OGG1_DROME
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 03-AUG-2022, entry version 167.
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; Q9V3I8; -.
DR EnsemblMetazoa; FBtr0071223; FBpp0071168; FBgn0027864.
DR GeneID; 31806; -.
DR KEGG; dme:Dmel_CG1795; -.
DR UCSC; CG1795-RA; d. melanogaster.
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; YAQTYVF; -.
DR OrthoDB; 1079482at2759; -.
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 tissues.
DR ExpressionAtlas; Q9V3I8; baseline and differential.
DR Genevisible; Q9V3I8; DM.
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; 1.10.1670.10; -; 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 Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF07934; OGG_N; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
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
