P09838 · TDT_MOUSE
- ProteinDNA nucleotidylexotransferase
- GeneDntt
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids510 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Isoform TDT-S
Transferase that catalyzes the nontemplated addition of nucleoside triphosphate to coding ends during V(D)J recombination (N addition). Involved in the generation of diversity in the antigen-binding region of immunoglobulin heavy and light chains and T-cell receptors during B- and T-cell development. Does not act on double-stranded DNA with blunt ends.
Isoform TDT-L
3'-to-5' DNA exonuclease. Involved in the generation of diversity in the antigen-binding region of immunoglobulin heavy and light chains and T-cell receptors during B- and T-cell development. Acts on single-stranded and double-stranded DNA with 3' or 5' extensions, but not on double-stranded DNA with blunt ends. Attenuates not only isoform TDT-S-catalyzed N addition, but also P (palindromic) addition in coding joins (PubMed:11938351).
Lacks terminal transferase activity (PubMed:11136823, PubMed:7556063).
Lacks terminal transferase activity (PubMed:11136823, PubMed:7556063).
Catalytic activity
- a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Cofactor
Note: Can also utilize other divalent cations, such as Mn2+ and Co2+ (in vitro).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
300 μM | dATP | 35 |
In assays with isoform TDT-S.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 333-338 | a 2'-deoxyribonucleoside 5'-triphosphate (UniProtKB | ChEBI) | ||||
Sequence: GFRRGK | ||||||
Binding site | 342-345 | a 2'-deoxyribonucleoside 5'-triphosphate (UniProtKB | ChEBI) | ||||
Sequence: HDVD | ||||||
Binding site | 343 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 345 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 434 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 449-450 | a 2'-deoxyribonucleoside 5'-triphosphate (UniProtKB | ChEBI) | ||||
Sequence: GW |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | cytosol | |
Cellular Component | euchromatin | |
Cellular Component | nuclear matrix | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | DNA nucleotidylexotransferase activity | |
Molecular Function | DNA-directed DNA polymerase activity | |
Molecular Function | hydrolase activity | |
Molecular Function | metal ion binding | |
Biological Process | DNA metabolic process | |
Biological Process | DNA modification | |
Biological Process | double-strand break repair via nonhomologous end joining | |
Biological Process | response to ATP |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA nucleotidylexotransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP09838
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 29 | Almost complete loss of exonuclease activity in TDT-L; when associated with A-170 and A-473. Decreased transferase activity in TDT-S; when associated with A-170 and A-473. | ||||
Sequence: D → A | ||||||
Mutagenesis | 170 | Almost complete loss of exonuclease activity in TDT-L; when associated with A-29 and A-473. Decreased transferase activity in TDT-S; when associated with A-29 and A-473. | ||||
Sequence: D → A | ||||||
Mutagenesis | 342 | Nearly abolishes enzyme activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 398 | Nearly abolishes enzyme activity. | ||||
Sequence: L → A | ||||||
Mutagenesis | 399 | Nearly abolishes enzyme activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 400 | Reduces enzyme activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 403 | Nearly abolishes enzyme activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 473 | Almost complete loss of exonuclease activity in TDT-L; when associated with A-29 and A-170. Decreased transferase activity in TDT-S; when associated with A-29 and A-170. | ||||
Sequence: D → A | ||||||
Mutagenesis | 473 | Nearly abolishes enzyme activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 475 | Nearly abolishes enzyme activity. | ||||
Sequence: H → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 27 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000218792 | 1-510 | DNA nucleotidylexotransferase | |||
Sequence: MDPLQAVHLGPRKKRPRQLGTPVASTPYDIRFRDLVLFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQLQNIKASSELELLDISWLIECMGAGKPVEMMGRHQLVVNRNSSPSPVPGSQNVPAPAVKKISQYACQRRTTLNNYNQLFTDALDILAENDELRENEGSCLAFMRASSVLKSLPFPITSMKDTEGIPCLGDKVKSIIEGIIEDGESSEAKAVLNDERYKSFKLFTSVFGVGLKTAEKWFRMGFRTLSKIQSDKSLRFTQMQKAGFLYYEDLVSCVNRPEAEAVSMLVKEAVVTFLPDALVTMTGGFRRGKMTGHDVDFLITSPEATEDEEQQLLHKVTDFWKQQGLLLYCDILESTFEKFKQPSRKVDALDHFQKCFLILKLDHGRVHSEKSGQQEGKGWKAIRVDLVMCPYDRRAFALLGWTGSRQFERDLRRYATHERKMMLDNHALYDRTKRVFLEAESEEEIFAHLGLDYIEPWERNA | ||||||
Modified residue | 134 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform TDT-L: Expressed in the thymus, and, at lower levels, in the bone marrow (PubMed:11136823, PubMed:7556063, PubMed:8464703).
Detected in both cycling and noncycling pro-B and pre-B cells (at protein level) (PubMed:11938351).
Isoform TDT-S: Expressed in both cycling and noncycling pro-B, but not pre-B, cells (at protein level) (PubMed:11938351).
Not detected in mature peripheral or germinal center B cells (PubMed:11938351).
Detected in both cycling and noncycling pro-B and pre-B cells (at protein level) (PubMed:11938351).
Isoform TDT-S: Expressed in both cycling and noncycling pro-B, but not pre-B, cells (at protein level) (PubMed:11938351).
Not detected in mature peripheral or germinal center B cells (PubMed:11938351).
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-22 | Disordered | ||||
Sequence: MDPLQAVHLGPRKKRPRQLGTP | ||||||
Motif | 11-17 | Nuclear localization signal | ||||
Sequence: PRKKRPR | ||||||
Domain | 27-124 | BRCT | ||||
Sequence: PYDIRFRDLVLFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQLQNIKASSELELLDISWLIECMGAGKPVEMMGRHQ | ||||||
Region | 151-510 | Mediates interaction with DNTTIP2 | ||||
Sequence: SQYACQRRTTLNNYNQLFTDALDILAENDELRENEGSCLAFMRASSVLKSLPFPITSMKDTEGIPCLGDKVKSIIEGIIEDGESSEAKAVLNDERYKSFKLFTSVFGVGLKTAEKWFRMGFRTLSKIQSDKSLRFTQMQKAGFLYYEDLVSCVNRPEAEAVSMLVKEAVVTFLPDALVTMTGGFRRGKMTGHDVDFLITSPEATEDEEQQLLHKVTDFWKQQGLLLYCDILESTFEKFKQPSRKVDALDHFQKCFLILKLDHGRVHSEKSGQQEGKGWKAIRVDLVMCPYDRRAFALLGWTGSRQFERDLRRYATHERKMMLDNHALYDRTKRVFLEAESEEEIFAHLGLDYIEPWERNA | ||||||
Region | 258-262 | Involved in DNA binding | ||||
Sequence: VGLKT |
Sequence similarities
Belongs to the DNA polymerase type-X family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P09838-2
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.
- NameTDT-S
- SynonymsTDT-Small, TdtS
- Length510
- Mass (Da)58,266
- Last updated2018-12-05 v4
- ChecksumCF6E850EE36EE3BF
P09838-1
- NameTDT-L
- SynonymsTDT-Large, TdtL
- Differences from canonical
- 482-482: K → KGKTVTISPLDGKVSKLQKAL
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 26 | in Ref. 2; CAA48634 | ||||
Sequence: T → M | ||||||
Sequence conflict | 99 | in Ref. 2; CAA48634 | ||||
Sequence: L → F | ||||||
Sequence conflict | 193 | in Ref. 1; CAA27735 | ||||
Sequence: R → G | ||||||
Sequence conflict | 287 | in Ref. 1; CAA27735 | ||||
Sequence: Q → K | ||||||
Sequence conflict | 309 | in Ref. 1; CAA27735 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 367 | in Ref. 1; CAA27735 | ||||
Sequence: D → H | ||||||
Sequence conflict | 441-445 | in Ref. 1; CAA27735 | ||||
Sequence: DRRAF → ECAC | ||||||
Alternative sequence | VSP_059967 | 482 | in isoform TDT-L | |||
Sequence: K → KGKTVTISPLDGKVSKLQKAL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X04123 EMBL· GenBank· DDBJ | CAA27735.1 EMBL· GenBank· DDBJ | mRNA | ||
X68670 EMBL· GenBank· DDBJ | CAA48634.2 EMBL· GenBank· DDBJ | mRNA | ||
AF316014 EMBL· GenBank· DDBJ | AAK07884.1 EMBL· GenBank· DDBJ | mRNA | ||
AF316015 EMBL· GenBank· DDBJ | AAK07885.1 EMBL· GenBank· DDBJ | mRNA | ||
AK087978 EMBL· GenBank· DDBJ | BAC40071.1 EMBL· GenBank· DDBJ | mRNA | ||
AK088709 EMBL· GenBank· DDBJ | BAC40518.1 EMBL· GenBank· DDBJ | mRNA |