Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9V3I8

- OGG1_DROME

UniProt

Q9V3I8 - OGG1_DROME

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (16 May 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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-SubCell
    2. nucleus Source: UniProtKB-SubCell

    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.

    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

    MLAHNLGFHK KRLFSNMKAV LQDRGVIGLS LEECDLERTL LGGQSFRWRS    50
    ICDGNRTKYG GVVFNTYWVL QQEESFITYE AYGTSSPLAT KDYSSLISDY 100
    LRVDFDLKVN QKDWLSKDDN FVKFLSKPVR LLSQEPFENI FSFLCSQNNN 150
    IKRISSMIEW FCATFGTKIG HFNGADAYTF PTINRFHDIP CEDLNAQLRA 200
    AKFGYRAKFI AQTLQEIQKK GGQNWFISLK SMPFEKAREE LTLLPGIGYK 250
    VADCICLMSM GHLESVPVDI HIYRIAQNYY LPHLTGQKNV TKKIYEEVSK 300
    HFQKLHGKYA GWAQAILFSA DLSQFQNTST VACKKKSNKK PKK 343
    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.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.

    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

    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 1, 2014
    This is version 115 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