ID TDT_MOUSE STANDARD; PRT; 529 AA. AC P09838; DT 01-MAR-1989 (Rel. 10, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE DNA nucleotidylexotransferase (EC 2.7.7.31) (Terminal addition enzyme) DE (Terminal deoxynucleotidyltransferase) (TDT) (Terminal transferase). GN DNTT OR 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 SEQUENCE FROM N.A. 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 SEQUENCE FROM N.A. 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 RT terminal deoxynucleotidyl transferase."; RL Nucleic Acids Res. 21:1187-1191(1993). RN [3] RP 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). 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 FUNCTION OF THIS ENZYME IS THE CC ADDITION OF NUCLEOTIDES AT THE JUNCTION (N REGION) OF REARRANGED CC IG HEAVY CHAIN AND T CELL RECEPTOR GENE SEGMENTS DURING THE CC MATURATION OF B AND T CELLS. CC -!- CATALYTIC ACTIVITY: N deoxynucleoside triphosphate + CC {deoxynucleotide}(M) = N diphosphate + {deoxynucleotide}(M+N). CC -!- COFACTOR: REQUIRES MAGNESIUM. CC -!- SUBCELLULAR LOCATION: NUCLEAR (TDT-S) OR CYTOPLASMIC (TDT-L). CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; TDT-L(ARGE) (SHOWN HERE) AND CC TDT-S(MALL); ARE PRODUCED BY ALTERNATIVE SPLICING. THE TDT-S FORM CC IS THE MAJOR FORM. THE TWO FORMS DIFFER IN SUBCELLULAR LOCATION CC AND IN ACTIVITY AS THE LONG CYTOPLASMIC FORM CAN NOT ACT ON N CC REGIONS. CC -!- SIMILARITY: BELONGS TO 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; CAA48634.1; -. DR PIR; B23595; B23595. DR HSSP; P06766; 1BPB. DR MGD; MGI:98659; Tdt. DR InterPro; IPR001357; BRCT. DR InterPro; IPR002054; DNA_polX. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF00966; DNA_polymeraseX; 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 Transferase; Nucleotidyltransferase; Terminal addition; Magnesium; KW Alternative splicing; Nuclear protein. FT DOMAIN 27 118 BRCT. FT VARSPLIC 482 501 MISSING (IN ISOFORM TDT-S). FT CONFLICT 26 26 M -> T (IN REF. 1). FT CONFLICT 99 99 F -> L (IN REF. 1). 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 DRAS -> ECAC (IN REF. 1). SQ SEQUENCE 529 AA; 60179 MW; DE949FD7CE3A9562 CRC64; MDPLQAVHLG PRKKRPRQLG TPVASMPYDI RFRDLVLFIL EKKMGTTRRA FLMELARRKG FRVENELSDS VTHIVAENNS GSDVLEWLQL QNIKASSEFE 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 DRASALLGWT GSRQFERDLR RYATHERKMM LDNHALYDRT KGKTVTISPL DGKVSKLQKA LRVFLEAESE EEIFAHLGLD YIEPWERNA //