ID TDT_MOUSE STANDARD; PRT; 530 AA. AC P09838; Q99PD0; Q99PD1; DT 01-MAR-1989 (Rel. 10, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 25-JAN-2005 (Rel. 46, Last annotation update) DE DNA nucleotidylexotransferase (EC 2.7.7.31) (Terminal addition enzyme) DE (Terminal deoxynucleotidyltransferase) (TDT) (Terminal transferase). GN Name=Dntt; Synonyms=Tdt; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=86286588; PubMed=3755527; 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. RC STRAIN=BALB/c; TISSUE=Thymus; RX MEDLINE=93219079; PubMed=8464703; 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 (ISOFORMS TDT-L AND TDT-S), AND CHARACTERIZATION. RC STRAIN=C57BL/6; TISSUE=Thymus; RX PubMed=11136823; 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. RC STRAIN=NOD; TISSUE=Thymus; RX MEDLINE=22354683; PubMed=12466851; DOI=10.1038/nature01266; RA Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S., RA Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H., RA Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T., RA Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J., RA Schriml L.M., Kanapin A., Matsuda H., Batalov S., Beisel K.W., RA Blake J.A., Bradt D., Brusic V., Chothia C., Corbani L.E., Cousins S., RA Dalla E., Dragani T.A., Fletcher C.F., Forrest A., Frazer K.S., RA Gaasterland T., Gariboldi M., Gissi C., Godzik A., Gough J., RA Grimmond S., Gustincich S., Hirokawa N., Jackson I.J., Jarvis E.D., RA Kanai A., Kawaji H., Kawasawa Y., Kedzierski R.M., King B.L., RA Konagaya A., Kurochkin I.V., Lee Y., Lenhard B., Lyons P.A., RA Maglott D.R., Maltais L., Marchionni L., McKenzie L., Miki H., RA Nagashima T., Numata K., Okido T., Pavan W.J., Pertea G., Pesole G., RA Petrovsky N., Pillai R., Pontius J.U., Qi D., Ramachandran S., RA Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z., Ringwald M., RA Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K., RA Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M., RA Verardo R., Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C., RA Wilming L.G., Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L., RA Yuan Z., Zavolan M., Zhu Y., Zimmer A., Carninci P., Hayatsu N., RA Hirozane-Kishikawa T., Konno H., Nakamura M., Sakazume N., Sato K., RA Shiraki T., Waki K., Kawai J., Aizawa K., Arakawa T., Fukuda S., RA Hara A., Hashizume W., Imotani K., Ishii Y., Itoh M., Kagawa I., RA Miyazaki A., Sakai K., Sasaki D., Shibata K., Shinagawa A., RA Yasunishi A., Yoshino M., Waterston R., Lander E.S., Rogers J., RA Birney E., Hayashizaki Y.; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [6] RP PRELIMINARY CHARACTERIZATION OF ALTERNATIVE FORMS. RX MEDLINE=96016194; 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 [7] RP CHARACTERIZATION OF ALTERNATIVE FORMS. RX MEDLINE=20435863; 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 [8] RP ERRATUM. RX PubMed=11032847; RA Boule J.-B., Rougeon F., Papanicolaou C.; RL J. Biol. Chem. 275:33184-33184(2000). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 130-530 (ISOFORM TLT-S). RX MEDLINE=21681410; 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 of CC 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: N deoxynucleoside triphosphate + CC {deoxynucleotide}(M) = N diphosphate + {deoxynucleotide}(M+N). CC -!- COFACTOR: Magnesium. CC -!- SUBUNIT: Interacts with PRP19 and TDIF1 (By similarity). CC -!- SUBCELLULAR LOCATION: Nuclear (isoform TDT-S); cytoplasmic CC (isoform TDT-L). 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; -. DR EMBL; X68670; CAA48634.2; -. DR EMBL; AF316014; AAK07884.1; -. DR EMBL; AF316015; AAK07885.1; -. DR EMBL; AK087978; BAC40071.1; -. DR EMBL; AK088709; BAC40518.1; -. DR PDB; 1JMS; X-ray; A=130-530. DR PDB; 1KDH; X-ray; A=148-530. DR PDB; 1KEJ; X-ray; A=148-530. DR MGD; MGI:98659; Dntt. DR GO; GO:0005634; C:nucleus; TAS. DR GO; GO:0003912; F:DNA nucleotidylexotransferase activity; IDA. DR GO; GO:0006259; P:DNA metabolism; IDA. DR InterPro; IPR001357; BRCT. DR InterPro; IPR002054; DNA_polX. DR InterPro; IPR001726; DNA_polXtrans. DR InterPro; IPR010996; DNApol_B_N_like. DR InterPro; IPR002934; NTP_transf. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF01909; NTP_transf_2; 1. DR PRINTS; PR00869; DNAPOLX. DR SMART; SM00292; BRCT; 1. DR SMART; SM00483; POLXc; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS00522; DNA_POLYMERASE_X; 1. KW 3D-structure; Alternative splicing; Magnesium; Metal-binding; KW Nuclear protein; Nucleotidyltransferase; Terminal addition; KW Transferase. FT DOMAIN 27 118 BRCT. FT SITE 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 VARSPLIC 483 502 Missing (in isoform TDT-S). FT /FTId=VSP_001309. FT CONFLICT 26 26 T -> M (in Ref. 2). FT CONFLICT 99 99 L -> F (in Ref. 2). FT CONFLICT 193 193 R -> G (in Ref. 1). FT CONFLICT 287 287 Q -> K (in Ref. 1). FT CONFLICT 309 309 E -> Q (in Ref. 1). FT CONFLICT 367 367 D -> H (in Ref. 1). FT CONFLICT 441 444 DRRA -> ECAC (in Ref. 1). 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 //