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Tyrosyl-DNA phosphodiesterase 2 (Tyr-DNA phosphodiesterase 2) (EC 3.1.4.-) (5'-tyrosyl-DNA phosphodiesterase) (5'-Tyr-DNA phosphodiesterase) (TRAF and TNF receptor-associated protein)

 TYDP2_BOVIN             Reviewed;         364 AA.
A7YWI9;
15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 1.
28-MAR-2018, entry version 65.
RecName: Full=Tyrosyl-DNA phosphodiesterase 2;
Short=Tyr-DNA phosphodiesterase 2;
EC=3.1.4.-;
AltName: Full=5'-tyrosyl-DNA phosphodiesterase;
Short=5'-Tyr-DNA phosphodiesterase;
AltName: Full=TRAF and TNF receptor-associated protein;
Name=TDP2; Synonyms=TTRAP;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Basal ganglia;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: DNA repair enzyme that can remove a variety of covalent
adducts from DNA through hydrolysis of a 5'-phosphodiester bond,
giving rise to DNA with a free 5' phosphate. Catalyzes the
hydrolysis of dead-end complexes between DNA and the topoisomerase
2 (TOP2) active site tyrosine residue. The 5'-tyrosyl DNA
phosphodiesterase activity can enable the repair of TOP2-induced
DNA double-strand breaks/DSBs without the need for nuclease
activity, creating a 'clean' DSB with 5'-phosphate termini that
are ready for ligation. Thereby, protects the transcription of
many genes involved in neurological development and maintenance
from the abortive activity of TOP2. Hydrolyzes 5'-
phosphoglycolates on protruding 5' ends on DSBs due to DNA damage
by radiation and free radicals. Has preference for single-stranded
DNA or duplex DNA with a 4 base pair overhang as substrate. Has
also 3'-tyrosyl DNA phosphodiesterase activity, but less
efficiently and much slower than TDP1. Constitutes the major if
not only 5'-tyrosyl-DNA phosphodiesterase in cells. Also acts as
an adapter by participating in the specific activation of
MAP3K7/TAK1 in response to TGF-beta: associates with components of
the TGF-beta receptor-TRAF6-TAK1 signaling module and promotes
their ubiquitination dependent complex formation. Involved in non-
canonical TGF-beta induced signaling routes. May also act as a
negative regulator of ETS1 and may inhibit NF-kappa-B activation.
Acts as a regulator of ribosome biogenesis following stress.
{ECO:0000250|UniProtKB:O95551}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Magnesium. Can use other divalent cations as cofactor in
vitro, such as manganese. {ECO:0000250};
-!- SUBUNIT: Interacts with TRAF2, TRAF3, TRAF5, TRAF6, TNFRSF8/CD30,
TNFRSF5/CD40, TNFRSF1B/TNF-R75, ETS1, ETS2, FLI1, SMAD3 and
ACVR1B/ALK4. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, PML body
{ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Localizes to
nucleolar cavities following stress; localization to nucleolus is
dependent on PML protein. {ECO:0000250}.
-!- PTM: Ubiquitinated by TRAF6. {ECO:0000250}.
-!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
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EMBL; BC134603; AAI34604.1; -; mRNA.
RefSeq; NP_001098811.1; NM_001105341.1.
UniGene; Bt.13626; -.
ProteinModelPortal; A7YWI9; -.
SMR; A7YWI9; -.
STRING; 9913.ENSBTAP00000000472; -.
PaxDb; A7YWI9; -.
Ensembl; ENSBTAT00000000472; ENSBTAP00000000472; ENSBTAG00000000365.
GeneID; 507579; -.
KEGG; bta:507579; -.
CTD; 51567; -.
VGNC; VGNC:35714; TDP2.
eggNOG; KOG2756; Eukaryota.
eggNOG; ENOG410XP85; LUCA.
GeneTree; ENSGT00390000014242; -.
HOVERGEN; HBG079625; -.
InParanoid; A7YWI9; -.
KO; K19619; -.
OMA; QCFLAEN; -.
OrthoDB; EOG091G0FBI; -.
TreeFam; TF314813; -.
Reactome; R-BTA-5693571; Nonhomologous End-Joining (NHEJ).
Proteomes; UP000009136; Chromosome 23.
Bgee; ENSBTAG00000000365; -.
GO; GO:0016235; C:aggresome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0016605; C:PML body; ISS:UniProtKB.
GO; GO:0070260; F:5'-tyrosyl-DNA phosphodiesterase activity; ISS:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
GO; GO:0036317; F:tyrosyl-RNA phosphodiesterase activity; IEA:Ensembl.
GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
GO; GO:0048666; P:neuron development; ISS:UniProtKB.
Gene3D; 3.60.10.10; -; 1.
InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
InterPro; IPR005135; Endo/exonuclease/phosphatase.
InterPro; IPR009060; UBA-like_sf.
Pfam; PF03372; Exo_endo_phos; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF56219; SSF56219; 1.
2: Evidence at transcript level;
Acetylation; Complete proteome; DNA damage; DNA repair; Hydrolase;
Isopeptide bond; Magnesium; Metal-binding; Nuclease; Nucleus;
Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 364 Tyrosyl-DNA phosphodiesterase 2.
/FTId=PRO_0000390449.
ACT_SITE 353 353 Proton acceptor. {ECO:0000250}.
METAL 122 122 Magnesium. {ECO:0000250}.
METAL 154 154 Magnesium. {ECO:0000250}.
METAL 264 264 Magnesium. {ECO:0000250}.
METAL 266 266 Magnesium. {ECO:0000250}.
METAL 352 352 Magnesium. {ECO:0000250}.
METAL 353 353 Magnesium. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:O95551}.
MOD_RES 88 88 Phosphothreonine; by ACVR1B.
{ECO:0000250|UniProtKB:O95551}.
MOD_RES 92 92 Phosphothreonine; by ACVR1B.
{ECO:0000250|UniProtKB:O95551}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000250|UniProtKB:O95551}.
CROSSLNK 23 23 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95551}.
SEQUENCE 364 AA; 40826 MW; 1BEF10BA57C1199A CRC64;
MERNSGPEAG PEAELEEGEP EVKKRKLMCV EFASVASCDA AVAQCYLAEN DWEMERALNS
YFEPAVEESA SESRPESLSE PGSCVDLTKE ETNDSISSKT STSEDKSVQQ EDGSVFSFIT
WNIDGLDMNN LLERARGVCS YLTLYSPDVI FLQEVIPPYY AYLKKKASSY KIITGREEGY
FTAIMLKKSR VKFKSQEIIP FPNTQMMRNL LCVHVSVSGN ELCLMTSHLE STRGHAKERM
NQFKMVLEKM QEAPGSATVI FAGDTNLRDQ EVTKCGGLPN NILDVWEFLG KPKHCQYTWD
TQMNSNLGIA ANCKLRFDRI FFRAAAEGGH IIPQSLDLLG LEKLDCGRFP SDHWGLLCTL
DVIL


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