KU80_ARATH
ID KU80_ARATH Reviewed; 680 AA.
AC Q9FQ09; Q9C7Z3; Q9LNF5;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=ATP-dependent DNA helicase 2 subunit KU80;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent DNA helicase 2 subunit 2;
DE AltName: Full=ATP-dependent DNA helicase II 80 kDa subunit;
GN Name=KU80; OrderedLocusNames=At1g48050; ORFNames=F21D18.26, T2J15.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH KU70.
RC STRAIN=cv. Columbia;
RX PubMed=12148535; DOI=10.1046/j.1365-313x.2002.01258.x;
RA Tamura K., Adachi Y., Chiba K., Oguchi K., Takahashi H.;
RT "Identification of Ku70 and Ku80 homologues in Arabidopsis thaliana:
RT evidence for a role in the repair of DNA double-strand breaks.";
RL Plant J. 29:771-781(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH KU70.
RX PubMed=12032094; DOI=10.1093/emboj/21.11.2819;
RA Riha K., Watson J.M., Parkey J., Shippen D.E.;
RT "Telomere length deregulation and enhanced sensitivity to genotoxic stress
RT in Arabidopsis mutants deficient in Ku70.";
RL EMBO J. 21:2819-2826(2002).
RN [5]
RP FUNCTION, INTERACTION WITH KU70, AND DISRUPTION PHENOTYPE.
RX PubMed=12182708; DOI=10.1046/j.1365-313x.2002.01370.x;
RA West C.E., Waterworth W.M., Story G.W., Sunderland P.A., Jiang Q.,
RA Bray C.M.;
RT "Disruption of the Arabidopsis AtKu80 gene demonstrates an essential role
RT for AtKu80 protein in efficient repair of DNA double-strand breaks in
RT vivo.";
RL Plant J. 31:517-528(2002).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12615949; DOI=10.1105/tpc.008623;
RA Gallego M.E., Jalut N., White C.I.;
RT "Telomerase dependence of telomere lengthening in Ku80 mutant
RT Arabidopsis.";
RL Plant Cell 15:782-789(2003).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=12753583; DOI=10.1046/j.1365-313x.2003.01738.x;
RA Friesner J., Britt A.B.;
RT "Ku80- and DNA ligase IV-deficient plants are sensitive to ionizing
RT radiation and defective in T-DNA integration.";
RL Plant J. 34:427-440(2003).
RN [8]
RP INTERACTION WITH WEX.
RX PubMed=16396834; DOI=10.1093/nar/gki984;
RA Li B., Conway N., Navarro S., Comai L., Comai L.;
RT "A conserved and species-specific functional interaction between the Werner
RT syndrome-like exonuclease atWEX and the Ku heterodimer in Arabidopsis.";
RL Nucleic Acids Res. 33:6861-6867(2005).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16380432; DOI=10.1073/pnas.0506437103;
RA Li J., Vaidya M., White C., Vainstein A., Citovsky V., Tzfira T.;
RT "Involvement of KU80 in T-DNA integration in plant cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:19231-19236(2005).
RN [10]
RP INDUCTION BY HEAT SHOCK.
RX PubMed=18515112; DOI=10.1016/j.bbagrm.2008.05.002;
RA Liu P.F., Wang Y.K., Chang W.C., Chang H.Y., Pan R.L.;
RT "Regulation of Arabidopsis thaliana Ku genes at different developmental
RT stages under heat stress.";
RL Biochim. Biophys. Acta 1779:402-407(2008).
CC -!- FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase.
CC Involved in DNA non-homologous end joining (NHEJ) required for double-
CC strand break repair. When associated with KU70, binds to double-
CC stranded telomeric and non-telomeric DNA sequences, but not to single-
CC stranded DNA. Plays a role in maintaining telomere length. Acts as a
CC negative regulator of telomerase. Binds to and recombines double-
CC stranded T-DNA molecules. {ECO:0000269|PubMed:12032094,
CC ECO:0000269|PubMed:12182708, ECO:0000269|PubMed:12615949,
CC ECO:0000269|PubMed:16380432}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Heterodimer with KU70. Interacts with WEX.
CC {ECO:0000269|PubMed:12032094, ECO:0000269|PubMed:12148535,
CC ECO:0000269|PubMed:12182708, ECO:0000269|PubMed:16396834}.
CC -!- INTERACTION:
CC Q9FQ09; Q84LH3: WEX; NbExp=2; IntAct=EBI-926593, EBI-926580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12148535}. Cytoplasm
CC {ECO:0000269|PubMed:12148535}. Note=Predominantly in the nucleus.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:12032094, ECO:0000269|PubMed:12148535}.
CC -!- INDUCTION: Up-regulated in response to induction of double-strand
CC breaks. Down-regulated by heat shock. {ECO:0000269|PubMed:12148535,
CC ECO:0000269|PubMed:18515112}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions. Hypersensitivity to ionising radiation (IR) and to DNA-
CC damaging agents. Longer telomeres. Defective in T-DNA integration.
CC {ECO:0000269|PubMed:12182708, ECO:0000269|PubMed:12615949,
CC ECO:0000269|PubMed:12753583, ECO:0000269|PubMed:16380432}.
CC -!- SIMILARITY: Belongs to the ku80 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79532.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51535.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF283758; AAG44851.1; -; mRNA.
DR EMBL; AC023673; AAF79532.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC051631; AAG51535.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32242.1; -; Genomic_DNA.
DR PIR; G96520; G96520.
DR RefSeq; NP_564520.1; NM_103701.2.
DR AlphaFoldDB; Q9FQ09; -.
DR SMR; Q9FQ09; -.
DR BioGRID; 26448; 7.
DR IntAct; Q9FQ09; 1.
DR STRING; 3702.AT1G48050.1; -.
DR iPTMnet; Q9FQ09; -.
DR PaxDb; Q9FQ09; -.
DR PRIDE; Q9FQ09; -.
DR ProteomicsDB; 250714; -.
DR EnsemblPlants; AT1G48050.1; AT1G48050.1; AT1G48050.
DR GeneID; 841223; -.
DR Gramene; AT1G48050.1; AT1G48050.1; AT1G48050.
DR KEGG; ath:AT1G48050; -.
DR Araport; AT1G48050; -.
DR TAIR; locus:2023757; AT1G48050.
DR eggNOG; KOG2326; Eukaryota.
DR HOGENOM; CLU_010975_2_2_1; -.
DR InParanoid; Q9FQ09; -.
DR OrthoDB; 598957at2759; -.
DR PhylomeDB; Q9FQ09; -.
DR PRO; PR:Q9FQ09; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FQ09; baseline and differential.
DR Genevisible; Q9FQ09; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043564; C:Ku70:Ku80 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:TAIR.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0071480; P:cellular response to gamma radiation; IBA:GO_Central.
DR GO; GO:0071481; P:cellular response to X-ray; IBA:GO_Central.
DR GO; GO:0015074; P:DNA integration; TAS:TAIR.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; TAS:TAIR.
DR GO; GO:0006302; P:double-strand break repair; IMP:TAIR.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR CDD; cd00873; KU80; 1.
DR Gene3D; 1.25.40.240; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR024193; Ku80.
DR InterPro; IPR005160; Ku_C.
DR InterPro; IPR036494; Ku_C_sf.
DR InterPro; IPR005161; Ku_N.
DR InterPro; IPR014893; Ku_PK_bind.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF02735; Ku; 1.
DR Pfam; PF03730; Ku_C; 1.
DR Pfam; PF03731; Ku_N; 1.
DR Pfam; PF08785; Ku_PK_bind; 1.
DR PIRSF; PIRSF016570; Ku80; 1.
DR SMART; SM00559; Ku78; 1.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF101420; SSF101420; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..680
FT /note="ATP-dependent DNA helicase 2 subunit KU80"
FT /id="PRO_0000394131"
FT DOMAIN 224..432
FT /note="Ku"
SQ SEQUENCE 680 AA; 76688 MW; FA7C0191DF05A976 CRC64;
MARNREGLVL VLDVGPAMRS VLPDVEKACS MLLQKKLIYN KYDEVGIVVF GTEETGNELA
REIGGYENVT VLRNIRVVDE LAAEHVKQLP RGTVAGDFLD ALIVGMDMLI KMYGNAHKGK
KRMCLITNAA CPTKDPFEGT KDDQVSTIAM KMAAEGIKME SIVMRSNLSG DAHERVIEEN
DHLLTLFSSN AIAKTVNVDS PLSLLGSLKT RRVAPVTLFR GDLEINPTMK IKVWVYKKVA
EERLPTLKMY SDKAPPTDKF AKHEVKVDYD YKVTAESTEV IAPEERIKGF RYGPQVIPIS
PDQIETLKFK TDKGMKLLGF TEASNILRHY YMKDVNIVVP DPSKEKSVLA VSAIAREMKE
TNKVAIVRCV WRNGQGNVVV GVLTPNVSER DDTPDSFYFN VLPFAEDVRE FPFPSFNKLP
SSWKPDEQQQ AVADNLVKML DLAPSAEEEV LKPDLTPNPV LQRFYEYLEL KSKSTDATLP
PMDGTFKRLM EQDPELSSNN KSIMDTFRGS FEVKENPKLK KASKRLLRDK PSGSDDEDNR
MITYDAKENK IDIVGDANPI QDFEAMISRR DKTDWTEKAI TQMKNLIMKL VENCTDEGDK
ALECVLALRK GCVLEQEPKQ FNEFLNHLFK LCQERNLSHL LEHFMSKKIT LIPKSEAADS
DIVDENAGDF IVKQESMLES
