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DNA topoisomerase 1 (EC 5.99.1.2) (DNA topoisomerase I)

 TOP1_RAT                Reviewed;         767 AA.
Q9WUL0;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
22-NOV-2017, entry version 123.
RecName: Full=DNA topoisomerase 1;
EC=5.99.1.2;
AltName: Full=DNA topoisomerase I;
Name=Top1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Glioblastoma;
Pourquier P., Gioffre C., Ueng L.-M., Robert J., Pommier Y.;
"Sequencing of rat topoisomerase I between sensitive and camptothecin-
resistant C6 glioblastoma cell lines.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-114, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Releases the supercoiling and torsional tension of DNA
introduced during the DNA replication and transcription by
transiently cleaving and rejoining one strand of the DNA duplex.
Introduces a single-strand break via transesterification at a
target site in duplex DNA. The scissile phosphodiester is attacked
by the catalytic tyrosine of the enzyme, resulting in the
formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the
expulsion of a 5'-OH DNA strand. The free DNA strand then rotates
around the intact phosphodiester bond on the opposing strand, thus
removing DNA supercoils. Finally, in the religation step, the DNA
5'-OH attacks the covalent intermediate to expel the active-site
tyrosine and restore the DNA phosphodiester backbone. Regulates
the alternative splicing of tissue factor (F3) pre-mRNA in
endothelial cells. Involved in the circadian transcription of the
core circadian clock component ARNTL/BMAL1 by altering the
chromatin structure around the ROR response elements (ROREs) on
the ARNTL/BMAL1 promoter. {ECO:0000250|UniProtKB:P11387}.
-!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded
DNA, followed by passage and rejoining. {ECO:0000255|PROSITE-
ProRule:PRU10130}.
-!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P11387}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000250|UniProtKB:P11387}. Nucleus, nucleoplasm
{ECO:0000250|UniProtKB:P11387}. Note=Diffuse nuclear localization
with some enrichment in nucleoli. On CPT treatment, cleared from
nucleoli into nucleoplasm. Sumoylated forms found in both
nucleoplasm and nucleoli. {ECO:0000250|UniProtKB:P11387}.
-!- PTM: Sumoylated. Lys-119 is the main site of sumoylation.
Sumoylation plays a role in partitioning TOP1 between nucleoli and
nucleoplasm. Levels are dramatically increased on camptothecin
(CPT) treatment. {ECO:0000250|UniProtKB:P11387}.
-!- PTM: Phosphorylation at Ser-508 by CK2 increases binding to
supercoiled DNA and sensitivity to camptothecin.
{ECO:0000250|UniProtKB:P11387}.
-!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
negative and positive supercoils, whereas prokaryotic enzymes
relax only negative supercoils.
-!- SIMILARITY: Belongs to the type IB topoisomerase family.
{ECO:0000305}.
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EMBL; AF140782; AAD30137.1; -; mRNA.
RefSeq; NP_072137.1; NM_022615.1.
UniGene; Rn.91572; -.
ProteinModelPortal; Q9WUL0; -.
SMR; Q9WUL0; -.
BioGrid; 249131; 1.
IntAct; Q9WUL0; 1.
BindingDB; Q9WUL0; -.
ChEMBL; CHEMBL1075164; -.
iPTMnet; Q9WUL0; -.
PhosphoSitePlus; Q9WUL0; -.
PRIDE; Q9WUL0; -.
GeneID; 64550; -.
KEGG; rno:64550; -.
UCSC; RGD:621246; rat.
CTD; 7150; -.
RGD; 621246; Top1.
HOGENOM; HOG000105469; -.
HOVERGEN; HBG007988; -.
InParanoid; Q9WUL0; -.
KO; K03163; -.
PhylomeDB; Q9WUL0; -.
TreeFam; TF105281; -.
PRO; PR:Q9WUL0; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0001651; C:dense fibrillar component; IDA:RGD.
GO; GO:0009330; C:DNA topoisomerase complex (ATP-hydrolyzing); ISO:RGD.
GO; GO:0001650; C:fibrillar center; IDA:RGD.
GO; GO:0005730; C:nucleolus; ISO:RGD.
GO; GO:0005654; C:nucleoplasm; ISO:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0000932; C:P-body; ISO:RGD.
GO; GO:0043204; C:perikaryon; ISO:RGD.
GO; GO:0032993; C:protein-DNA complex; ISO:RGD.
GO; GO:0031298; C:replication fork protection complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; ISO:RGD.
GO; GO:0003682; F:chromatin binding; ISO:RGD.
GO; GO:0031490; F:chromatin DNA binding; IDA:RGD.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:RGD.
GO; GO:0003917; F:DNA topoisomerase type I activity; IDA:RGD.
GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
GO; GO:0032403; F:protein complex binding; IDA:RGD.
GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
GO; GO:0003723; F:RNA binding; ISO:RGD.
GO; GO:0003697; F:single-stranded DNA binding; ISO:RGD.
GO; GO:0097100; F:supercoiled DNA binding; ISO:RGD.
GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
GO; GO:0071373; P:cellular response to luteinizing hormone stimulus; IEP:RGD.
GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0007623; P:circadian rhythm; ISO:RGD.
GO; GO:0006260; P:DNA replication; ISO:RGD.
GO; GO:0006265; P:DNA topological change; IDA:RGD.
GO; GO:0040016; P:embryonic cleavage; ISO:RGD.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
GO; GO:0051591; P:response to cAMP; IEP:RGD.
GO; GO:0042493; P:response to drug; ISO:RGD.
GO; GO:0010332; P:response to gamma radiation; IEP:RGD.
GO; GO:0009266; P:response to temperature stimulus; IEP:RGD.
GO; GO:0009303; P:rRNA transcription; IMP:RGD.
CDD; cd00659; Topo_IB_C; 1.
Gene3D; 1.10.10.41; -; 1.
Gene3D; 1.10.132.10; -; 1.
Gene3D; 2.170.11.10; -; 1.
Gene3D; 3.90.15.10; -; 1.
InterPro; IPR011010; DNA_brk_join_enz.
InterPro; IPR013034; DNA_topo_DNA_db_N_dom1.
InterPro; IPR013030; DNA_topo_DNA_db_N_dom2.
InterPro; IPR001631; TopoI.
InterPro; IPR018521; TopoI_AS.
InterPro; IPR025834; TopoI_C_dom.
InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
InterPro; IPR014727; TopoI_cat_a/b-sub_euk.
InterPro; IPR013500; TopoI_cat_euk.
InterPro; IPR008336; TopoI_DNA-bd_euk.
InterPro; IPR036202; TopoI_DNA-bd_euk_N_sf.
InterPro; IPR013499; TopoI_euk.
Pfam; PF14370; Topo_C_assoc; 1.
Pfam; PF01028; Topoisom_I; 1.
Pfam; PF02919; Topoisom_I_N; 1.
PRINTS; PR00416; EUTPISMRASEI.
SMART; SM00435; TOPEUc; 1.
SUPFAM; SSF56349; SSF56349; 2.
SUPFAM; SSF56741; SSF56741; 1.
PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
1: Evidence at protein level;
Acetylation; Biological rhythms; Complete proteome; DNA-binding;
Isomerase; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Topoisomerase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P11387}.
CHAIN 2 767 DNA topoisomerase 1.
/FTId=PRO_0000145203.
REGION 427 428 Interaction with DNA. {ECO:0000250}.
REGION 490 495 Interaction with DNA. {ECO:0000250}.
REGION 587 589 Interaction with DNA. {ECO:0000250}.
COMPBIAS 23 206 Lys-rich.
ACT_SITE 725 725 O-(3'-phospho-DNA)-tyrosine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10130}.
SITE 318 318 Interaction with DNA. {ECO:0000250}.
SITE 366 366 Interaction with DNA. {ECO:0000250}.
SITE 414 414 Interaction with DNA. {ECO:0000250}.
SITE 445 445 Interaction with DNA. {ECO:0000250}.
SITE 503 503 Interaction with DNA. {ECO:0000250}.
SITE 534 534 Interaction with DNA. {ECO:0000250}.
SITE 576 576 Interaction with DNA. {ECO:0000250}.
SITE 634 634 Interaction with DNA. {ECO:0000250}.
SITE 652 652 Interaction with DNA. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P11387}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:P11387}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 59 59 Phosphoserine.
{ECO:0000250|UniProtKB:P11387}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 174 174 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q04750}.
MOD_RES 282 282 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11387}.
MOD_RES 508 508 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 103 103 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 105 105 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000305}.
CROSSLNK 105 105 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 119 119 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 119 119 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 119 119 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 136 136 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 150 150 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 155 155 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000305}.
CROSSLNK 155 155 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 160 160 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 166 166 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 174 174 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 206 206 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 338 338 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 551 551 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 644 644 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 702 702 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P11387}.
CROSSLNK 714 714 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P11387}.
SEQUENCE 767 AA; 90760 MW; 79103F06DA61D73D CRC64;
MSGDHLHNDS QIEADFRLND SHKHKDKHKD REHRHKEHKK DKDKDREKSK HSNSEHKDSE
KKHKEKEKTK HKDGSSDKHK DKHKDRDKEK RKEEKIRAAG DAKIKKEKEN GFSSPPRIKD
EPEDDGYFAP PKEDIKPLKR PRDEDDADYK PKKIKTEDIK KEKKRKLEEE EDGKLKKPKN
KDKDKKVAEP DNKKKKAKKE EEQKWKWWEE ERYPEGIKWK FLEHKGPVFA PPYEPLPEGV
KFYYDGKVMK LSPKAEEVAT FFAKMLDHEY TTKEIFRKNF FKDWRKEMTN DEKNTITNLS
KCDFTQMSQY FKAQSEARKQ MSKEEKLKIK EENEKLLKEY GFCVMDNHRE RIANFKIEPP
GLFRGRGNHP KMGMLKRRIM PEDIIINCSK DAKVPSPPPG HKWKEVRHDN KVTWLVSWTE
NIQGSIKYIM LNPSSRIKGE KDWQKYETAR RLKKCVDKIR NQYREDWKSK EMKVRQRAVA
LYFIDKLALR AGNEKEEGET ADTVGCCSLR VEHINLHPEL DGQEYVVEFD FPGKDSIRYY
NKVPVEKRVF KNLQLFMENK QPEDDLFDRL NTGILNKHLQ DLMEGLTAKV FRTYNASITL
QQQLKELTAP DENVPAKILS YNRANRAVAI LCNHQRAPPK TFEKSMMNLQ SKIDAKKDQL
ADARKDLKSA KADAKVMKDA KTKKVVESKK KAVQRLEEQL MKLEVQATDR EENKQIALGT
SKLNYLDPRI TVAWCKKWGV PIEKIYNKTQ REKFAWAIDM TDEDYEF


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