P09838 (TDT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Terminal addition
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Magnesium Metal-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA metabolic process Inferred from direct assay Ref.2. Source: MGI DNA modification Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Traceable author statement PubMed 11938351. Source: MGI
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA nucleotidylexotransferase activity Inferred from direct assay Ref.2. Source: MGI DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 530

530

DNA nucleotidylexotransferase

PRO_0000218792

Regions

Domain

27 – 124

98

BRCT

Region

151 – 530

380

Mediates interaction with DNTTIP2 By similarity

Region

336 – 345

10

Involved in ssDNA binding By similarity

Sites

Metal binding

253

1

Sodium; via carbonyl oxygen

Metal binding

255

1

Sodium; via carbonyl oxygen

Metal binding

343

1

Magnesium

Metal binding

345

1

Magnesium

Metal binding

434

1

Magnesium

Natural variations

Alternative sequence

483 – 502

20

Missing in isoform TDT-S.

VSP_001309

Experimental info

Sequence conflict

26

1

T → M in CAA48634. Ref.2

Sequence conflict

99

1

L → F in CAA48634. Ref.2

Sequence conflict

193

1

R → G in CAA27735. Ref.1

Sequence conflict

287

1

Q → K in CAA27735. Ref.1

Sequence conflict

309

1

E → Q in CAA27735. Ref.1

Sequence conflict

367

1

D → H in CAA27735. Ref.1

Sequence conflict

441 – 445

5

DRRAF → ECAC in CAA27735. Ref.1

Secondary structure

1

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530

Helix Strand Turn

Details...

Helix

154 – 156

3

Helix

166 – 181

16

Helix

185 – 199

15

Helix

208 – 211

4

Helix

219 – 231

13

Helix

235 – 242

8

Helix

244 – 253

10

Helix

260 – 268

9

Helix

274 – 279

6

Helix

287 – 294

8

Helix

296 – 300

5

Helix

305 – 322

18

Beta strand

327 – 330

4

Helix

332 – 335

4

Beta strand

341 – 349

9

Helix

355 – 371

17

Beta strand

375 – 381

7

Beta strand

402 – 411

10

Helix

412 – 414

3

Beta strand

426 – 437

12

Helix

440 – 442

3

Helix

443 – 451

9

Helix

454 – 468

15

Beta strand

470 – 472

3

Beta strand

477 – 479

3

Turn

480 – 482

3

Beta strand

504 – 506

3

Helix

511 – 518

8

Helix

525 – 527

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform TDT-L (TDT-Large) (TdtL) [UniParc]. Last modified November 16, 2001. Version 3. Checksum: E6B109DCF39C8107	FASTA	530	60,331
	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
	Isoform TDT-S (TDT-Small) (TdtS) [UniParc]. Checksum: CF6E850EE36EE3BF	FASTA	510	58,266
	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 TKRVFLEAES EEEIFAHLGL DYIEPWERNA

References

	« Hide 'large scale' referencesShow '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. , 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, 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.

IPI

IPI00111374.
IPI00314577.

PIR

B23595.

RefSeq

NP_001036693.1. NM_001043228.1.
NP_033371.2. NM_009345.2.

UniGene

Mm.25620.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JMS	X-ray	2.36	A	130-530	[»]
1KDH	X-ray	3.00	A	148-530	[»]
1KEJ	X-ray	3.00	A	148-530	[»]

ProteinModelPortal

P09838.

SMR

P09838. Positions 23-125, 148-530.

ModBase

Search...

PTM databases

PhosphoSite

P09838.

Proteomic databases

PRIDE

P09838.

Protocols and materials databases

DNASU

21673.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000051806; ENSMUSP00000062078; ENSMUSG00000025014.
ENSMUST00000112200; ENSMUSP00000107819; ENSMUSG00000025014.

GeneID

21673.

KEGG

mmu:21673.

UCSC

uc008hlo.1. mouse.

Organism-specific databases

CTD

1791.

MGI

MGI:98659. Dntt.

Phylogenomic databases

eggNOG

COG1796.

GeneTree

ENSGT00530000063002.

HOGENOM

HOG000263600.

HOVERGEN

HBG003670.

InParanoid

P09838.

KO

K00977.

OMA

RRTTLNN.

OrthoDB

EOG4SQWWN.

Gene expression databases

ArrayExpress

P09838.

Bgee

P09838.

CleanEx

MM_DNTT.

Genevestigator

P09838.

GermOnline

ENSMUSG00000025014. Mus musculus.

Family and domain databases

InterPro

IPR001357. 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.
IPR002934. Nucleotidyltransferase.
IPR027292. TdT.
IPR001726. TdT/Mu.
[Graphical view]

PANTHER

PTHR11276:SF6. PTHR11276:SF6. 1 hit.

Pfam

PF00533. BRCT. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]

PIRSF

PIRSF000817. DNA_NT. 1 hit.
PIRSF501175. TDT. 1 hit.

PRINTS

PR00869. DNAPOLX.
PR00871. DNAPOLXTDT.

SMART

SM00292. BRCT. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]

SUPFAM

SSF52113. BRCT. 1 hit.
SSF81585. DNA_pol_lambd_fingers_domain. 1 hit.
SSF47802. DNApol_B_N_like. 1 hit.

PROSITE

PS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P09838.

NextBio

300956.

SOURCE

Search...

Entry information

Entry name

TDT_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 141 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program