UniProt functional annotation for P09838



	UniProt functional annotation for P09838

UniProt code: P09838.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

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. {ECO:0000269|PubMed:11136823, ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:23856622, ECO:0000269|PubMed:7556063, ECO:0000269|PubMed:8464703}.

Function: [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). {ECO:0000269|PubMed:11136823, ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:7556063}.

Catalytic activity: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.31; Evidence={ECO:0000269|PubMed:23856622, ECO:0000269|PubMed:23968551};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23856622}; Note=Can also utilize other divalent cations, such as Mn(2+) and Co(2+) (in vitro). {ECO:0000269|PubMed:23856622, ECO:0000305};

Biophysicochemical properties: Kinetic parameters: KM=300 uM for dATP (at 35 degrees Celsius) {ECO:0000269|PubMed:10878023}; Note=In assays with isoform TDT-S. {ECO:0000269|PubMed:10878023};

Subunit: Interacts with PRP19 and DNTTIP1. Forms a ternary complex with DNTTIP2 and core histone. Released from this complex by PCNA. Interacts with TRERF1. {ECO:0000250|UniProtKB:P04053}.

Subcellular location: [Isoform TDT-S]: Nucleus {ECO:0000269|PubMed:7556063}.

Subcellular location: [Isoform TDT-L]: Nucleus {ECO:0000269|PubMed:11136823}. Cytoplasm {ECO:0000269|PubMed:7556063}. Note=The subcellular location is controversial. Detected in the nucleus (PubMed:11136823). Found mainly in the cytoplasm (PubMed:7556063). {ECO:0000269|PubMed:11136823, ECO:0000269|PubMed:7556063}.

Tissue specificity: Isoform TDT-L: Expressed in the thymus, and, at lower levels, in the bone marrow (PubMed:8464703, PubMed:11136823, PubMed:7556063). 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). {ECO:0000269|PubMed:11136823, ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:7556063, ECO:0000269|PubMed:8464703}.

Miscellaneous: [Isoform TDT-S]: Major form in the thymus and the bone marrow (PubMed:8464703, PubMed:11136823). Catalyzes the nontemplated addition of nucleoside triphosphate to coding ends during V(D)J recombination (PubMed:23856622). May have a longer half-life than isoform TDT-L (PubMed:7556063). {ECO:0000269|PubMed:11136823, ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:7556063, ECO:0000269|PubMed:8464703}.

Miscellaneous: [Isoform TDT-L]: Exhibits 3'-to-5' DNA exonuclease activity (EC=3.1.11.-) (PubMed:23856622). May have a shorter half-life than isoform TDT-S (PubMed:7556063, PubMed:10878023). {ECO:0000269|PubMed:10878023, ECO:0000269|PubMed:11938351, ECO:0000269|PubMed:7556063}.

Similarity: Belongs to the DNA polymerase type-X family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



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. {ECO:0000269\|PubMed:11136823, ECO:0000269\|PubMed:11938351, ECO:0000269\|PubMed:23856622, ECO:0000269\|PubMed:7556063, ECO:0000269\|PubMed:8464703}.



Function:		[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). {ECO:0000269\|PubMed:11136823, ECO:0000269\|PubMed:11938351, ECO:0000269\|PubMed:7556063}.


Catalytic activity:		Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.31; Evidence={ECO:0000269\|PubMed:23856622, ECO:0000269\|PubMed:23968551};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269\|PubMed:23856622}; Note=Can also utilize other divalent cations, such as Mn(2+) and Co(2+) (in vitro). {ECO:0000269\|PubMed:23856622, ECO:0000305};
Biophysicochemical properties:		Kinetic parameters: KM=300 uM for dATP (at 35 degrees Celsius) {ECO:0000269\|PubMed:10878023}; Note=In assays with isoform TDT-S. {ECO:0000269\|PubMed:10878023};
Subunit:		Interacts with PRP19 and DNTTIP1. Forms a ternary complex with DNTTIP2 and core histone. Released from this complex by PCNA. Interacts with TRERF1. {ECO:0000250\|UniProtKB:P04053}.
Subcellular location:		[Isoform TDT-S]: Nucleus {ECO:0000269\|PubMed:7556063}.
Subcellular location:		[Isoform TDT-L]: Nucleus {ECO:0000269\|PubMed:11136823}. Cytoplasm {ECO:0000269\|PubMed:7556063}. Note=The subcellular location is controversial. Detected in the nucleus (PubMed:11136823). Found mainly in the cytoplasm (PubMed:7556063). {ECO:0000269\|PubMed:11136823, ECO:0000269\|PubMed:7556063}.
Tissue specificity:		Isoform TDT-L: Expressed in the thymus, and, at lower levels, in the bone marrow (PubMed:8464703, PubMed:11136823, PubMed:7556063). 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). {ECO:0000269\|PubMed:11136823, ECO:0000269\|PubMed:11938351, ECO:0000269\|PubMed:7556063, ECO:0000269\|PubMed:8464703}.
Miscellaneous:		[Isoform TDT-S]: Major form in the thymus and the bone marrow (PubMed:8464703, PubMed:11136823). Catalyzes the nontemplated addition of nucleoside triphosphate to coding ends during V(D)J recombination (PubMed:23856622). May have a longer half-life than isoform TDT-L (PubMed:7556063). {ECO:0000269\|PubMed:11136823, ECO:0000269\|PubMed:11938351, ECO:0000269\|PubMed:7556063, ECO:0000269\|PubMed:8464703}.
Miscellaneous:		[Isoform TDT-L]: Exhibits 3'-to-5' DNA exonuclease activity (EC=3.1.11.-) (PubMed:23856622). May have a shorter half-life than isoform TDT-S (PubMed:7556063, PubMed:10878023). {ECO:0000269\|PubMed:10878023, ECO:0000269\|PubMed:11938351, ECO:0000269\|PubMed:7556063}.
Similarity:		Belongs to the DNA polymerase type-X family. {ECO:0000305}.