ID   TOP1_CRIGR              Reviewed;         767 AA.
AC   Q07050;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=DNA topoisomerase 1;
DE            EC=5.99.1.2;
DE   AltName: Full=DNA topoisomerase I;
GN   Name=TOP1; Synonyms=TOP-1;
OS   Cricetulus griseus (Chinese hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94064611; PubMed=8244980;
RA   Tanizawa A., Bertrand R., Kohlhagen G., Tabuchi A., Jenkins J.,
RA   Pommier Y.;
RT   "Cloning of Chinese hamster DNA topoisomerase I cDNA and
RT   identification of a single point mutation responsible for camptothecin
RT   resistance.";
RL   J. Biol. Chem. 268:25463-25468(1993).
CC   -!- FUNCTION: The reaction catalyzed by topoisomerases leads to the
CC       conversion of one topological isomer of DNA to another.
CC   -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded
CC       DNA, followed by passage and rejoining.
CC   -!- ENZYME REGULATION: Specifically inhibited by camptothecin (CPT), a
CC       plant alkaloid with antitumor activity.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm.
CC       Note=Diffuse nuclear localization with some enrichment in
CC       nucleoli. On CPT treatment, cleared from nucleoli into
CC       nucleoplasm. Sumolyated forms found in both nucleoplasm and
CC       nucleoli (By similarity).
CC   -!- PTM: Sumoylated. Lys-119 is the main site of sumoylation.
CC       Sumoylation plays a role in partitioning TOP1 between nucleoli and
CC       nucleoplasm. Levels are dramatically increased on camptothecin
CC       (CPT) treatment (By similarity).
CC   -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC       negative and positive supercoils, whereas prokaryotic enzymes
CC       relax only negative supercoils.
CC   -!- MISCELLANEOUS: When a topoisomerase transiently breaks a DNA
CC       backbone bond, it simultaneously forms a protein-DNA link, in
CC       which a tyrosyl oxygen in the enzyme is joined to a DNA phosphorus
CC       at one end of the enzyme-severed DNA strand.
CC   -!- SIMILARITY: Belongs to the eukaryotic type I topoisomerase family.
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DR   EMBL; Z21624; CAA79747.1; -; mRNA.
DR   EMBL; Z21625; CAA79748.1; -; mRNA.
DR   PIR; A49546; A49546.
DR   HSSP; P11387; 1EJ9.
DR   SMR; Q07050; 203-767.
DR   HOVERGEN; Q07050; -.
DR   BRENDA; 5.99.1.2; 18.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0003917; F:DNA topoisomerase type I activity; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; ISS:UniProtKB.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0006268; P:DNA unwinding during replication; IEA:InterPro.
DR   InterPro; IPR018521; TopoI_AS.
DR   InterPro; IPR001631; TopoI_C.
DR   InterPro; IPR013499; TopoI_C_euk.
DR   InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR   InterPro; IPR014727; TopoI_cat_a/b-sub_euk.
DR   InterPro; IPR013500; TopoI_cat_euk.
DR   InterPro; IPR013030; TopoI_DNA-bd_mixed-a/b_euk.
DR   InterPro; IPR008336; TopoI_DNA_bd_euk.
DR   Gene3D; G3DSA:3.90.15.10; TopoI_cat_a-hlx-sub_euk; 1.
DR   Gene3D; G3DSA:1.10.132.10; TopoI_cat_a/b-sub_euk; 1.
DR   Gene3D; G3DSA:2.170.11.10; TopoI_DNA-bd_mixed-a/b_euk; 1.
DR   Pfam; PF01028; Topoisom_I; 1.
DR   Pfam; PF02919; Topoisom_I_N; 1.
DR   PRINTS; PR00416; EUTPISMRASEI.
DR   SMART; SM00435; TOPEUc; 1.
DR   PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; DNA-binding; Isomerase; Isopeptide bond;
KW   Nucleotide-binding; Nucleus; Topoisomerase; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    767       DNA topoisomerase 1.
FT                                /FTId=PRO_0000145200.
FT   COMPBIAS     23    206       Lys-rich.
FT   ACT_SITE    725    725       O-(3'-phospho-DNA)-tyrosine intermediate
FT                                (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   CROSSLNK    105    105       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO)
FT                                (Probable).
FT   CROSSLNK    119    119       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    155    155       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO)
FT                                (Probable).
FT   VARIANT     505    505       S -> G (in CPT-resistant cell).
SQ   SEQUENCE   767 AA;  90868 MW;  347336D424EF35A9 CRC64;
     MSGDHLHNDS QIEADFRLND SHKHKDKHKD REHRHKEHKK DKEKDREKSK HSNSEHKDSE
     KKHKEKEKTK HKDGSSEKHK DKHKDRDKEK RKEEKIRASG DAKIKKEKEN GFSSPPRIKD
     EPDDDGYFAP PKEDIKPLKR PRDEDDADYK PKKIKTEDIK KEKKRKLEEE EDGKLKKTKN
     KDKDKKGAES DNKKKKPKKE EEQKWKWWEE ERYPEGIKWK FLEHKGPVFA PPYEPLPEGV
     KFYYDGKVMK LSPKAEEVAT FFAKMLDHEY TTKEIFRKNF FKDWRKEMTN DEKNVITNLS
     KCDFTQMSQY FKDQSEARKQ MSKEEKLKIK EENEKLLKEY GFCVMDNHRE RIANFKIEPP
     GLFRGRGNHP KMGMLKRRIM PEDIIINCSK DAKVPSPPPG HKWKEVRHDN KVTWLVSWTE
     NIQGSIKYIM LNPSSRIKGE KDWQKYETAR RLKKCVDKIR NQYREDWKSK EMKVRQRAVA
     LYFIDKLALR AGNEKEEGET ADTVSCCSLR VEHINLHPEL DGQEYVVEFD FPGKDSIRYY
     NKVPVEKRVF KNLQLFMENK QPEDDLFDRL NTGILNKHLQ DLMEGLTAKV FRTYNASITL
     QQQLKELTAP DENVPAKILS YNRANRAVAI LCNHQRAPPK TFEKSMMNLQ SKIDAKKDQL
     ADARRDLKSA KADAKVMKDA KTKKVVESKK KAVQRLEEQL MKLEVQATDR EENKQIALGT
     SKLNYLDPRI TVAWCKKWGV PIEKIYNKTQ REKFAWAIDM TDEDYEF
//