ID   TOP3B_MOUSE             Reviewed;         862 AA.
AC   Q9Z321;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=DNA topoisomerase 3-beta-1;
DE            EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10131};
DE   AltName: Full=DNA topoisomerase III beta-1;
GN   Name=Top3b; Synonyms=Top3b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Testis;
RX   PubMed=9786843; DOI=10.1074/jbc.273.44.28553;
RA   Seki T., Seki M., Onodera R., Katada T., Enomoto T.;
RT   "Cloning of cDNA encoding a novel mouse DNA topoisomerase III (Topo
RT   IIIbeta) possessing negatively supercoiled DNA relaxing activity, whose
RT   message is highly expressed in the testis.";
RL   J. Biol. Chem. 273:28553-28556(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, Lung, Pancreas, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Releases the supercoiling and torsional tension of DNA
CC       introduced during the DNA replication and transcription by transiently
CC       cleaving and rejoining one strand of the DNA duplex. Introduces a
CC       single-strand break via transesterification at a target site in duplex
CC       DNA. The scissile phosphodiester is attacked by the catalytic tyrosine
CC       of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-
CC       enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free
CC       DNA strand than undergoes passage around the unbroken strand thus
CC       removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH
CC       attacks the covalent intermediate to expel the active-site tyrosine and
CC       restore the DNA phosphodiester backbone (By similarity). Possesses
CC       negatively supercoiled DNA relaxing activity. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC         passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10131};
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01383, ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB013603; BAA34227.1; -; mRNA.
DR   EMBL; BC031723; AAH31723.1; -; mRNA.
DR   CCDS; CCDS27990.1; -.
DR   RefSeq; NP_001313505.1; NM_001326576.1.
DR   RefSeq; NP_035754.1; NM_011624.3.
DR   RefSeq; XP_006522054.1; XM_006521991.3.
DR   RefSeq; XP_006522055.1; XM_006521992.3.
DR   RefSeq; XP_006522057.1; XM_006521994.3.
DR   RefSeq; XP_006522058.1; XM_006521995.2.
DR   RefSeq; XP_017172426.1; XM_017316937.1.
DR   AlphaFoldDB; Q9Z321; -.
DR   SMR; Q9Z321; -.
DR   BioGRID; 204279; 7.
DR   ComplexPortal; CPX-3302; TDRD3-TOP3B type IA topoisomerase complex.
DR   IntAct; Q9Z321; 5.
DR   MINT; Q9Z321; -.
DR   STRING; 10090.ENSMUSP00000023465; -.
DR   iPTMnet; Q9Z321; -.
DR   PhosphoSitePlus; Q9Z321; -.
DR   EPD; Q9Z321; -.
DR   MaxQB; Q9Z321; -.
DR   PaxDb; 10090-ENSMUSP00000023465; -.
DR   ProteomicsDB; 258951; -.
DR   Pumba; Q9Z321; -.
DR   Antibodypedia; 3974; 235 antibodies from 28 providers.
DR   DNASU; 21976; -.
DR   Ensembl; ENSMUST00000023465.16; ENSMUSP00000023465.8; ENSMUSG00000022779.17.
DR   Ensembl; ENSMUST00000232581.2; ENSMUSP00000156132.2; ENSMUSG00000022779.17.
DR   GeneID; 21976; -.
DR   KEGG; mmu:21976; -.
DR   UCSC; uc007yjj.1; mouse.
DR   AGR; MGI:1333803; -.
DR   CTD; 8940; -.
DR   MGI; MGI:1333803; Top3b.
DR   VEuPathDB; HostDB:ENSMUSG00000022779; -.
DR   eggNOG; KOG1957; Eukaryota.
DR   GeneTree; ENSGT00940000156516; -.
DR   HOGENOM; CLU_002929_1_0_1; -.
DR   InParanoid; Q9Z321; -.
DR   OMA; KGKTAYG; -.
DR   OrthoDB; 166270at2759; -.
DR   PhylomeDB; Q9Z321; -.
DR   TreeFam; TF105288; -.
DR   BioGRID-ORCS; 21976; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Top3b; mouse.
DR   PRO; PR:Q9Z321; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q9Z321; Protein.
DR   Bgee; ENSMUSG00000022779; Expressed in choroid plexus epithelium and 265 other cell types or tissues.
DR   ExpressionAtlas; Q9Z321; baseline and differential.
DR   GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR   GO; GO:0140225; C:DNA topoisomerase III-beta-TDRD3 complex; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003916; F:DNA topoisomerase activity; IBA:GO_Central.
DR   GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR   GO; GO:0007059; P:chromosome segregation; IMP:MGI.
DR   GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR   Gene3D; 3.40.50.140; -; 1.
DR   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR   Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR   Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR   InterPro; IPR000380; Topo_IA.
DR   InterPro; IPR003601; Topo_IA_2.
DR   InterPro; IPR023406; Topo_IA_AS.
DR   InterPro; IPR013497; Topo_IA_cen.
DR   InterPro; IPR013824; Topo_IA_cen_sub1.
DR   InterPro; IPR013825; Topo_IA_cen_sub2.
DR   InterPro; IPR013826; Topo_IA_cen_sub3.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034144; TOPRIM_TopoIII.
DR   PANTHER; PTHR11390:SF20; DNA TOPOISOMERASE 3-BETA-1; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   PROSITE; PS00396; TOPO_IA_1; 1.
DR   PROSITE; PS52039; TOPO_IA_2; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
DR   Genevisible; Q9Z321; MM.
PE   1: Evidence at protein level;
KW   DNA-binding; Isomerase; Reference proteome; Topoisomerase.
FT   CHAIN           1..862
FT                   /note="DNA topoisomerase 3-beta-1"
FT                   /id="PRO_0000145193"
FT   DOMAIN          3..153
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   DOMAIN          171..593
FT                   /note="Topo IA-type catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
FT   REGION          820..855
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..844
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        336
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
SQ   SEQUENCE   862 AA;  96949 MW;  D2C05429F79FD5CC CRC64;
     MKTVLMVAEK PSLAQSIAKI LSRGNMSSHK GLNGACSVHK YTGTFAGQPV HFKMTSVCGH
     VMTLDFLGKY NKWDKVDPAE LFSQAPTEKK EANPKLNMVK FLQVEGRGCD YVVLWLDCDK
     EGENICFEVL DAVLPVMNNA HNGEKTVFRA RFSSITDTDI CNAMTRLSEP DHNEALSVDA
     RQELDLRIGC AFTRFQTKYF QGKYGDLDSS LISFGPCQTP TLGFCVERHD KIQSFKPETY
     WVLQAKVHTD KEESLLLDWD RVRVFDWEIA QMFLNMTKLE KEAWVEATSR KEKAKQRPLA
     LNTVEMLRVA SSALGMGPQH AMQIAERLYT QGYISYPRTE TTHYPENFDL KGSLRQQANH
     PYWADSVKQL LAEGINRPRK GHDAGDHPPI TPMKSATEAE LGGDAWRLYE YITRHFIATV
     SHDCKYLQST ISFRIGPEHF TCMGKTVISP GFTEIMPWQS VPLEESLPTC QKGDTFTVGE
     VKMLEKQTSP PDYLTEAELI TLMEKHGIGT DASIPVHINN ICQRNYVTVE SGRRLKPTNL
     GIVLVHGYYK IDAELVLPTI RSAVEKQLNL IAQGKADYHQ VLGHTLDIFK RKFHYFVDSI
     AGMDELMEVS FSPLAATGKP LSRCGKCHRF MKYIQAKPSR LHCSHCDETY TLPQNGTIKL
     YKELRCPLDD FELVLWSSGS RGKSYPLCPY CYNHPPFRDM KKGMGCNECT HPTCQHSLSM
     LGIGQCVECE NGVLVLDPTS GPKWKVACNT CNVVAHCFEN AHRVRVSADT CNTCEAALLD
     VDFNKAKSPL PGNETQHTGC IFCDPVFQEL VELKHAASCH PMHRGGPGRR QGRGRGRGRR
     PPGKPNPRRP KDKMSALAAY FV
//