LOCUS       NP_001380697            1528 aa            linear   ROD 29-MAR-2024
DEFINITION  DNA topoisomerase 2-alpha [Rattus norvegicus].
ACCESSION   NP_001380697
VERSION     NP_001380697.1
DBSOURCE    REFSEQ: accession NM_001393768.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1528)
  AUTHORS   Kawano,S., Kato,Y., Okada,N., Sano,K., Tsutsui,K., Tsutsui,K.M. and
            Ikeda,S.
  TITLE     DNA-binding activity of rat DNA topoisomerase II alpha C-terminal
            domain contributes to efficient DNA catenation in vitro
  JOURNAL   J Biochem 159 (3), 363-369 (2016)
   PUBMED   26527691
  REMARK    GeneRIF: C-terminal domain of rat topo IIalpha is associated with
            efficient DNA catenation in vitro, based on comparison of wild-type
            rat topo IIalpha and its deletion mutants.
REFERENCE   2  (residues 1 to 1528)
  AUTHORS   Mladenovic,M., Stankovic,N., Matic,S., Stanic,S., Mihailovic,M.,
            Mihailovic,V., Katanic,J., Boroja,T. and Vukovic,N.
  TITLE     Newly discovered chroman-2,4-diones neutralize the in vivo DNA
            damage induced by alkylation through the inhibition of
            Topoisomerase IIalpha: A story behind the molecular modeling
            approach
  JOURNAL   Biochem Pharmacol 98 (1), 243-266 (2015)
   PUBMED   26319574
  REMARK    GeneRIF: The genotoxic and antigenotoxic effects of 8
            chroman-2,4-diones are reported; the role of their TOPIIalpha
            inhibitory effect is described.
REFERENCE   3  (residues 1 to 1528)
  AUTHORS   Houlard,M., Godwin,J., Metson,J., Lee,J., Hirano,T. and Nasmyth,K.
  TITLE     Condensin confers the longitudinal rigidity of chromosomes
  JOURNAL   Nat Cell Biol 17 (6), 771-781 (2015)
   PUBMED   25961503
REFERENCE   4  (residues 1 to 1528)
  AUTHORS   Rochette,L., Guenancia,C., Gudjoncik,A., Hachet,O., Zeller,M.,
            Cottin,Y. and Vergely,C.
  TITLE     Anthracyclines/trastuzumab: new aspects of cardiotoxicity and
            molecular mechanisms
  JOURNAL   Trends Pharmacol Sci 36 (6), 326-348 (2015)
   PUBMED   25895646
  REMARK    Review article
REFERENCE   5  (residues 1 to 1528)
  AUTHORS   Ogawa,Y., Kawano,Y., Yamazaki,Y. and Onishi,Y.
  TITLE     Shikonin shortens the circadian period: possible involvement of
            Top2 inhibition
  JOURNAL   Biochem Biophys Res Commun 443 (1), 339-343 (2014)
   PUBMED   24321095
REFERENCE   6  (residues 1 to 1528)
  AUTHORS   Baloch,Z., Cohen,S., Fresa,K. and Coffman,F.D.
  TITLE     Modulation of topoisomerase activities by tumor necrosis factor
  JOURNAL   Cell Immunol 160 (1), 98-103 (1995)
   PUBMED   7842491
REFERENCE   7  (residues 1 to 1528)
  AUTHORS   Adachi,N., Ikeda,H. and Kikuchi,A.
  TITLE     Mutant isolation of mouse DNA topoisomerase II alpha in yeast
  JOURNAL   Nucleic Acids Res 22 (20), 4229-4233 (1994)
   PUBMED   7937150
REFERENCE   8  (residues 1 to 1528)
  AUTHORS   Watanabe,M., Tsutsui,K., Tsutsui,K. and Inoue,Y.
  TITLE     Differential expressions of the topoisomerase II alpha and II beta
            mRNAs in developing rat brain
  JOURNAL   Neurosci Res 19 (1), 51-57 (1994)
   PUBMED   8008235
REFERENCE   9  (residues 1 to 1528)
  AUTHORS   Adachi,N., Miyaike,M., Ikeda,H. and Kikuchi,A.
  TITLE     Characterization of cDNA encoding the mouse DNA topoisomerase II
            that can complement the budding yeast top2 mutation
  JOURNAL   Nucleic Acids Res 20 (20), 5297-5303 (1992)
   PUBMED   1331984
REFERENCE   10 (residues 1 to 1528)
  AUTHORS   Ura,K. and Hirose,S.
  TITLE     Possible role of DNA topoisomerase II on transcription of the
            homeobox gene Hox-2.1 in F9 embryonal carcinoma cells
  JOURNAL   Nucleic Acids Res 19 (22), 6087-6092 (1991)
   PUBMED   1683482
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000010.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643294.41650.1,
                                           SRR26643429.38884.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1528
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..1528
                     /product="DNA topoisomerase 2-alpha"
                     /EC_number="5.6.2.2"
                     /note="DNA topoisomerase II, alpha isozyme; topoisomerase
                     (DNA) II alpha; topoisomerase (DNA) 2 alpha"
                     /calculated_mol_wt=173159
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Region          24..1443
                     /region_name="PTZ00108"
                     /note="DNA topoisomerase 2-like protein; Provisional"
                     /db_xref="CDD:240271"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Region          341..343
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000250|UniProtKB:P11388"
                     /note="propagated from UniProtKB/Swiss-Prot (P41516.1)"
     Site            488
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (P41516.1)"
     Site            491
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (P41516.1)"
     Site            660
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (P41516.1)"
     Site            661
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (P41516.1)"
     Site            722
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (P41516.1)"
     Site            756
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (P41516.1)"
     Site            762
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (P41516.1)"
     Site            803
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:P06786; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            855
                     /site_type="other"
                     /note="Important for DNA bending, intercalates between
                     base pairs of target DNA.
                     /evidence=ECO:0000250|UniProtKB:P06786; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            930
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (P41516.1)"
     Region          989..998
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000250|UniProtKB:P11388"
                     /note="propagated from UniProtKB/Swiss-Prot (P41516.1)"
     Region          1088..1121
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41516.1)"
     Site            1211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1245
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q01320; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1325
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q01320; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1352
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1420
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q01320; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Region          1431..1437
                     /region_name="Interaction with PLSCR1.
                     /evidence=ECO:0000250|UniProtKB:P11388"
                     /note="propagated from UniProtKB/Swiss-Prot (P41516.1)"
     Region          1433..1520
                     /region_name="DTHCT"
                     /note="DTHCT (NUC029) region; pfam08070"
                     /db_xref="CDD:462355"
     Site            1440
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q01320; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1467
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1472
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     Site            1523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (P41516.1)"
     CDS             1..1528
                     /gene="Top2a"
                     /coded_by="NM_001393768.1:110..4696"
                     /db_xref="GeneID:360243"
                     /db_xref="RGD:62048"
ORIGIN      
        1 melsplqpvn enmllnkkkn edgkkrlsve riyqkktqle hillrpdtyi gsvelvtqqm
       61 wvydedvgin yrevtfvpgl ykifdeilvn aadnkqrdpk mscirvtida ennlisiwnn
      121 gkgipvvehk vekmyvpali fgqlltssny dddekkvtgg rngygaklcn ifstkftvet
      181 asreykkmfk qtwmdnmgra gdmelkpfsg edytcitfqp dlskfkmqsl dkdivalmvr
      241 raydiagstk dvkvflngnr lpvkgfrsyv dmylkdkvde tgnalkvvhe qvnprwevcl
      301 tmsekgfqqi sfvnsiatsk ggrhvdyvad qivsklvdvv kkknkggvav kahqvknhmw
      361 ifvnalienp tfdsqtkenm tlqaksfgst cqlsekfika aigcgivesi lnwvkfkaqi
      421 qlnkkcsavk hnrikgipkl ddandagsrn saectlilte gdsaktlavs glgvvgrdky
      481 gvfplrgkil nvreashkqi menaeinnii kivglqykkn yededslktl rygkimimtd
      541 qdqdgshikg llinfihhnw psllrhrfle efitpivkvs knkqeiafys lpefeewksa
      601 npnhkkwkvk yykglgtsts keakeyfanm krhriqfkys gpeddaaisl afskkqvddr
      661 kewltnfmed rrqrkllglp edylygqttm yltyndfink elilfsnsdn ersipsmvdg
      721 lkpgqrkvlf tcfkrndkre vkvaqlagsv aemssyhhge mslmmtiinl aqnfvgsnnl
      781 nllqpigqfg trlhggkdsa spryiftmls plarllfpsk ddhtlrflyd dnqrvepewy
      841 ipiipmvlin gaegigtgws ckipnfdvre vvnnirrlld geeplpmlps yknykgtiee
      901 lasnqyving evailnstti eitelpirtw tqtykeqvle pmlngtektp plitdyreyh
      961 tdttvkfvik mteeklaeae rvglhkvfkl qtsltcnsmv lfdhvgclkk ydtvldilrd
     1021 ffelrlkyyg lrkewllgml gaessklnnq arfilekidg kivienkpkk elikvliqrg
     1081 ydsdpvkawk eaqqkvpeee eneeneeses essspaaesg ptfnylldmp lwyltkekkd
     1141 elckqrdeke qelntlkkkt psdlwkedla afveelevve akekqdeqvg lpgkgvkakg
     1201 kkaqisevlp spvgkrvipq vtmemraeae kkirrkikse nvegtpaedg aepgglrqrl
     1261 ekrqkrepgt rakkqttlpf kpikkgkkkn pwsdsesdms snesnfdvpp rekepriaat
     1321 kakftadlds dddfsgldek dededffpld dtppktkmpp kntkkalkpq ksstsvdles
     1381 dgkdsvpasp gasaadvpae tepskpsskq tvgvkrtitk gqsltstagt kkravpketk
     1441 sdsalnahvs kkpapakakn srkrkpsssd ssdsefekai skgatskkpk geerdfhvdl
     1501 ddtvapraks grarkpikyl eesdddlf
//
