TYDP1_RAT
ID TYDP1_RAT Reviewed; 609 AA.
AC Q4G056;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Tyrosyl-DNA phosphodiesterase 1;
DE Short=Tyr-DNA phosphodiesterase 1;
DE EC=3.1.4.- {ECO:0000250|UniProtKB:Q9NUW8};
GN Name=Tdp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; THR-148 AND SER-149, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: DNA repair enzyme that can remove a variety of covalent
CC adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving
CC rise to DNA with a free 3' phosphate. Catalyzes the hydrolysis of dead-
CC end complexes between DNA and the topoisomerase I active site tyrosine
CC residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA
CC double-strand breaks due to DNA damage by radiation and free radicals.
CC Acts on blunt-ended double-strand DNA breaks and on single-stranded
CC DNA. Has low 3'exonuclease activity and can remove a single nucleoside
CC from the 3'end of DNA and RNA molecules with 3'hydroxyl groups. Has no
CC exonuclease activity towards DNA or RNA with a 3'phosphate (By
CC similarity). {ECO:0000250|UniProtKB:Q9NUW8}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9NUW8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NUW8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NUW8}.
CC -!- SIMILARITY: Belongs to the tyrosyl-DNA phosphodiesterase family.
CC {ECO:0000305}.
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DR EMBL; BC098739; AAH98739.1; -; mRNA.
DR RefSeq; NP_001026827.1; NM_001031657.1.
DR AlphaFoldDB; Q4G056; -.
DR SMR; Q4G056; -.
DR STRING; 10116.ENSRNOP00000005167; -.
DR iPTMnet; Q4G056; -.
DR PhosphoSitePlus; Q4G056; -.
DR PaxDb; Q4G056; -.
DR PRIDE; Q4G056; -.
DR GeneID; 314380; -.
DR KEGG; rno:314380; -.
DR UCSC; RGD:1309618; rat.
DR CTD; 55775; -.
DR RGD; 1309618; Tdp1.
DR eggNOG; KOG2031; Eukaryota.
DR HOGENOM; CLU_010413_4_0_1; -.
DR InParanoid; Q4G056; -.
DR PhylomeDB; Q4G056; -.
DR TreeFam; TF105989; -.
DR BRENDA; 3.1.4.1; 5301.
DR Reactome; R-RNO-5693571; Nonhomologous End-Joining (NHEJ).
DR PRO; PR:Q4G056; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q4G056; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0017005; F:3'-tyrosyl-DNA phosphodiesterase activity; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:RGD.
DR GO; GO:0006281; P:DNA repair; ISO:RGD.
DR GO; GO:0006302; P:double-strand break repair; ISO:RGD.
DR GO; GO:0000012; P:single strand break repair; ISO:RGD.
DR InterPro; IPR010347; Tdp1.
DR PANTHER; PTHR12415; PTHR12415; 1.
DR Pfam; PF06087; Tyr-DNA_phospho; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA damage; DNA repair; Exonuclease; Hydrolase; Nuclease;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..609
FT /note="Tyrosyl-DNA phosphodiesterase 1"
FT /id="PRO_0000340098"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..404
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT COMPBIAS 28..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT ACT_SITE 494
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT BINDING 496
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT SITE 519
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ37"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 148
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 609 AA; 68632 MW; 20425F3A520BC4B9 CRC64;
MSQESSYGKW TISSSDDSED EKPKPVKPST SSGPQAGQGV SKEPTYTCSE ARKAAHKRQI
SPVKFNNTDS VLPHKKQKMD SPEGLGWCLS SSDDEQQPDV TQQEQPKGVP PQEKKYAPSA
NVTTAQKVED RSPPDSHRAQ RADEEYETSG EGQDIWDMLD KENPFQFYLT RVSGIKAKYN
SKALHIKDIL SPLFGTLVSS AQFNYCFDVN WLIKQYPPEF RKKPILLVHG DKREAKADLH
AQAKPYANIS LCQAKLDIAF GTHHTKMMLL LYEEGLRVVI HTSNLIREDW HQKTQGIWLS
PLYPRIYQGN HTSGESSTHF KADLTSYLMA YNAPPLQEWI DIIQEHDLSE TNVYLIGSTP
GRFQGSHKDN WGHFRLRKLL QAHAPSAPRG ECWPVVGQFS SIGSLGPDES KWLCSEFKES
LLAVREEGRT PGRSAVPLHL IYPSVENVRT SLEGYPAGGS LPYGIQTAEK QRWLHPYFHK
WSAETSGRSN AMPHIKTYMR PSPDFSKLAW FLVTSANLSK AAWGALEKNG AQLMIRSYEL
GVLFLPSAFG LDTFKVKQKF FSSSSEPMAS FPVPYDLPPE LYGSKDRPWI WNIPYVKAPD
THGNMWVPS
