ID TDT_MOUSE Reviewed; 530 AA. AC P09838; Q99PD0; Q99PD1; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 16-NOV-2001, sequence version 3. DT 19-MAR-2014, entry version 148. DE RecName: Full=DNA nucleotidylexotransferase; DE EC=2.7.7.31; DE AltName: Full=Terminal addition enzyme; DE AltName: Full=Terminal deoxynucleotidyltransferase; DE Short=TDT; DE Short=Terminal transferase; GN Name=Dntt; Synonyms=Tdt; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. 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]. RC STRAIN=BALB/c; 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), AND RP CHARACTERIZATION. RC STRAIN=C57BL/6; 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) RT enters the nucleus and, rather than catalyzing N addition, modulates RT the catalytic activity of the short isoform."; RL J. Exp. Med. 193:89-99(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [7] RP PRELIMINARY CHARACTERIZATION OF ALTERNATIVE FORMS. RX PubMed=7556063; RA Bentolila L.A., Fanton D'Andon M., Nguyen T.Q., Martinez O., RA Rougeon F., Doyen N.; RT "The two isoforms of mouse terminal deoxynucleotidyl transferase RT differ in both the ability to add N regions and subcellular RT localization."; RL EMBO J. 14:4221-4229(1995). RN [8] RP CHARACTERIZATION OF ALTERNATIVE FORMS. 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. RX PubMed=11032847; RA Boule J.-B., Rougeon F., Papanicolaou C.; RL J. Biol. Chem. 275:33184-33184(2000). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 130-530 (ISOFORM TLT-S). 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). CC -!- FUNCTION: Template-independent DNA polymerase which catalyzes the CC random addition of deoxynucleoside 5'-triphosphate to the 3'-end CC of a DNA initiator. One of the in vivo functions of this enzyme is CC the addition of nucleotides at the junction (N region) of CC rearranged Ig heavy chain and T-cell receptor gene segments during CC the maturation of B- and T-cells. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- COFACTOR: Magnesium. CC -!- SUBUNIT: Interacts with PRP19 and DNTTIP1. Forms a ternary complex CC with DNTTIP2 and core histone. Released from this complex by PCNA CC (By similarity). CC -!- SUBCELLULAR LOCATION: Isoform TDT-S: Nucleus. CC -!- SUBCELLULAR LOCATION: Isoform TDT-L: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=TDT-L; Synonyms=TDT-Large, TdtL; CC IsoId=P09838-1; Sequence=Displayed; CC Note=Inactivated at physiological temperature but is stable at CC lower temperatures; CC Name=TDT-S; Synonyms=TDT-Small, TdtS; CC IsoId=P09838-2; Sequence=VSP_001309; CC Note=Major form; CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. CC -!- SIMILARITY: Contains 1 BRCT domain. 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 PIR; B23595; B23595. DR RefSeq; NP_001036693.1; NM_001043228.1. DR RefSeq; NP_033371.2; NM_009345.2. DR UniGene; Mm.25620; -. DR PDB; 1JMS; X-ray; 2.36 A; A=130-530. DR PDB; 1KDH; X-ray; 3.00 A; A=148-530. DR PDB; 1KEJ; X-ray; 3.00 A; A=148-530. DR PDB; 4I27; X-ray; 2.60 A; A=133-530. DR PDB; 4I28; X-ray; 2.15 A; A=133-530. DR PDB; 4I29; X-ray; 2.20 A; A=133-530. DR PDB; 4I2A; X-ray; 1.90 A; A=133-530. DR PDB; 4I2B; X-ray; 2.20 A; A=133-530. DR PDB; 4I2C; X-ray; 2.10 A; A=133-530. DR PDB; 4I2D; X-ray; 2.30 A; A=133-530. DR PDB; 4I2E; X-ray; 2.00 A; A=133-530. DR PDB; 4I2F; X-ray; 2.10 A; A=133-530. DR PDB; 4I2G; X-ray; 2.50 A; A=133-530. DR PDB; 4I2H; X-ray; 2.75 A; A=133-530. DR PDB; 4I2I; X-ray; 2.50 A; A=133-530. DR PDB; 4I2J; X-ray; 2.70 A; A=133-530. DR PDB; 4IQT; X-ray; 2.60 A; A=133-530. DR PDB; 4IQU; X-ray; 2.40 A; A=133-530. DR PDB; 4IQV; X-ray; 2.90 A; A=133-530. DR PDB; 4IQW; X-ray; 2.60 A; A=132-530. 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 ProteinModelPortal; P09838; -. DR SMR; P09838; 23-125, 149-530. DR PhosphoSite; P09838; -. DR PRIDE; P09838; -. DR DNASU; 21673; -. DR Ensembl; ENSMUST00000051806; ENSMUSP00000062078; ENSMUSG00000025014. [P09838-1] DR Ensembl; ENSMUST00000112200; ENSMUSP00000107819; ENSMUSG00000025014. [P09838-2] DR GeneID; 21673; -. DR KEGG; mmu:21673; -. DR UCSC; uc008hlo.1; mouse. [P09838-1] DR CTD; 1791; -. DR MGI; MGI:98659; Dntt. DR eggNOG; COG1796; -. DR GeneTree; ENSGT00530000063002; -. DR HOGENOM; HOG000263600; -. DR HOVERGEN; HBG003670; -. DR InParanoid; P09838; -. DR KO; K00977; -. DR OMA; RRTTLNN; -. DR OrthoDB; EOG7BS4BH; -. DR TreeFam; TF103012; -. DR EvolutionaryTrace; P09838; -. DR NextBio; 300956; -. DR PRO; PR:P09838; -. DR ArrayExpress; P09838; -. DR Bgee; P09838; -. DR CleanEx; MM_DNTT; -. DR Genevestigator; P09838; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; TAS:MGI. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006304; P:DNA modification; IEA:UniProtKB-KW. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:GOC. DR Gene3D; 1.10.150.110; -; 1. DR Gene3D; 3.40.50.10190; -; 1. DR InterPro; IPR001357; BRCT_dom. 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; IPR022312; DNA_pol_X. DR InterPro; IPR027421; DNA_pol_X_lyase_dom. DR InterPro; IPR002934; Nucleotidyltransferase. DR InterPro; IPR027292; TdT. DR InterPro; IPR001726; TdT/Mu. DR PANTHER; PTHR11276:SF6; PTHR11276:SF6; 1. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF10391; DNA_pol_lambd_f; 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; SSF47802; SSF47802; 1. DR SUPFAM; SSF52113; SSF52113; 1. DR SUPFAM; SSF81585; SSF81585; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS00522; DNA_POLYMERASE_X; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; KW Direct protein sequencing; Magnesium; Metal-binding; KW Nucleotidyltransferase; Nucleus; Reference proteome; KW Terminal addition; Transferase. FT CHAIN 1 530 DNA nucleotidylexotransferase. FT /FTId=PRO_0000218792. FT DOMAIN 27 124 BRCT. FT REGION 151 530 Mediates interaction with DNTTIP2 (By FT similarity). FT REGION 336 345 Involved in ssDNA binding (By FT similarity). FT METAL 253 253 Sodium; via carbonyl oxygen. FT METAL 255 255 Sodium; via carbonyl oxygen. FT METAL 343 343 Magnesium. FT METAL 345 345 Magnesium. FT METAL 434 434 Magnesium. FT VAR_SEQ 483 502 Missing (in isoform TDT-S). FT /FTId=VSP_001309. FT CONFLICT 26 26 T -> M (in Ref. 2; CAA48634). FT CONFLICT 99 99 L -> F (in Ref. 2; CAA48634). FT CONFLICT 193 193 R -> G (in Ref. 1; CAA27735). FT CONFLICT 287 287 Q -> K (in Ref. 1; CAA27735). FT CONFLICT 309 309 E -> Q (in Ref. 1; CAA27735). FT CONFLICT 367 367 D -> H (in Ref. 1; CAA27735). FT CONFLICT 441 445 DRRAF -> ECAC (in Ref. 1; CAA27735). FT HELIX 154 156 FT HELIX 166 181 FT HELIX 185 199 FT HELIX 208 211 FT HELIX 219 231 FT HELIX 235 242 FT HELIX 244 253 FT HELIX 260 268 FT HELIX 274 279 FT HELIX 287 294 FT HELIX 296 300 FT HELIX 305 322 FT STRAND 327 330 FT HELIX 332 335 FT STRAND 339 342 FT STRAND 344 349 FT HELIX 355 372 FT STRAND 375 381 FT STRAND 394 396 FT STRAND 401 411 FT HELIX 412 414 FT STRAND 425 437 FT HELIX 440 442 FT HELIX 443 451 FT HELIX 454 468 FT STRAND 470 472 FT STRAND 477 479 FT TURN 480 482 FT STRAND 504 506 FT HELIX 511 518 FT HELIX 525 527 SQ SEQUENCE 530 AA; 60331 MW; E6B109DCF39C8107 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 TKGKTVTISP LDGKVSKLQK ALRVFLEAES EEEIFAHLGL DYIEPWERNA //