Q9V3I8 (OGG1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-glycosylase/DNA lyase

Alternative name(s):
dOgg1

Including the following 2 domains:

1. 8-oxoguanine DNA glycosylase
   EC=3.2.2.-
2. DNA-(apurinic or apyrimidinic site) lyase
   Short name=AP lyase
   EC=4.2.99.18

Gene names

Name:	Ogg1
ORF Names:	CG1795

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion. Efficiently incises DNA duplexes containing 8-hydroxyguanine (8-OH-Gua), 8-hydroxyadenine (8-OH-Ade) and abasic (AP) sites placed opposite to a cytosine. Ref.1
Catalytic activity	The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
Subcellular location	Nucleus. Cytoplasm. Note: Nuclear and cytoplasmic in nurse cells and oocyte. Ref.1
Tissue specificity	Expressed in the cytoplasm of the nurse cells from oogenesis stage 3 and in the oocyte cytoplasm from stage 10B onwards. Expressed uniformly in third larval instar wing imaginal disk.
Developmental stage	Expressed maternally and zygotically in the larvae. Ref.1
Sequence similarities	Belongs to the type-1 OGG1 family.
Sequence caution	The sequence AAD46882.1 differs from that shown. Reason: Frameshift at position 15.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Cytoplasm Nucleus
Molecular function	Glycosidase Hydrolase Lyase Nuclease
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	base-excision repair Inferred from electronic annotation. Source: InterPro nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC nucleotide-excision repair Inferred from electronic annotation. Source: InterPro response to DNA damage stimulus Inferred from mutant phenotype PubMed 19543366. Source: FlyBase
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	damaged DNA binding Inferred from electronic annotation. Source: InterPro nuclease activity Inferred from electronic annotation. Source: UniProtKB-KW oxidized purine nucleobase lesion DNA N-glycosylase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 343	343	N-glycosylase/DNA lyase		PRO_0000058594
Sites
	Active site	250	1	Schiff-base intermediate with DNA By similarity
	Binding site	148	1	DNA By similarity
	Binding site	153	1	DNA By similarity
	Binding site	206	1	DNA By similarity
	Binding site	267	1	8-oxoguanine; via carbonyl oxygen By similarity
	Binding site	269	1	8-oxoguanine By similarity
	Binding site	271	1	DNA By similarity
	Binding site	314	1	8-oxoguanine By similarity
	Binding site	318	1	8-oxoguanine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9V3I8 [UniParc]. Last modified May 16, 2003. Version 2. Checksum: 85E1D946A6915516	FASTA	343	39,406
	10 20 30 40 50 60 MLAHNLGFHK KRLFSNMKAV LQDRGVIGLS LEECDLERTL LGGQSFRWRS ICDGNRTKYG 70 80 90 100 110 120 GVVFNTYWVL QQEESFITYE AYGTSSPLAT KDYSSLISDY LRVDFDLKVN QKDWLSKDDN 130 140 150 160 170 180 FVKFLSKPVR LLSQEPFENI FSFLCSQNNN IKRISSMIEW FCATFGTKIG HFNGADAYTF 190 200 210 220 230 240 PTINRFHDIP CEDLNAQLRA AKFGYRAKFI AQTLQEIQKK GGQNWFISLK SMPFEKAREE 250 260 270 280 290 300 LTLLPGIGYK VADCICLMSM GHLESVPVDI HIYRIAQNYY LPHLTGQKNV TKKIYEEVSK 310 320 330 340 HFQKLHGKYA GWAQAILFSA DLSQFQNTST VACKKKSNKK PKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Repair of oxidative DNA damage in Drosophila melanogaster: identification and characterization of dOgg1, a second DNA glycosylase activity for 8-hydroxyguanine and formamidopyrimidines." Dherin C., Dizdaroglu M., Doerflinger H., Boiteux S., Radicella J.P. Nucleic Acids Res. 28:4583-4592(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila complementary DNA resource." Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A. Science 287:2222-2224(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014298 Genomic DNA. Translation: AAF46404.2. AF160942 mRNA. Translation: AAD46882.1. Frameshift.
RefSeq	NP_572499.2. NM_132271.5.
UniGene	Dm.3084.
3D structure databases
ProteinModelPortal	Q9V3I8.
SMR	Q9V3I8. Positions 33-324.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0071223; FBpp0071168; FBgn0027864.
GeneID	31806.
KEGG	dme:Dmel_CG1795.
UCSC	CG1795-RA. d. melanogaster.
Organism-specific databases
CTD	4968.
FlyBase	FBgn0027864. Ogg1.
Phylogenomic databases
eggNOG	COG0122.
GeneTree	ENSGT00640000091554.
HOGENOM	HOG000279962.
InParanoid	Q9V3I8.
KO	K03660.
OMA	CDLERTL.
OrthoDB	EOG4WWQ13.
PhylomeDB	Q9V3I8.
Gene expression databases
Bgee	Q9V3I8.
GermOnline	CG1795. Drosophila melanogaster.
Family and domain databases
Gene3D	1.10.1670.10. 1 hit. 1.10.340.30. 1 hit.
InterPro	IPR011257. DNA_glycosylase. IPR003265. HhH-GPD_domain. IPR023170. HTH_base_excis_C. IPR012904. OGG_N. [Graphical view]
Pfam	PF00730. HhH-GPD. 1 hit. PF07934. OGG_N. 1 hit. [Graphical view]
SMART	SM00478. ENDO3c. 1 hit. [Graphical view]
SUPFAM	SSF48150. DNA_glycsylse. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	31806.
NextBio	775409.

Entry information

Entry name

OGG1_DROME

Accession

Primary (citable) accession number: Q9V3I8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 16, 2003
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project