ID TDT_MOUSE Reviewed; 510 AA. AC P09838; Q99PD0; Q99PD1; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 05-DEC-2018, sequence version 4. DT 24-JAN-2024, entry version 209. DE RecName: Full=DNA nucleotidylexotransferase; DE EC=2.7.7.31 {ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:23856622, ECO:0000269|PubMed:23968551}; DE EC=3.1.11.- {ECO:0000269|PubMed:11938351}; DE AltName: Full=Terminal addition enzyme; DE AltName: Full=Terminal deoxynucleotidyltransferase {ECO:0000303|PubMed:3755527}; DE Short=TDT; DE Short=Terminal transferase; GN Name=Dntt; Synonyms=Tdt; 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] (ISOFORM TDT-L). RC TISSUE=Lymphoma; RX PubMed=3755527; DOI=10.1093/nar/14.14.5777; RA Koiwai O., Yokota T., Kageyama T., Hirose T., Yoshida S., Arai K.; RT "Isolation and characterization of bovine and mouse terminal RT deoxynucleotidyltransferase cDNAs expressible in mammalian cells."; RL Nucleic Acids Res. 14:5777-5792(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TDT-S), FUNCTION, ALTERNATIVE SPLICING, RP AND TISSUE SPECIFICITY. RC STRAIN=BALB/cJ; TISSUE=Thymus; RX PubMed=8464703; DOI=10.1093/nar/21.5.1187; RA Doyen N., Fanton D'Andon M., Bentolila L.A., Nguyen T.Q., Rougeon F.; RT "Differential splicing in mouse thymus generates two forms of terminal RT deoxynucleotidyl transferase."; RL Nucleic Acids Res. 21:1187-1191(1993). RN [3] RP SEQUENCE REVISION TO 443-445. RA Doyen N.; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TDT-L AND TDT-S), FUNCTION, AND TISSUE RP SPECIFICITY. RC STRAIN=C57BL/6J; TISSUE=Thymus; RX PubMed=11136823; DOI=10.1084/jem.193.1.89; RA Benedict C.L., Gilfillan S., Kearney J.F.; RT "The long isoform of terminal deoxynucleotidyl transferase (TdtL) enters RT the nucleus and, rather than catalyzing N addition, modulates the catalytic RT activity of the short isoform."; RL J. Exp. Med. 193:89-99(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TDT-L). RC STRAIN=NOD; TISSUE=Thymus; 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 [6] RP PROTEIN SEQUENCE OF 388-393, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [7] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ALTERNATIVE RP SPLICING. RX PubMed=7556063; DOI=10.1002/j.1460-2075.1995.tb00096.x; RA Bentolila L.A., Fanton D'Andon M., Nguyen T.Q., Martinez O., Rougeon F., RA Doyen N.; RT "The two isoforms of mouse terminal deoxynucleotidyl transferase differ in RT both the ability to add N regions and subcellular localization."; RL EMBO J. 14:4221-4229(1995). RN [8] RP FUNCTION, ALTERNATIVE SPLICING, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10878023; DOI=10.1074/jbc.m005544200; RA Boule J.-B., Rougeon F., Papanicolaou C.; RT "Comparison of the two murine terminal deoxynucleotidyltransferase RT isoforms. A 20-amino acid insertion in the highly conserved carboxyl- RT terminal region modifies the thermosensitivity but not the catalytic RT activity."; RL J. Biol. Chem. 275:28984-28988(2000). RN [9] RP ERRATUM OF PUBMED:10878023. RX PubMed=11032847; RA Boule J.-B., Rougeon F., Papanicolaou C.; RL J. Biol. Chem. 275:33184-33184(2000). RN [10] RP FUNCTION, TISSUE SPECIFICITY, CHARACTERIZATION OF ISOFORMS TDT-L AND TDT-S, RP AND MUTAGENESIS OF ASP-29; ASP-170 AND ASP-473. RX PubMed=11938351; DOI=10.1038/ni788; RA Thai T.H., Purugganan M.M., Roth D.B., Kearney J.F.; RT "Distinct and opposite diversifying activities of terminal transferase RT splice variants."; RL Nat. Immunol. 3:457-462(2002). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Lung; 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 [12] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 130-510 (ISOFORM TDT-S) IN RP COMPLEXES WITH MAGNESIUM; COBALT AND ATP ANALOG. RX PubMed=11823435; DOI=10.1093/emboj/21.3.427; RA Delarue M., Boule J.-B., Lescar J., Expert-Bezancon N., Jourdan N., RA Sukumar N., Rougeon F., Papanicolaou C.; RT "Crystal structures of a template-independent DNA polymerase: murine RT terminal deoxynucleotidyltransferase."; RL EMBO J. 21:427-439(2002). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 132-510 (ISOFORM TDT-S) IN RP COMPLEXES WITH SYNTHETIC INHIBITORS AND NUCLEOTIDE, AND CATALYTIC ACTIVITY. RX PubMed=23968551; DOI=10.1021/jm4010187; RA Costi R., Crucitti G.C., Pescatori L., Messore A., Scipione L., RA Tortorella S., Amoroso A., Crespan E., Campiglia P., Maresca B., Porta A., RA Granata I., Novellino E., Gouge J., Delarue M., Maga G., Di Santo R.; RT "New nucleotide-competitive non-nucleoside inhibitors of terminal RT deoxynucleotidyl transferase: discovery, characterization, and crystal RT structure in complex with the target."; RL J. Med. Chem. 56:7431-7441(2013). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 132-510 (ISOFORM TDT-S) IN RP COMPLEXES WITH ATP; CTP; TTP; NUCLEOTIDE; MAGNESIUM; MANGANESE AND ZINC, RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF HIS-342; RP LEU-398; ASP-399; HIS-400; LYS-403; ASP-473 AND HIS-475. RX PubMed=23856622; DOI=10.1016/j.jmb.2013.07.009; RA Gouge J., Rosario S., Romain F., Beguin P., Delarue M.; RT "Structures of intermediates along the catalytic cycle of terminal RT deoxynucleotidyltransferase: dynamical aspects of the two-metal ion RT mechanism."; RL J. Mol. Biol. 425:4334-4352(2013). CC -!- FUNCTION: [Isoform TDT-S]: Transferase that catalyzes the nontemplated CC addition of nucleoside triphosphate to coding ends during V(D)J CC recombination (N addition). Involved in the generation of diversity in CC the antigen-binding region of immunoglobulin heavy and light chains and CC T-cell receptors during B- and T-cell development. Does not act on CC double-stranded DNA with blunt ends. {ECO:0000269|PubMed:11136823, CC ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:23856622, CC ECO:0000269|PubMed:7556063, ECO:0000269|PubMed:8464703}. CC -!- FUNCTION: [Isoform TDT-L]: 3'-to-5' DNA exonuclease. Involved in the CC generation of diversity in the antigen-binding region of immunoglobulin CC heavy and light chains and T-cell receptors during B- and T-cell CC development. Acts on single-stranded and double-stranded DNA with 3' or CC 5' extensions, but not on double-stranded DNA with blunt ends. CC Attenuates not only isoform TDT-S-catalyzed N addition, but also P CC (palindromic) addition in coding joins (PubMed:11938351). Lacks CC terminal transferase activity (PubMed:11136823, PubMed:7556063). CC {ECO:0000269|PubMed:11136823, ECO:0000269|PubMed:11938351, CC ECO:0000269|PubMed:7556063}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, CC ChEBI:CHEBI:173112; EC=2.7.7.31; CC Evidence={ECO:0000269|PubMed:23856622, ECO:0000269|PubMed:23968551}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:23856622}; CC Note=Can also utilize other divalent cations, such as Mn(2+) and Co(2+) CC (in vitro). {ECO:0000269|PubMed:23856622, ECO:0000305}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=300 uM for dATP (at 35 degrees Celsius) CC {ECO:0000269|PubMed:10878023}; CC Note=In assays with isoform TDT-S. {ECO:0000269|PubMed:10878023}; CC -!- SUBUNIT: Interacts with PRP19 and DNTTIP1. Forms a ternary complex with CC DNTTIP2 and core histone. Released from this complex by PCNA. Interacts CC with TRERF1. {ECO:0000250|UniProtKB:P04053}. CC -!- SUBCELLULAR LOCATION: [Isoform TDT-S]: Nucleus CC {ECO:0000269|PubMed:7556063}. CC -!- SUBCELLULAR LOCATION: [Isoform TDT-L]: Nucleus CC {ECO:0000269|PubMed:11136823}. Cytoplasm {ECO:0000269|PubMed:7556063}. CC Note=The subcellular location is controversial. Detected in the nucleus CC (PubMed:11136823). Found mainly in the cytoplasm (PubMed:7556063). CC {ECO:0000269|PubMed:11136823, ECO:0000269|PubMed:7556063}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=TDT-S; Synonyms=TDT-Small, TdtS {ECO:0000303|PubMed:8464703}; CC IsoId=P09838-2; Sequence=Displayed; CC Name=TDT-L; Synonyms=TDT-Large, TdtL {ECO:0000303|PubMed:8464703}; CC IsoId=P09838-1; Sequence=VSP_059967; CC -!- TISSUE SPECIFICITY: Isoform TDT-L: Expressed in the thymus, and, at CC lower levels, in the bone marrow (PubMed:8464703, PubMed:11136823, CC PubMed:7556063). Detected in both cycling and noncycling pro-B and pre- CC B cells (at protein level) (PubMed:11938351). Isoform TDT-S: Expressed CC in both cycling and noncycling pro-B, but not pre-B, cells (at protein CC level) (PubMed:11938351). Not detected in mature peripheral or germinal CC center B cells (PubMed:11938351). {ECO:0000269|PubMed:11136823, CC ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:7556063, CC ECO:0000269|PubMed:8464703}. CC -!- MISCELLANEOUS: [Isoform TDT-S]: Major form in the thymus and the bone CC marrow (PubMed:8464703, PubMed:11136823). Catalyzes the nontemplated CC addition of nucleoside triphosphate to coding ends during V(D)J CC recombination (PubMed:23856622). May have a longer half-life than CC isoform TDT-L (PubMed:7556063). {ECO:0000269|PubMed:11136823, CC ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:7556063, CC ECO:0000269|PubMed:8464703}. CC -!- MISCELLANEOUS: [Isoform TDT-L]: Exhibits 3'-to-5' DNA exonuclease CC activity (EC=3.1.11.-) (PubMed:23856622). May have a shorter half-life CC than isoform TDT-S (PubMed:7556063, PubMed:10878023). CC {ECO:0000269|PubMed:10878023, ECO:0000269|PubMed:11938351, CC ECO:0000269|PubMed:7556063}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {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; X04123; CAA27735.1; -; mRNA. DR EMBL; X68670; CAA48634.2; -; mRNA. DR EMBL; AF316014; AAK07884.1; -; mRNA. DR EMBL; AF316015; AAK07885.1; -; mRNA. DR EMBL; AK087978; BAC40071.1; -; mRNA. DR EMBL; AK088709; BAC40518.1; -; mRNA. DR CCDS; CCDS29807.1; -. [P09838-1] DR CCDS; CCDS37984.1; -. [P09838-2] DR PIR; B23595; B23595. DR RefSeq; NP_001036693.1; NM_001043228.1. [P09838-2] DR RefSeq; NP_033371.2; NM_009345.2. [P09838-1] DR PDB; 1JMS; X-ray; 2.36 A; A=130-510. DR PDB; 1KDH; X-ray; 3.00 A; A=148-510. DR PDB; 1KEJ; X-ray; 3.00 A; A=148-510. DR PDB; 4I27; X-ray; 2.60 A; A=132-510. DR PDB; 4I28; X-ray; 2.15 A; A=132-510. DR PDB; 4I29; X-ray; 2.20 A; A=132-510. DR PDB; 4I2A; X-ray; 1.90 A; A=132-510. DR PDB; 4I2B; X-ray; 2.20 A; A=132-510. DR PDB; 4I2C; X-ray; 2.10 A; A=132-510. DR PDB; 4I2D; X-ray; 2.30 A; A=132-510. DR PDB; 4I2E; X-ray; 2.00 A; A=132-510. DR PDB; 4I2F; X-ray; 2.10 A; A=132-510. DR PDB; 4I2G; X-ray; 2.50 A; A=132-510. DR PDB; 4I2H; X-ray; 2.75 A; A=132-510. DR PDB; 4I2I; X-ray; 2.50 A; A=132-510. DR PDB; 4I2J; X-ray; 2.70 A; A=132-510. DR PDB; 4IQT; X-ray; 2.60 A; A=132-510. DR PDB; 4IQU; X-ray; 2.40 A; A=132-510. DR PDB; 4IQV; X-ray; 2.90 A; A=132-510. DR PDB; 4IQW; X-ray; 2.60 A; A=132-510. DR PDB; 4QZ8; X-ray; 2.70 A; A=132-510. DR PDB; 4QZ9; X-ray; 2.05 A; A=132-510. DR PDB; 4QZA; X-ray; 2.15 A; A=132-510. DR PDB; 4QZB; X-ray; 2.15 A; A=132-510. DR PDB; 4QZC; X-ray; 2.75 A; A=132-510. DR PDB; 4QZD; X-ray; 2.70 A; A=132-510. DR PDB; 4QZE; X-ray; 2.25 A; A=132-510. DR PDB; 4QZF; X-ray; 2.60 A; A=132-510. DR PDB; 4QZG; X-ray; 2.75 A; A=132-510. DR PDB; 4QZH; X-ray; 2.60 A; A=132-510. DR PDB; 4QZI; X-ray; 2.65 A; A=132-510. DR PDB; 5D46; X-ray; 2.80 A; A=132-510. DR PDB; 5D49; X-ray; 1.99 A; A=132-510. DR PDB; 5D4B; X-ray; 2.66 A; A/B=132-510. DR PDB; 6GO3; X-ray; 2.20 A; A=132-377, A=409-510. DR PDB; 6GO4; X-ray; 1.96 A; A=132-377, A=409-510. DR PDB; 6GO5; X-ray; 2.35 A; A/B=132-377, A/B=409-510. DR PDB; 6GO6; X-ray; 2.09 A; A=132-377, A=409-510. DR PDB; 6GO7; X-ray; 2.55 A; A=132-377, A=409-510. DR PDBsum; 1JMS; -. DR PDBsum; 1KDH; -. DR PDBsum; 1KEJ; -. DR PDBsum; 4I27; -. DR PDBsum; 4I28; -. DR PDBsum; 4I29; -. DR PDBsum; 4I2A; -. DR PDBsum; 4I2B; -. DR PDBsum; 4I2C; -. DR PDBsum; 4I2D; -. DR PDBsum; 4I2E; -. DR PDBsum; 4I2F; -. DR PDBsum; 4I2G; -. DR PDBsum; 4I2H; -. DR PDBsum; 4I2I; -. DR PDBsum; 4I2J; -. DR PDBsum; 4IQT; -. DR PDBsum; 4IQU; -. DR PDBsum; 4IQV; -. DR PDBsum; 4IQW; -. DR PDBsum; 4QZ8; -. DR PDBsum; 4QZ9; -. DR PDBsum; 4QZA; -. DR PDBsum; 4QZB; -. DR PDBsum; 4QZC; -. DR PDBsum; 4QZD; -. DR PDBsum; 4QZE; -. DR PDBsum; 4QZF; -. DR PDBsum; 4QZG; -. DR PDBsum; 4QZH; -. DR PDBsum; 4QZI; -. DR PDBsum; 5D46; -. DR PDBsum; 5D49; -. DR PDBsum; 5D4B; -. DR PDBsum; 6GO3; -. DR PDBsum; 6GO4; -. DR PDBsum; 6GO5; -. DR PDBsum; 6GO6; -. DR PDBsum; 6GO7; -. DR AlphaFoldDB; P09838; -. DR SMR; P09838; -. DR BioGRID; 204095; 4. DR STRING; 10090.ENSMUSP00000062078; -. DR iPTMnet; P09838; -. DR PhosphoSitePlus; P09838; -. DR jPOST; P09838; -. DR MaxQB; P09838; -. DR PaxDb; 10090-ENSMUSP00000062078; -. DR ProteomicsDB; 263150; -. [P09838-2] DR ProteomicsDB; 263151; -. [P09838-2] DR Antibodypedia; 16924; 697 antibodies from 40 providers. DR DNASU; 21673; -. DR Ensembl; ENSMUST00000051806.12; ENSMUSP00000062078.5; ENSMUSG00000025014.14. [P09838-1] DR Ensembl; ENSMUST00000112200.3; ENSMUSP00000107819.2; ENSMUSG00000025014.14. [P09838-2] DR GeneID; 21673; -. DR KEGG; mmu:21673; -. DR UCSC; uc008hlo.1; mouse. [P09838-2] DR AGR; MGI:98659; -. DR CTD; 1791; -. DR MGI; MGI:98659; Dntt. DR VEuPathDB; HostDB:ENSMUSG00000025014; -. DR eggNOG; KOG2534; Eukaryota. DR GeneTree; ENSGT00940000158584; -. DR HOGENOM; CLU_008698_0_0_1; -. DR InParanoid; P09838; -. DR OMA; PKVINLW; -. DR OrthoDB; 3019669at2759; -. DR PhylomeDB; P09838; -. DR TreeFam; TF103012; -. DR BRENDA; 2.7.7.31; 3474. DR BioGRID-ORCS; 21673; 7 hits in 78 CRISPR screens. DR ChiTaRS; Dntt; mouse. DR EvolutionaryTrace; P09838; -. DR PRO; PR:P09838; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; P09838; Protein. DR Bgee; ENSMUSG00000025014; Expressed in thymus and 25 other cell types or tissues. DR ExpressionAtlas; P09838; baseline and differential. DR Genevisible; P09838; MM. DR GO; GO:0000785; C:chromatin; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0000791; C:euchromatin; ISO:MGI. DR GO; GO:0016363; C:nuclear matrix; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003912; F:DNA nucleotidylexotransferase activity; IDA:MGI. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006259; P:DNA metabolic process; IDA:MGI. DR GO; GO:0006304; P:DNA modification; IEA:UniProtKB-KW. DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central. DR GO; GO:0033198; P:response to ATP; ISO:MGI. DR CDD; cd00141; NT_POLXc; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1. DR Gene3D; 3.40.50.10190; BRCT domain; 1. DR Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1. DR Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR002054; DNA-dir_DNA_pol_X. DR InterPro; IPR019843; DNA_pol-X_BS. DR InterPro; IPR010996; DNA_pol_b-like_N. DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain. DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf. DR InterPro; IPR037160; DNA_Pol_thumb_sf. DR InterPro; IPR022312; DNA_pol_X. DR InterPro; IPR043519; NT_sf. DR InterPro; IPR029398; PolB_thumb. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR InterPro; IPR027292; TdT. DR InterPro; IPR001726; TdT/Mu. DR PANTHER; PTHR11276:SF21; DNA NUCLEOTIDYLEXOTRANSFERASE; 1. DR PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF14791; DNA_pol_B_thumb; 1. DR Pfam; PF10391; DNA_pol_lambd_f; 1. DR Pfam; PF14716; HHH_8; 1. DR Pfam; PF01909; NTP_transf_2; 1. DR PIRSF; PIRSF000817; DNA_NT; 1. DR PIRSF; PIRSF501175; TDT; 1. DR PRINTS; PR00869; DNAPOLX. DR PRINTS; PR00871; DNAPOLXTDT. DR SMART; SM00292; BRCT; 1. DR SMART; SM00483; POLXc; 1. DR SUPFAM; SSF52113; BRCT domain; 1. DR SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1. DR SUPFAM; SSF81301; Nucleotidyltransferase; 1. DR SUPFAM; SSF81585; PsbU/PolX domain-like; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS00522; DNA_POLYMERASE_X; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing; KW Hydrolase; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; KW Phosphoprotein; Reference proteome; Terminal addition; Transferase. FT CHAIN 1..510 FT /note="DNA nucleotidylexotransferase" FT /id="PRO_0000218792" FT DOMAIN 27..124 FT /note="BRCT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 151..510 FT /note="Mediates interaction with DNTTIP2" FT /evidence="ECO:0000250|UniProtKB:P04053" FT REGION 258..262 FT /note="Involved in DNA binding" FT /evidence="ECO:0000269|PubMed:11823435, FT ECO:0000269|PubMed:23856622" FT MOTIF 11..17 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250|UniProtKB:P06526" FT BINDING 333..338 FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate" FT /ligand_id="ChEBI:CHEBI:61560" FT /evidence="ECO:0000305, ECO:0007744|PDB:4I2B, FT ECO:0007744|PDB:4I2C, ECO:0007744|PDB:4I2D, FT ECO:0007744|PDB:4I2E" FT BINDING 342..345 FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate" FT /ligand_id="ChEBI:CHEBI:61560" FT /evidence="ECO:0000305, ECO:0007744|PDB:4I2B, FT ECO:0007744|PDB:4I2C, ECO:0007744|PDB:4I2D, FT ECO:0007744|PDB:4I2E" FT BINDING 343 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000305, ECO:0007744|PDB:1JMS, FT ECO:0007744|PDB:4I2B" FT BINDING 345 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000305, ECO:0007744|PDB:1JMS, FT ECO:0007744|PDB:4I2B" FT BINDING 434 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000305, ECO:0007744|PDB:1JMS, FT ECO:0007744|PDB:4I2B" FT BINDING 449..450 FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate" FT /ligand_id="ChEBI:CHEBI:61560" FT /evidence="ECO:0000305, ECO:0007744|PDB:4I2B, FT ECO:0007744|PDB:4I2C, ECO:0007744|PDB:4I2D, FT ECO:0007744|PDB:4I2E" FT MOD_RES 134 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT VAR_SEQ 482 FT /note="K -> KGKTVTISPLDGKVSKLQKAL (in isoform TDT-L)" FT /evidence="ECO:0000303|PubMed:11136823, FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:3755527" FT /id="VSP_059967" FT MUTAGEN 29 FT /note="D->A: Almost complete loss of exonuclease activity FT in TDT-L; when associated with A-170 and A-473. Decreased FT transferase activity in TDT-S; when associated with A-170 FT and A-473." FT /evidence="ECO:0000269|PubMed:11938351" FT MUTAGEN 170 FT /note="D->A: Almost complete loss of exonuclease activity FT in TDT-L; when associated with A-29 and A-473. Decreased FT transferase activity in TDT-S; when associated with A-29 FT and A-473." FT /evidence="ECO:0000269|PubMed:11938351" FT MUTAGEN 342 FT /note="H->A: Nearly abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:23856622" FT MUTAGEN 398 FT /note="L->A: Nearly abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:23856622" FT MUTAGEN 399 FT /note="D->A: Nearly abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:23856622" FT MUTAGEN 400 FT /note="H->A: Reduces enzyme activity." FT /evidence="ECO:0000269|PubMed:23856622" FT MUTAGEN 403 FT /note="K->A: Nearly abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:23856622" FT MUTAGEN 473 FT /note="D->A: Almost complete loss of exonuclease activity FT in TDT-L; when associated with A-29 and A-170. Decreased FT transferase activity in TDT-S; when associated with A-29 FT and A-170." FT /evidence="ECO:0000269|PubMed:11938351" FT MUTAGEN 473 FT /note="D->A: Nearly abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:23856622" FT MUTAGEN 475 FT /note="H->A: Nearly abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:23856622" FT CONFLICT 26 FT /note="T -> M (in Ref. 2; CAA48634)" FT /evidence="ECO:0000305" FT CONFLICT 99 FT /note="L -> F (in Ref. 2; CAA48634)" FT /evidence="ECO:0000305" FT CONFLICT 193 FT /note="R -> G (in Ref. 1; CAA27735)" FT /evidence="ECO:0000305" FT CONFLICT 287 FT /note="Q -> K (in Ref. 1; CAA27735)" FT /evidence="ECO:0000305" FT CONFLICT 309 FT /note="E -> Q (in Ref. 1; CAA27735)" FT /evidence="ECO:0000305" FT CONFLICT 367 FT /note="D -> H (in Ref. 1; CAA27735)" FT /evidence="ECO:0000305" FT CONFLICT 441..445 FT /note="DRRAF -> ECAC (in Ref. 1; CAA27735)" FT /evidence="ECO:0000305" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 166..181 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 185..199 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 208..211 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 219..231 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 235..242 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 244..253 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 260..268 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 274..279 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 287..294 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 296..300 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 305..322 FT /evidence="ECO:0007829|PDB:4I2A" FT STRAND 327..330 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 332..335 FT /evidence="ECO:0007829|PDB:4I2A" FT STRAND 339..342 FT /evidence="ECO:0007829|PDB:4I2A" FT STRAND 344..349 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 355..372 FT /evidence="ECO:0007829|PDB:4I2A" FT STRAND 375..381 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 387..389 FT /evidence="ECO:0007829|PDB:5D49" FT STRAND 394..396 FT /evidence="ECO:0007829|PDB:4I2A" FT STRAND 401..411 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 412..414 FT /evidence="ECO:0007829|PDB:4I2A" FT STRAND 425..437 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 440..442 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 443..451 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 454..468 FT /evidence="ECO:0007829|PDB:4I2A" FT STRAND 470..472 FT /evidence="ECO:0007829|PDB:4I2A" FT STRAND 477..479 FT /evidence="ECO:0007829|PDB:4I2A" FT TURN 480..483 FT /evidence="ECO:0007829|PDB:4I2A" FT STRAND 484..486 FT /evidence="ECO:0007829|PDB:4I2E" FT HELIX 491..498 FT /evidence="ECO:0007829|PDB:4I2A" FT HELIX 505..507 FT /evidence="ECO:0007829|PDB:4I2A" SQ SEQUENCE 510 AA; 58266 MW; CF6E850EE36EE3BF CRC64; MDPLQAVHLG PRKKRPRQLG TPVASTPYDI RFRDLVLFIL EKKMGTTRRA FLMELARRKG FRVENELSDS VTHIVAENNS GSDVLEWLQL QNIKASSELE LLDISWLIEC MGAGKPVEMM GRHQLVVNRN SSPSPVPGSQ NVPAPAVKKI SQYACQRRTT LNNYNQLFTD ALDILAENDE LRENEGSCLA FMRASSVLKS LPFPITSMKD TEGIPCLGDK VKSIIEGIIE DGESSEAKAV LNDERYKSFK LFTSVFGVGL KTAEKWFRMG FRTLSKIQSD KSLRFTQMQK AGFLYYEDLV SCVNRPEAEA VSMLVKEAVV TFLPDALVTM TGGFRRGKMT GHDVDFLITS PEATEDEEQQ LLHKVTDFWK QQGLLLYCDI LESTFEKFKQ PSRKVDALDH FQKCFLILKL DHGRVHSEKS GQQEGKGWKA IRVDLVMCPY DRRAFALLGW TGSRQFERDL RRYATHERKM MLDNHALYDR TKRVFLEAES EEEIFAHLGL DYIEPWERNA //