KU70_DROME
ID KU70_DROME Reviewed; 631 AA.
AC Q23976; B5RIF6; B6UVU9; B6UVV0; B6UVV1; B6UVV2; B6UVV3; B6UVV4; B6UVV5;
AC B6UVV6; B6UVV7; B6UVV8; B6UVV9; B6UVW0; B6UVW2; B6UVW3; B6UVW4; Q24006;
AC Q8SYY3; Q9VGP5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=ATP-dependent DNA helicase 2 subunit 1;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent DNA helicase II subunit dp70;
DE AltName: Full=ATP-dependent helicase Irbp;
DE AltName: Full=Inverted repeat-binding protein;
DE AltName: Full=Yolk protein factor 1 subunit beta;
GN Name=Irbp; Synonyms=dp70, YPF1b; ORFNames=CG5247;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND VARIANTS
RP SER-174 AND PRO-553.
RC STRAIN=Canton-S; TISSUE=Ovary;
RX PubMed=8157678; DOI=10.1016/s0021-9258(19)78149-6;
RA Jacoby D.B., Wensink P.C.;
RT "Yolk protein factor 1 is a Drosophila homolog of Ku, the DNA-binding
RT subunit of a DNA-dependent protein kinase from humans.";
RL J. Biol. Chem. 269:11484-11491(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-553.
RC STRAIN=SB2040; TISSUE=Embryo;
RX PubMed=7809101; DOI=10.1073/pnas.91.26.12681;
RA Beall E.L., Admon A., Rio D.C.;
RT "A Drosophila protein homologous to the human p70 Ku autoimmune antigen
RT interacts with the P transposable element inverted repeats.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:12681-12685(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-460, AND VARIANTS ASP-48; VAL-136;
RP SER-174 AND SER-336.
RC STRAIN=NC301, NC304, NC306, NC319, NC322, NC335, NC336, NC350, NC357,
RC NC358, NC359, NC361, NC362, NC375, NC397, and NC399;
RX PubMed=18984573; DOI=10.1534/genetics.108.093807;
RA Anderson J.A., Gilliland W.D., Langley C.H.;
RT "Molecular population genetics and evolution of Drosophila meiosis genes.";
RL Genetics 181:177-185(2009).
CC -!- FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase.
CC Involved in non-homologous end joining (NHEJ) DNA double strand break
CC repair (By similarity). Sequence-specific DNA-binding protein that has
CC a high affinity for a 31 bp sequence in the Yp1 gene. Site-specific DNA
CC binding to 31 bp P element inverted repeats. {ECO:0000250,
CC ECO:0000269|PubMed:8157678}.
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 of a 70 kDa and a 80 kDa subunit.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically,
CC expression is at low levels in all stages of development.
CC {ECO:0000269|PubMed:8157678}.
CC -!- SIMILARITY: Belongs to the ku70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48866.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U05208; AAA20644.1; -; mRNA.
DR EMBL; U15004; AAC46492.1; -; mRNA.
DR EMBL; AE014297; AAF54631.1; -; Genomic_DNA.
DR EMBL; AY071244; AAL48866.1; ALT_FRAME; mRNA.
DR EMBL; BT044080; ACH92145.1; -; mRNA.
DR EMBL; FJ218647; ACI96795.1; -; Genomic_DNA.
DR EMBL; FJ218648; ACI96796.1; -; Genomic_DNA.
DR EMBL; FJ218649; ACI96797.1; -; Genomic_DNA.
DR EMBL; FJ218650; ACI96798.1; -; Genomic_DNA.
DR EMBL; FJ218651; ACI96799.1; -; Genomic_DNA.
DR EMBL; FJ218652; ACI96800.1; -; Genomic_DNA.
DR EMBL; FJ218653; ACI96801.1; -; Genomic_DNA.
DR EMBL; FJ218654; ACI96802.1; -; Genomic_DNA.
DR EMBL; FJ218655; ACI96803.1; -; Genomic_DNA.
DR EMBL; FJ218656; ACI96804.1; -; Genomic_DNA.
DR EMBL; FJ218657; ACI96805.1; -; Genomic_DNA.
DR EMBL; FJ218658; ACI96806.1; -; Genomic_DNA.
DR EMBL; FJ218659; ACI96807.1; -; Genomic_DNA.
DR EMBL; FJ218660; ACI96808.1; -; Genomic_DNA.
DR EMBL; FJ218661; ACI96809.1; -; Genomic_DNA.
DR EMBL; FJ218662; ACI96810.1; -; Genomic_DNA.
DR PIR; A53623; A53623.
DR RefSeq; NP_536773.1; NM_080512.5.
DR AlphaFoldDB; Q23976; -.
DR SMR; Q23976; -.
DR BioGRID; 72892; 36.
DR IntAct; Q23976; 10.
DR STRING; 7227.FBpp0081861; -.
DR PaxDb; Q23976; -.
DR DNASU; 117419; -.
DR EnsemblMetazoa; FBtr0082385; FBpp0081861; FBgn0011774.
DR GeneID; 117419; -.
DR KEGG; dme:Dmel_CG5247; -.
DR CTD; 117419; -.
DR FlyBase; FBgn0011774; Irbp.
DR VEuPathDB; VectorBase:FBgn0011774; -.
DR eggNOG; KOG2327; Eukaryota.
DR GeneTree; ENSGT00940000153239; -.
DR HOGENOM; CLU_014815_2_0_1; -.
DR InParanoid; Q23976; -.
DR OMA; PNDMMGI; -.
DR OrthoDB; 402798at2759; -.
DR PhylomeDB; Q23976; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 117419; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 117419; -.
DR PRO; PR:Q23976; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0011774; Expressed in ovary and 11 other tissues.
DR ExpressionAtlas; Q23976; baseline and differential.
DR Genevisible; Q23976; DM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043564; C:Ku70:Ku80 complex; IDA:FlyBase.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISS:FlyBase.
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:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:FlyBase.
DR GO; GO:0000723; P:telomere maintenance; IMP:FlyBase.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR Gene3D; 4.10.970.10; -; 1.
DR InterPro; IPR006165; Ku70.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR027388; Ku70_bridge/pillars_dom_sf.
DR InterPro; IPR005160; Ku_C.
DR InterPro; IPR005161; Ku_N.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR12604:SF2; PTHR12604:SF2; 1.
DR Pfam; PF02735; Ku; 1.
DR Pfam; PF03730; Ku_C; 1.
DR Pfam; PF03731; Ku_N; 1.
DR PIRSF; PIRSF003033; Ku70; 1.
DR SMART; SM00559; Ku78; 1.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR TIGRFAMs; TIGR00578; ku70; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chromosome; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..631
FT /note="ATP-dependent DNA helicase 2 subunit 1"
FT /id="PRO_0000210183"
FT DOMAIN 262..487
FT /note="Ku"
FT REGION 550..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 48
FT /note="E -> D (in strain: NC304, NC322, NC359, NC361, NC375
FT and NC399)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 136
FT /note="A -> V (in strain: NC304, NC322, NC359, NC361 and
FT NC399)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 174
FT /note="R -> S (in strain: Canton-S, NC301, NC304, NC319,
FT NC322, NC335, NC350, NC357, NC358, NC359, NC361, NC362,
FT NC375 and NC399)"
FT /evidence="ECO:0000269|PubMed:18984573,
FT ECO:0000269|PubMed:8157678"
FT VARIANT 336
FT /note="R -> S (in strain: NC335)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 553
FT /note="H -> P (in strain: Canton-S and SB2040)"
FT /evidence="ECO:0000269|PubMed:7809101,
FT ECO:0000269|PubMed:8157678"
FT CONFLICT 244
FT /note="S -> P (in Ref. 1; AAA20644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 631 AA; 72535 MW; A991F04699741F5A CRC64;
MSTWNPENDV DLLSGSEDEE DVSMKRDYHG REAILFVVDA NLQTAGVERL LEALNIIRTA
FISGLLVNDK DLIGLIFANT KHSPPPLEAS ALDNIVMPDN CAVFLPLRQL TKPIVEHYLE
FMGGVETQFA DVYGLAEPDG RGRFDLMIRL CIEMLEKCGK KLNNAKIAYV TDVREPHPSN
SNHFQAALQK ASDLEGKEFE FHVIPMVDDF DYEPFYKEFI TLSRAIELDA FQVPDAQMLR
EILSDRKLKQ DFLRRCLGHF SFYLGPNLSM SVQYYNYFQR RAYPRKVQIL RRDNSVVRTK
RVITVQKQKD DGSQDIEHEY QIKVTGGWYT CNVGERDLRI SMDQLNRVRN LHKPQMMLLG
FKHRSSLPEV SYIKPANFMY PDDQSIIGSK RLFRALWERC LVRDKIAICL FMCKRKSIPR
YVALVPVEAP DNGEDKNYRS LLCGDGFKIV YLPEAKHIRH LDLQDWNNTE NTADEQKVEF
FQKIIKKLRV DYQPNLINDP SLDALQANLL ALSLDFSTDT KGLDNLLDTS QQDKRIEKLL
PDYEMFAPEA EPHKKRAAKS TTAGASGPKM AKIDDDQLKE FEFVKSLNKD EALTSCTAAQ
LHFILQHHFD VTMPKSSKKA KLVAKIEELH K
