Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P09838 (TDT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA nucleotidylexotransferase

EC=2.7.7.31
Alternative name(s):
Terminal addition enzyme
Terminal deoxynucleotidyltransferase
Short name=TDT
Short name=Terminal transferase
Gene names
Name:Dntt
Synonyms:Tdt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells.

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactor

Magnesium.

Subunit structure

Interacts with PRP19 and DNTTIP1. Forms a ternary complex with DNTTIP2 and core histone. Released from this complex by PCNA By similarity.

Subcellular location

Isoform TDT-S: Nucleus.

Isoform TDT-L: Cytoplasm.

Sequence similarities

Belongs to the DNA polymerase type-X family.

Contains 1 BRCT domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform TDT-L (identifier: P09838-1)

Also known as: TDT-Large; TdtL;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Inactivated at physiological temperature but is stable at lower temperatures.
Isoform TDT-S (identifier: P09838-2)

Also known as: TDT-Small; TdtS;

The sequence of this isoform differs from the canonical sequence as follows:
     483-502: Missing.
Note: Major form.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 530530DNA nucleotidylexotransferase
PRO_0000218792

Regions

Domain27 – 12498BRCT
Region151 – 530380Mediates interaction with DNTTIP2 By similarity
Region336 – 34510Involved in ssDNA binding By similarity

Sites

Metal binding2531Sodium; via carbonyl oxygen
Metal binding2551Sodium; via carbonyl oxygen
Metal binding3431Magnesium
Metal binding3451Magnesium
Metal binding4341Magnesium

Natural variations

Alternative sequence483 – 50220Missing in isoform TDT-S.
VSP_001309

Experimental info

Sequence conflict261T → M in CAA48634. Ref.2
Sequence conflict991L → F in CAA48634. Ref.2
Sequence conflict1931R → G in CAA27735. Ref.1
Sequence conflict2871Q → K in CAA27735. Ref.1
Sequence conflict3091E → Q in CAA27735. Ref.1
Sequence conflict3671D → H in CAA27735. Ref.1
Sequence conflict441 – 4455DRRAF → ECAC in CAA27735. Ref.1

Secondary structure

............................................................ 530
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform TDT-L (TDT-Large) (TdtL) [UniParc].

Last modified November 16, 2001. Version 3.
Checksum: E6B109DCF39C8107

FASTA53060,331
        10         20         30         40         50         60 
MDPLQAVHLG PRKKRPRQLG TPVASTPYDI RFRDLVLFIL EKKMGTTRRA FLMELARRKG 

        70         80         90        100        110        120 
FRVENELSDS VTHIVAENNS GSDVLEWLQL QNIKASSELE LLDISWLIEC MGAGKPVEMM 

       130        140        150        160        170        180 
GRHQLVVNRN SSPSPVPGSQ NVPAPAVKKI SQYACQRRTT LNNYNQLFTD ALDILAENDE 

       190        200        210        220        230        240 
LRENEGSCLA FMRASSVLKS LPFPITSMKD TEGIPCLGDK VKSIIEGIIE DGESSEAKAV 

       250        260        270        280        290        300 
LNDERYKSFK LFTSVFGVGL KTAEKWFRMG FRTLSKIQSD KSLRFTQMQK AGFLYYEDLV 

       310        320        330        340        350        360 
SCVNRPEAEA VSMLVKEAVV TFLPDALVTM TGGFRRGKMT GHDVDFLITS PEATEDEEQQ 

       370        380        390        400        410        420 
LLHKVTDFWK QQGLLLYCDI LESTFEKFKQ PSRKVDALDH FQKCFLILKL DHGRVHSEKS 

       430        440        450        460        470        480 
GQQEGKGWKA IRVDLVMCPY DRRAFALLGW TGSRQFERDL RRYATHERKM MLDNHALYDR 

       490        500        510        520        530 
TKGKTVTISP LDGKVSKLQK ALRVFLEAES EEEIFAHLGL DYIEPWERNA 

« Hide

Isoform TDT-S (TDT-Small) (TdtS) [UniParc].

Checksum: CF6E850EE36EE3BF
Show »

FASTA51058,266

References

« Hide 'large scale' references
[1]"Isolation and characterization of bovine and mouse terminal deoxynucleotidyltransferase cDNAs expressible in mammalian cells."
Koiwai O., Yokota T., Kageyama T., Hirose T., Yoshida S., Arai K.
Nucleic Acids Res. 14:5777-5792(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Differential splicing in mouse thymus generates two forms of terminal deoxynucleotidyl transferase."
Doyen N., Fanton D'Andon M., Bentolila L.A., Nguyen T.Q., Rougeon F.
Nucleic Acids Res. 21:1187-1191(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Thymus.
[3]Doyen N.
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 443-445.
[4]"The long isoform of terminal deoxynucleotidyl transferase (TdtL) enters the nucleus and, rather than catalyzing N addition, modulates the catalytic activity of the short isoform."
Benedict C.L., Gilfillan S., Kearney J.F.
J. Exp. Med. 193:89-99(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TDT-L AND TDT-S), CHARACTERIZATION.
Strain: C57BL/6.
Tissue: Thymus.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
Tissue: Thymus.
[6]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 388-393, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[7]"The two isoforms of mouse terminal deoxynucleotidyl transferase differ in both the ability to add N regions and subcellular localization."
Bentolila L.A., Fanton D'Andon M., Nguyen T.Q., Martinez O., Rougeon F., Doyen N.
EMBO J. 14:4221-4229(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY CHARACTERIZATION OF ALTERNATIVE FORMS.
[8]"Comparison of the two murine terminal deoxynucleotidyltransferase isoforms. A 20-amino acid insertion in the highly conserved carboxyl-terminal region modifies the thermosensitivity but not the catalytic activity."
Boule J.-B., Rougeon F., Papanicolaou C.
J. Biol. Chem. 275:28984-28988(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF ALTERNATIVE FORMS.
[9]Erratum
Boule J.-B., Rougeon F., Papanicolaou C.
J. Biol. Chem. 275:33184-33184(2000) [PubMed] [Europe PMC] [Abstract]
[10]"Crystal structures of a template-independent DNA polymerase: murine terminal deoxynucleotidyltransferase."
Delarue M., Boule J.-B., Lescar J., Expert-Bezancon N., Jourdan N., Sukumar N., Rougeon F., Papanicolaou C.
EMBO J. 21:427-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 130-530 (ISOFORM TLT-S).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04123 mRNA. Translation: CAA27735.1.
X68670 mRNA. Translation: CAA48634.2.
AF316014 mRNA. Translation: AAK07884.1.
AF316015 mRNA. Translation: AAK07885.1.
AK087978 mRNA. Translation: BAC40071.1.
AK088709 mRNA. Translation: BAC40518.1.
PIRB23595.
RefSeqNP_001036693.1. NM_001043228.1.
NP_033371.2. NM_009345.2.
UniGeneMm.25620.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JMSX-ray2.36A130-530[»]
1KDHX-ray3.00A148-530[»]
1KEJX-ray3.00A148-530[»]
4I27X-ray2.60A133-530[»]
4I28X-ray2.15A133-530[»]
4I29X-ray2.20A133-530[»]
4I2AX-ray1.90A133-530[»]
4I2BX-ray2.20A133-530[»]
4I2CX-ray2.10A133-530[»]
4I2DX-ray2.30A133-530[»]
4I2EX-ray2.00A133-530[»]
4I2FX-ray2.10A133-530[»]
4I2GX-ray2.50A133-530[»]
4I2HX-ray2.75A133-530[»]
4I2IX-ray2.50A133-530[»]
4I2JX-ray2.70A133-530[»]
4IQTX-ray2.60A133-530[»]
4IQUX-ray2.40A133-530[»]
4IQVX-ray2.90A133-530[»]
4IQWX-ray2.60A132-530[»]
ProteinModelPortalP09838.
SMRP09838. Positions 23-125, 149-530.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP09838.

Proteomic databases

PRIDEP09838.

Protocols and materials databases

DNASU21673.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000051806; ENSMUSP00000062078; ENSMUSG00000025014. [P09838-1]
ENSMUST00000112200; ENSMUSP00000107819; ENSMUSG00000025014. [P09838-2]
GeneID21673.
KEGGmmu:21673.
UCSCuc008hlo.1. mouse. [P09838-1]

Organism-specific databases

CTD1791.
MGIMGI:98659. Dntt.

Phylogenomic databases

eggNOGCOG1796.
GeneTreeENSGT00530000063002.
HOGENOMHOG000263600.
HOVERGENHBG003670.
InParanoidP09838.
KOK00977.
OMARRTTLNN.
OrthoDBEOG7BS4BH.
PhylomeDBP09838.
TreeFamTF103012.

Gene expression databases

ArrayExpressP09838.
BgeeP09838.
CleanExMM_DNTT.
GenevestigatorP09838.

Family and domain databases

Gene3D1.10.150.110. 1 hit.
3.40.50.10190. 1 hit.
InterProIPR001357. BRCT_dom.
IPR002054. DNA-dir_DNA_pol_X.
IPR019843. DNA_pol-X_BS.
IPR010996. DNA_pol_b-like_N.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR022312. DNA_pol_X.
IPR027421. DNA_pol_X_lyase_dom.
IPR002934. Nucleotidyltransferase.
IPR027292. TdT.
IPR001726. TdT/Mu.
[Graphical view]
PANTHERPTHR11276:SF6. PTHR11276:SF6. 1 hit.
PfamPF00533. BRCT. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFPIRSF000817. DNA_NT. 1 hit.
PIRSF501175. TDT. 1 hit.
PRINTSPR00869. DNAPOLX.
PR00871. DNAPOLXTDT.
SMARTSM00292. BRCT. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]
SUPFAMSSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
SSF81585. SSF81585. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09838.
NextBio300956.
PROP09838.
SOURCESearch...

Entry information

Entry nameTDT_MOUSE
AccessionPrimary (citable) accession number: P09838
Secondary accession number(s): Q99PD0, Q99PD1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 16, 2001
Last modified: April 16, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot