ID   OGG1_DROME              Reviewed;         343 AA.
AC   Q9V3I8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 2.
DT   27-MAR-2024, entry version 173.
DE   RecName: Full=N-glycosylase/DNA lyase;
DE   AltName: Full=dOgg1;
DE   Includes:
DE     RecName: Full=8-oxoguanine DNA glycosylase;
DE              EC=3.2.2.-;
DE   Includes:
DE     RecName: Full=DNA-(apurinic or apyrimidinic site) lyase;
DE              Short=AP lyase;
DE              EC=4.2.99.18;
GN   Name=Ogg1; ORFNames=CG1795;
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, FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=11095666; DOI=10.1093/nar/28.23.4583;
RA   Dherin C., Dizdaroglu M., Doerflinger H., Boiteux S., Radicella J.P.;
RT   "Repair of oxidative DNA damage in Drosophila melanogaster: identification
RT   and characterization of dOgg1, a second DNA glycosylase activity for 8-
RT   hydroxyguanine and formamidopyrimidines.";
RL   Nucleic Acids Res. 28:4583-4592(2000).
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=10731138; DOI=10.1126/science.287.5461.2222;
RA   Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA   Harvey D.A.;
RT   "A Drosophila complementary DNA resource.";
RL   Science 287:2222-2224(2000).
CC   -!- FUNCTION: DNA repair enzyme that incises DNA at 8-oxoG residues.
CC       Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-
CC       methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase
CC       activity that nicks DNA 3' to the lesion. Efficiently incises DNA
CC       duplexes containing 8-hydroxyguanine (8-OH-Gua), 8-hydroxyadenine (8-
CC       OH-Ade) and abasic (AP) sites placed opposite to a cytosine.
CC       {ECO:0000269|PubMed:11095666}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC         deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC         dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC         2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC         COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC         ChEBI:CHEBI:167181; EC=4.2.99.18;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11095666}. Cytoplasm
CC       {ECO:0000269|PubMed:11095666}. Note=Nuclear and cytoplasmic in nurse
CC       cells and oocyte.
CC   -!- TISSUE SPECIFICITY: Expressed in the cytoplasm of the nurse cells from
CC       oogenesis stage 3 and in the oocyte cytoplasm from stage 10B onwards.
CC       Expressed uniformly in third larval instar wing imaginal disk.
CC   -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically in the
CC       larvae. {ECO:0000269|PubMed:11095666}.
CC   -!- SIMILARITY: Belongs to the type-1 OGG1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD46882.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE014298; AAF46404.2; -; Genomic_DNA.
DR   EMBL; AF160942; AAD46882.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_572499.2; NM_132271.5.
DR   AlphaFoldDB; Q9V3I8; -.
DR   SMR; Q9V3I8; -.
DR   BioGRID; 58265; 1.
DR   STRING; 7227.FBpp0071168; -.
DR   PaxDb; 7227-FBpp0071168; -.
DR   EnsemblMetazoa; FBtr0071223; FBpp0071168; FBgn0027864.
DR   GeneID; 31806; -.
DR   KEGG; dme:Dmel_CG1795; -.
DR   UCSC; CG1795-RA; d. melanogaster.
DR   AGR; FB:FBgn0027864; -.
DR   CTD; 4968; -.
DR   FlyBase; FBgn0027864; Ogg1.
DR   VEuPathDB; VectorBase:FBgn0027864; -.
DR   eggNOG; KOG2875; Eukaryota.
DR   GeneTree; ENSGT00640000091554; -.
DR   HOGENOM; CLU_027543_3_2_1; -.
DR   InParanoid; Q9V3I8; -.
DR   OMA; GYAQEYL; -.
DR   OrthoDB; 118473at2759; -.
DR   PhylomeDB; Q9V3I8; -.
DR   Reactome; R-DME-110329; Cleavage of the damaged pyrimidine.
DR   Reactome; R-DME-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR   Reactome; R-DME-110331; Cleavage of the damaged purine.
DR   Reactome; R-DME-110357; Displacement of DNA glycosylase by APEX1.
DR   BioGRID-ORCS; 31806; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 31806; -.
DR   PRO; PR:Q9V3I8; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0027864; Expressed in oviduct (Drosophila) and 26 other cell types or tissues.
DR   ExpressionAtlas; Q9V3I8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IBA:GO_Central.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:FlyBase.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006284; P:base-excision repair; IMP:FlyBase.
DR   GO; GO:0006285; P:base-excision repair, AP site formation; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:FlyBase.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 3.30.310.40; -; 1.
DR   Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   InterPro; IPR012904; OGG_N.
DR   PANTHER; PTHR10242; 8-OXOGUANINE DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR10242:SF2; N-GLYCOSYLASE_DNA LYASE; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   Pfam; PF07934; OGG_N; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   SUPFAM; SSF55945; TATA-box binding protein-like; 1.
DR   Genevisible; Q9V3I8; DM.
PE   2: Evidence at transcript level;
KW   Cytoplasm; DNA damage; DNA repair; Glycosidase; Hydrolase; Lyase;
KW   Multifunctional enzyme; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..343
FT                   /note="N-glycosylase/DNA lyase"
FT                   /id="PRO_0000058594"
FT   ACT_SITE        250
FT                   /note="Schiff-base intermediate with DNA"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   343 AA;  39406 MW;  85E1D946A6915516 CRC64;
     MLAHNLGFHK KRLFSNMKAV LQDRGVIGLS LEECDLERTL LGGQSFRWRS ICDGNRTKYG
     GVVFNTYWVL QQEESFITYE AYGTSSPLAT KDYSSLISDY LRVDFDLKVN QKDWLSKDDN
     FVKFLSKPVR LLSQEPFENI FSFLCSQNNN IKRISSMIEW FCATFGTKIG HFNGADAYTF
     PTINRFHDIP CEDLNAQLRA AKFGYRAKFI AQTLQEIQKK GGQNWFISLK SMPFEKAREE
     LTLLPGIGYK VADCICLMSM GHLESVPVDI HIYRIAQNYY LPHLTGQKNV TKKIYEEVSK
     HFQKLHGKYA GWAQAILFSA DLSQFQNTST VACKKKSNKK PKK
//