EXO1_DROME
ID EXO1_DROME Reviewed; 732 AA.
AC Q24558; B9EQW7; Q24557; Q960X5;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Exonuclease 1;
DE EC=3.1.-.-;
DE AltName: Full=Exonuclease I;
DE AltName: Full=Protein tosca;
GN Name=tos; Synonyms=exo1; ORFNames=CG10387;
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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=8812111; DOI=10.1006/dbio.1996.0200;
RA Digilio F.A., Pannuti A., Lucchesi J., Furia M., Polito L.;
RT "A Drosophila gene encoding a nuclease specifically expressed in the female
RT germline.";
RL Dev. Biol. 178:90-100(1996).
RN [2]
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 [3]
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 [4]
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 [5]
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 (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-433; THR-443 AND
RP SER-447, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: 5'->3' double-stranded DNA exonuclease which may also contain
CC a cryptic 3'->5' double-stranded DNA exonuclease activity. Also
CC exhibits endonuclease activity against 5'-overhanging flap structures
CC similar to those generated by displacement synthesis when DNA
CC polymerase encounters the 5'-end of a downstream Okazaki fragment.
CC Required for DNA mismatch repair (MMR) (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. They probably participate in
CC the reaction catalyzed by the enzyme. May bind an additional third
CC magnesium ion after substrate binding. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the female germline.
CC {ECO:0000269|PubMed:8812111}.
CC -!- DEVELOPMENTAL STAGE: Maternally expressed. Accumulates in the
CC developing oocyte. {ECO:0000269|PubMed:8812111}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC subfamily. {ECO:0000305}.
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DR EMBL; X89021; CAA61430.1; -; mRNA.
DR EMBL; X89022; CAA61431.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53687.1; -; Genomic_DNA.
DR EMBL; AY051794; AAK93218.1; -; mRNA.
DR EMBL; BT058042; ACM78484.1; -; mRNA.
DR RefSeq; NP_477145.1; NM_057797.4.
DR AlphaFoldDB; Q24558; -.
DR SMR; Q24558; -.
DR BioGRID; 61114; 32.
DR IntAct; Q24558; 3.
DR STRING; 7227.FBpp0080675; -.
DR iPTMnet; Q24558; -.
DR PaxDb; Q24558; -.
DR PRIDE; Q24558; -.
DR DNASU; 35119; -.
DR EnsemblMetazoa; FBtr0081131; FBpp0080675; FBgn0015553.
DR GeneID; 35119; -.
DR KEGG; dme:Dmel_CG10387; -.
DR UCSC; CG10387-RA; d. melanogaster.
DR CTD; 35119; -.
DR FlyBase; FBgn0015553; tos.
DR VEuPathDB; VectorBase:FBgn0015553; -.
DR eggNOG; KOG2518; Eukaryota.
DR GeneTree; ENSGT00510000047676; -.
DR HOGENOM; CLU_017284_1_0_1; -.
DR InParanoid; Q24558; -.
DR OMA; FFKKVDF; -.
DR OrthoDB; 796591at2759; -.
DR PhylomeDB; Q24558; -.
DR Reactome; R-DME-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-DME-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-69473; G2/M DNA damage checkpoint.
DR SignaLink; Q24558; -.
DR BioGRID-ORCS; 35119; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35119; -.
DR PRO; PR:Q24558; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0015553; Expressed in ovary and 16 other tissues.
DR Genevisible; Q24558; DM.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0008409; F:5'-3' exonuclease activity; ISS:UniProtKB.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051908; F:double-stranded DNA 5'-3' exodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0048256; F:flap endonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045145; F:single-stranded DNA 5'-3' exodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; ISS:UniProtKB.
DR GO; GO:0006298; P:mismatch repair; ISS:UniProtKB.
DR CDD; cd09908; H3TH_EXO1; 1.
DR CDD; cd09857; PIN_EXO1; 1.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR032641; Exo1.
DR InterPro; IPR037315; EXO1_H3TH.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR044752; PIN-like_EXO1.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR019974; XPG_CS.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR11081; PTHR11081; 1.
DR PANTHER; PTHR11081:SF8; PTHR11081:SF8; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; SSF47807; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
DR PROSITE; PS00841; XPG_1; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA excision; DNA repair; DNA-binding; Endonuclease;
KW Excision nuclease; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..732
FT /note="Exonuclease 1"
FT /id="PRO_0000154043"
FT REGION 1..99
FT /note="N-domain"
FT REGION 138..230
FT /note="I-domain"
FT REGION 422..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 443
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 130
FT /note="A -> T (in Ref. 1; CAA61430)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="T -> I (in Ref. 4; AAK93218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 83181 MW; A1AF71CDFC7813AC CRC64;
MGITGLIPFV GKASSQLHLK DIRGSTVAVD TYCWLHKGVF GCAEKLARGE DTDVYIQYCL
KYVNMLLSYD IKPILVFDGQ HLPAKALTEK RRRDSRKQSK ERAAELLRLG RIEEARSHMR
RCVDVTHDMA LRLIRECRSR NVDCIVAPYE ADAQMAWLNR ADVAQYIITE DSDLTLFGAK
NIIFKLDLNG SGLLVEAEKL HLAMGCTEEK YHFDKFRRMC ILSGCDYLDS LPGIGLAKAC
KFILKTEQED MRIALKKIPS YLNMRNLEVD DDYIENFMKA EATFRHMFIY NPLERRMQRL
CALEDYETDE RYCSNAGTLL EDSEQALHLA LGNLNPFSMK RLDSWTPEKA WPTPKNVKRS
KHKSIWQTNF QSENTHTPKK ENPCALFFKK VDFVGKTLNE EIEANQRLEQ AKQTEAELFN
MYSFKAKRRR SPSREDSVDQ ERTPPPSPVH KSRHNPFAKE RTGEEANQRS PVVCENASLL
RLLSPKKASP LDGEAGVKKV DSLKRSIFAK EQVQIRSRFF ATQDEQTRLQ REHLRDTEND
DMDEQKLSSH SGHKKLRLVC KDIPGKNPIR QRCSSQISDG ETDTDTTASS LLESQDKGVP
SPLESQEDLN NSQPQIPTEG NTNSTTIRIK SLDLLLENSP EPTQESDRNN NDAIILLSDD
SCSSDQRASS TSSSSQQRQN FLPTSKRRVG LSKPSTAKKG TPKSRTNGKL GAVSQNQTKL
SMFGFQTKPV LK
