CC Reaction=dTMP + H2O = thymidine + phosphate; Xref=Rhea:RHEA:11080, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17748, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:63528; Evidence={ECO:0000250|UniProtKB:Q9JM14}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dUMP + H2O = 2'-deoxyuridine + phosphate; CC Xref=Rhea:RHEA:29355, ChEBI:CHEBI:15377, ChEBI:CHEBI:16450, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:246422; Evidence={ECO:0000269|Ref.12}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dAMP + H2O = 2'-deoxyadenosine + phosphate; CC Xref=Rhea:RHEA:29371, ChEBI:CHEBI:15377, ChEBI:CHEBI:17256, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58245; CC Evidence={ECO:0000250|UniProtKB:Q9JM14}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dCMP + H2O = 2'-deoxycytidine + phosphate; CC Xref=Rhea:RHEA:29363, ChEBI:CHEBI:15377, ChEBI:CHEBI:15698, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57566; CC Evidence={ECO:0000250|UniProtKB:Q9JM14}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dGMP + H2O = 2'-deoxyguanosine + phosphate; CC Xref=Rhea:RHEA:29379, ChEBI:CHEBI:15377, ChEBI:CHEBI:17172, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57673; CC Evidence={ECO:0000250|UniProtKB:Q9JM14}; CC -!- CATALYTIC ACTIVITY: CC Reaction=UMP + H2O = uridine + phosphate; Xref=Rhea:RHEA:29359, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16704, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57865; Evidence={ECO:0000250|UniProtKB:Q9JM14}; CC -!- CATALYTIC ACTIVITY: CC Reaction=thymidine 3'-phosphate + H2O = thymidine + phosphate; CC Xref=Rhea:RHEA:37247, ChEBI:CHEBI:15377, ChEBI:CHEBI:17748, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:77843; CC Evidence={ECO:0000250|UniProtKB:Q9JM14}; CC -!- CATALYTIC ACTIVITY: CC Reaction=uridine 2'-phosphate + H2O = uridine + phosphate; CC Xref=Rhea:RHEA:37355, ChEBI:CHEBI:15377, ChEBI:CHEBI:16704, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:77802; CC Evidence={ECO:0000250|UniProtKB:Q9JM14}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-UMP + H2O = uridine + phosphate; Xref=Rhea:RHEA:27890, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16704, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:60784; Evidence={ECO:0000250|UniProtKB:Q9JM14}; CC -!- CATALYTIC ACTIVITY: CC Reaction=IMP + H2O = inosine + phosphate; Xref=Rhea:RHEA:27718, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58053; Evidence={ECO:0000250|UniProtKB:Q9JM14}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:17985935}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17985935}. CC -!- INTERACTION: CC Q8TCD5; Q8TCD5: NT5C; NbExp=6; IntAct=EBI-6137412, EBI-6137412; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JM14}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8TCD5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8TCD5-2; Sequence=VSP_008710, VSP_008711, VSP_008712; CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle, heart and pancreas. CC {ECO:0000269|PubMed:10681516}. CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. 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; AF154829; AAF36534.2; -; mRNA. DR EMBL; AK000419; BAA91151.1; -; mRNA. DR EMBL; AC022211; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008183; AAH08183.1; -; mRNA. DR EMBL; BC017454; AAH17454.1; -; mRNA. DR EMBL; BC022334; AAH22334.1; -; mRNA. DR EMBL; BK000192; DAA00070.1; -; Genomic_DNA. DR CCDS; CCDS11715.1; -. [Q8TCD5-1] DR RefSeq; NP_001239306.1; NM_001252377.2. DR RefSeq; NP_055410.1; NM_014595.3. [Q8TCD5-1] DR PDB; 2I7D; X-ray; 1.20 A; A/B=3-195. DR PDB; 4L57; X-ray; 1.08 A; A/B=1-195. DR PDB; 4YIH; X-ray; 1.82 A; A/B=1-195. DR PDB; 6G2N; X-ray; 1.40 A; A/B=2-201. DR AlphaFoldDB; Q8TCD5; -. DR BMRB; Q8TCD5; -. DR SMR; Q8TCD5; -. DR BioGRID; 119049; 62. DR FunCoup; Q8TCD5; 1005. DR IntAct; Q8TCD5; 38. DR NDEx; IQUERY-CP-NT5C; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000245552; -. DR ChEMBL; CHEMBL3751653; -. DR DrugBank; DB00709; Lamivudine. DR DEPOD; NT5C; -. DR iPTMnet; Q8TCD5; -. DR PhosphoSitePlus; Q8TCD5; -. DR BioMuta; NT5C; -. DR DMDM; 38258193; -. DR OGP; Q8TCD5; -. DR jPOST; Q8TCD5; -. DR MassIVE; Q8TCD5; -. DR PaxDb; 9606-ENSP00000245552; -. DR PeptideAtlas; Q8TCD5; -. DR ProteomicsDB; 74121; -. [Q8TCD5-1] DR ProteomicsDB; 74122; -. [Q8TCD5-2] DR Pumba; Q8TCD5; -. DR Antibodypedia; 19500; 75 antibodies from 19 providers. DR DNASU; 30833; -. DR Ensembl; ENST00000245552.7; ENSP00000245552.2; ENSG00000125458.8. [Q8TCD5-1] DR Ensembl; ENST00000580758.5; ENSP00000462123.1; ENSG00000125458.8. [Q8TCD5-2] DR GeneID; 30833; -. DR KEGG; hsa:30833; -. DR MANE-Select; ENST00000245552.7; ENSP00000245552.2; NM_014595.3; NP_055410.1. DR UCSC; uc060jte.1; human. [Q8TCD5-1] DR AGR; HGNC:17144; -. DR ClinPGx; PA31798; -. DR CTD; 30833; -. DR DisGeNET; 30833; -. DR GeneCards; NT5C; -. DR HGNC; HGNC:17144; NT5C. DR HPA; ENSG00000125458; Low tissue specificity. DR MIM; 191720; gene. DR OpenTargets; ENSG00000125458; -. DR VEuPathDB; HostDB:ENSG00000125458; -. DR eggNOG; ENOG502QZUW; Eukaryota. DR GeneTree; ENSGT00390000011596; -. DR HOGENOM; CLU_2095990_0_0_1; -. DR InParanoid; Q8TCD5; -. DR OMA; MLHMQDT; -. DR OrthoDB; 10248475at2759; -. DR PAN-GO; Q8TCD5; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q8TCD5; -. DR PathwayCommons; Q8TCD5; -. DR Reactome; R-HSA-73621; Pyrimidine catabolism. DR Reactome; R-HSA-74259; Purine catabolism. DR SABIO-RK; Q8TCD5; -. DR SignaLink; Q8TCD5; -. DR Agora; ENSG00000125458; -. DR BioGRID-ORCS; 30833; 28 hits in 1175 CRISPR screens. DR ChiTaRS; NT5C; human. DR EvolutionaryTrace; Q8TCD5; -. DR GeneWiki; NT5C; -. DR GenomeRNAi; 30833; -. DR Pharos; Q8TCD5; Tbio. DR PRO; PR:Q8TCD5; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q8TCD5; protein. DR Bgee; ENSG00000125458; Expressed in mucosa of transverse colon and 149 other cell types or tissues. DR ExpressionAtlas; Q8TCD5; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; HTP:FlyBase. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0008254; F:3'-nucleotidase activity; ISS:UniProtKB. DR GO; GO:0002953; F:5'-deoxynucleotidase activity; IEA:RHEA. DR GO; GO:0008253; F:5'-nucleotidase activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008252; F:nucleotidase activity; IDA:UniProtKB. DR GO; GO:0019103; F:pyrimidine nucleotide binding; IDA:UniProtKB. DR GO; GO:0046059; P:dAMP catabolic process; ISS:UniProtKB. DR GO; GO:0006249; P:dCMP catabolic process; ISS:UniProtKB. DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro. DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB. DR GO; GO:0046055; P:dGMP catabolic process; IEA:Ensembl. DR GO; GO:0046074; P:dTMP catabolic process; ISS:UniProtKB. DR GO; GO:0046079; P:dUMP catabolic process; IEA:Ensembl. DR GO; GO:0046038; P:GMP catabolic process; ISS:UniProtKB. DR GO; GO:0006204; P:IMP catabolic process; ISS:UniProtKB. DR GO; GO:0009223; P:pyrimidine deoxyribonucleotide catabolic process; IDA:UniProtKB. DR GO; GO:0046045; P:TMP catabolic process; ISS:UniProtKB. DR GO; GO:0046050; P:UMP catabolic process; ISS:UniProtKB. DR CDD; cd02587; HAD_5-3dNT; 1. DR FunFam; 1.10.40.40:FF:000001; 5'(3')-deoxyribonucleotidase, cytosolic type; 1. DR FunFam; 3.40.50.1000:FF:000133; 5'(3')-deoxyribonucleotidase, cytosolic type; 1. DR Gene3D; 1.10.40.40; Deoxyribonucleotidase, domain 2; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR InterPro; IPR010708; 5'(3')-deoxyribonucleotidase. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR PANTHER; PTHR16504; 5'(3')-DEOXYRIBONUCLEOTIDASE; 1. DR PANTHER; PTHR16504:SF5; 5'(3')-DEOXYRIBONUCLEOTIDASE, CYTOSOLIC TYPE; 1. DR Pfam; PF06941; NT5C; 1. DR SFLD; SFLDG01145; C1.2.1; 1. DR SFLD; SFLDG01126; C1.2:_Nucleotidase_Like; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR PDBsum; 2I7D; -. DR PDBsum; 4L57; -. DR PDBsum; 4YIH; -. DR PDBsum; 6G2N; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing; KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism; KW Nucleotide-binding; Phosphoprotein; Proteomics identification; KW Reference proteome. FT CHAIN 1..201 FT /note="5'(3')-deoxyribonucleotidase, cytosolic type" FT /id="PRO_0000164371" FT ACT_SITE 10 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q9JM14" FT ACT_SITE 12 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q9JM14" FT BINDING 10 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:24531480, FT ECO:0007744|PDB:4L57" FT BINDING 12 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:24531480, FT ECO:0007744|PDB:4L57" FT BINDING 46 FT /ligand="dGMP" FT /ligand_id="ChEBI:CHEBI:57673" FT /evidence="ECO:0000250|UniProtKB:Q9JM14" FT BINDING 46 FT /ligand="dUMP" FT /ligand_id="ChEBI:CHEBI:246422" FT /evidence="ECO:0000250|UniProtKB:Q9JM14" FT BINDING 65 FT /ligand="dUMP" FT /ligand_id="ChEBI:CHEBI:246422" FT /evidence="ECO:0000250|UniProtKB:Q9JM14" FT BINDING 100 FT /ligand="dGMP" FT /ligand_id="ChEBI:CHEBI:57673" FT /evidence="ECO:0000250|UniProtKB:Q9JM14" FT BINDING 100 FT /ligand="dUMP" FT /ligand_id="ChEBI:CHEBI:246422" FT /evidence="ECO:0000250|UniProtKB:Q9JM14" FT BINDING 134 FT /ligand="dGMP" FT /ligand_id="ChEBI:CHEBI:57673" FT /evidence="ECO:0000250|UniProtKB:Q9JM14" FT BINDING 134 FT /ligand="dUMP" FT /ligand_id="ChEBI:CHEBI:246422" FT /evidence="ECO:0000250|UniProtKB:Q9JM14" FT BINDING 145 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:24531480, FT ECO:0007744|PDB:4L57" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT VAR_SEQ 93..100 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_008710" FT VAR_SEQ 113..125 FT /note="YRWVEQHLGPQFV -> VWLPRPYSARGAA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_008711" FT VAR_SEQ 126..201 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_008712" FT VARIANT 68 FT /note="P -> L (in dbSNP:rs11541956)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_048102" FT STRAND 5..9 FT /evidence="ECO:0007829|PDB:4L57" FT TURN 13..15 FT /evidence="ECO:0007829|PDB:4L57" FT HELIX 18..29 FT /evidence="ECO:0007829|PDB:4L57" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:4L57" FT HELIX 46..53 FT /evidence="ECO:0007829|PDB:4L57" FT HELIX 57..65 FT /evidence="ECO:0007829|PDB:4L57" FT TURN 68..73 FT /evidence="ECO:0007829|PDB:4L57" FT HELIX 80..89 FT /evidence="ECO:0007829|PDB:4L57" FT STRAND 93..99 FT /evidence="ECO:0007829|PDB:4L57" FT HELIX 100..102 FT /evidence="ECO:0007829|PDB:4L57" FT TURN 106..108 FT /evidence="ECO:0007829|PDB:4L57" FT HELIX 109..120 FT /evidence="ECO:0007829|PDB:4L57" FT HELIX 122..125 FT /evidence="ECO:0007829|PDB:4L57" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:4L57" FT HELIX 134..136 FT /evidence="ECO:0007829|PDB:4L57" FT STRAND 140..147 FT /evidence="ECO:0007829|PDB:4L57" FT STRAND 157..163 FT /evidence="ECO:0007829|PDB:4L57" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:4L57" FT STRAND 177..180 FT /evidence="ECO:0007829|PDB:6G2N" FT HELIX 187..192 FT /evidence="ECO:0007829|PDB:4L57" SQ SEQUENCE 201 AA; 23383 MW; C4C289BBDEC0FA89 CRC64; MARSVRVLVD MDGVLADFEA GLLRGFRRRF PEEPHVPLEQ RRGFLAREQY RALRPDLADK VASVYEAPGF FLDLEPIPGA LDAVREMNDL PDTQVFICTS PLLKYHHCVG EKYRWVEQHL GPQFVERIIL TRDKTVVLGD LLIDDKDTVR GQEETPSWEH ILFTCCHNRH LVLPPTRRRL LSWSDNWREI LDSKRGAAQR E //