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Q9V3I8

- OGG1_DROME

UniProt

Q9V3I8 - OGG1_DROME

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Protein

N-glycosylase/DNA lyase

Gene

Ogg1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei148 – 1481DNABy similarity
Binding sitei153 – 1531DNABy similarity
Binding sitei206 – 2061DNABy similarity
Active sitei250 – 2501Schiff-base intermediate with DNABy similarity
Binding sitei267 – 26718-oxoguanine; via carbonyl oxygenBy similarity
Binding sitei269 – 26918-oxoguanineBy similarity
Binding sitei271 – 2711DNABy similarity
Binding sitei314 – 31418-oxoguanineBy similarity
Binding sitei318 – 31818-oxoguanineBy similarity

GO - Molecular functioni

  1. damaged DNA binding Source: InterPro
  2. oxidized purine nucleobase lesion DNA N-glycosylase activity Source: InterPro

GO - Biological processi

  1. base-excision repair Source: InterPro
  2. cellular response to DNA damage stimulus Source: FlyBase
  3. nucleotide-excision repair Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiREACT_204223. Recognition and association of DNA glycosylase with site containing an affected purine.
REACT_207098. Displacement of DNA glycosylase by APE1.
REACT_220490. Cleavage of the damaged purine.

Names & Taxonomyi

Protein namesi
Recommended name:
N-glycosylase/DNA lyase
Alternative name(s):
dOgg1
Including the following 2 domains:
8-oxoguanine DNA glycosylase (EC:3.2.2.-)
DNA-(apurinic or apyrimidinic site) lyase (EC:4.2.99.18)
Short name:
AP lyase
Gene namesi
Name:Ogg1
ORF Names:CG1795
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0027864. Ogg1.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication
Note: Nuclear and cytoplasmic in nurse cells and oocyte.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 343343N-glycosylase/DNA lyasePRO_0000058594Add
BLAST

Expressioni

Tissue specificityi

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 stagei

Expressed maternally and zygotically in the larvae.1 Publication

Gene expression databases

BgeeiQ9V3I8.
ExpressionAtlasiQ9V3I8. differential.

Structurei

3D structure databases

ProteinModelPortaliQ9V3I8.
SMRiQ9V3I8. Positions 33-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the type-1 OGG1 family.Curated

Phylogenomic databases

eggNOGiCOG0122.
GeneTreeiENSGT00640000091554.
HOGENOMiHOG000279962.
InParanoidiQ9V3I8.
KOiK03660.
OMAiSPQANKE.
OrthoDBiEOG7XDBGB.
PhylomeDBiQ9V3I8.

Family and domain databases

Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
InterProiIPR011257. DNA_glycosylase.
IPR003265. HhH-GPD_domain.
IPR023170. HTH_base_excis_C.
IPR012904. OGG_N.
[Graphical view]
PfamiPF00730. HhH-GPD. 1 hit.
PF07934. OGG_N. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9V3I8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLAHNLGFHK KRLFSNMKAV LQDRGVIGLS LEECDLERTL LGGQSFRWRS
60 70 80 90 100
ICDGNRTKYG GVVFNTYWVL QQEESFITYE AYGTSSPLAT KDYSSLISDY
110 120 130 140 150
LRVDFDLKVN QKDWLSKDDN FVKFLSKPVR LLSQEPFENI FSFLCSQNNN
160 170 180 190 200
IKRISSMIEW FCATFGTKIG HFNGADAYTF PTINRFHDIP CEDLNAQLRA
210 220 230 240 250
AKFGYRAKFI AQTLQEIQKK GGQNWFISLK SMPFEKAREE LTLLPGIGYK
260 270 280 290 300
VADCICLMSM GHLESVPVDI HIYRIAQNYY LPHLTGQKNV TKKIYEEVSK
310 320 330 340
HFQKLHGKYA GWAQAILFSA DLSQFQNTST VACKKKSNKK PKK
Length:343
Mass (Da):39,406
Last modified:May 16, 2003 - v2
Checksum:i85E1D946A6915516
GO

Sequence cautioni

The sequence AAD46882.1 differs from that shown. Reason: Frameshift at position 15. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF46404.2.
AF160942 mRNA. Translation: AAD46882.1. Frameshift.
RefSeqiNP_572499.2. NM_132271.5.
UniGeneiDm.3084.

Genome annotation databases

EnsemblMetazoaiFBtr0071223; FBpp0071168; FBgn0027864.
GeneIDi31806.
KEGGidme:Dmel_CG1795.
UCSCiCG1795-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF46404.2 .
AF160942 mRNA. Translation: AAD46882.1 . Frameshift.
RefSeqi NP_572499.2. NM_132271.5.
UniGenei Dm.3084.

3D structure databases

ProteinModelPortali Q9V3I8.
SMRi Q9V3I8. Positions 33-324.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0071223 ; FBpp0071168 ; FBgn0027864 .
GeneIDi 31806.
KEGGi dme:Dmel_CG1795.
UCSCi CG1795-RA. d. melanogaster.

Organism-specific databases

CTDi 4968.
FlyBasei FBgn0027864. Ogg1.

Phylogenomic databases

eggNOGi COG0122.
GeneTreei ENSGT00640000091554.
HOGENOMi HOG000279962.
InParanoidi Q9V3I8.
KOi K03660.
OMAi SPQANKE.
OrthoDBi EOG7XDBGB.
PhylomeDBi Q9V3I8.

Enzyme and pathway databases

Reactomei REACT_204223. Recognition and association of DNA glycosylase with site containing an affected purine.
REACT_207098. Displacement of DNA glycosylase by APE1.
REACT_220490. Cleavage of the damaged purine.

Miscellaneous databases

GenomeRNAii 31806.
NextBioi 775409.
PROi Q9V3I8.

Gene expression databases

Bgeei Q9V3I8.
ExpressionAtlasi Q9V3I8. differential.

Family and domain databases

Gene3Di 1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
InterProi IPR011257. DNA_glycosylase.
IPR003265. HhH-GPD_domain.
IPR023170. HTH_base_excis_C.
IPR012904. OGG_N.
[Graphical view ]
Pfami PF00730. HhH-GPD. 1 hit.
PF07934. OGG_N. 1 hit.
[Graphical view ]
SMARTi SM00478. ENDO3c. 1 hit.
[Graphical view ]
SUPFAMi SSF48150. SSF48150. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiOGG1_DROME
AccessioniPrimary (citable) accession number: Q9V3I8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 16, 2003
Last modified: October 29, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3