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O70249 (OGG1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-glycosylase/DNA lyase

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
Synonyms:Mmh, Ogh1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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

Nucleusnucleoplasm By similarity. Nucleus speckle By similarity. Nucleus matrix By similarity. Note: Together with APEX1 is recruited to nuclear speckles in UVA-irradiated cells By similarity.

Sequence similarities

Belongs to the type-1 OGG1 family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   Molecular functionGlycosidase
Hydrolase
Lyase
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from direct assay Ref.1. Source: GOC

DNA repair

Traceable author statement PubMed 12060578. Source: RGD

acute inflammatory response

Inferred from expression pattern PubMed 12853071. Source: RGD

base-excision repair

Inferred from direct assay Ref.1. Source: RGD

cellular response to cadmium ion

Inferred from expression pattern PubMed 12499121. Source: RGD

nucleotide-excision repair

Inferred from electronic annotation. Source: InterPro

regulation of protein import into nucleus, translocation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from expression pattern PubMed 11872643PubMed 15031674. Source: RGD

response to estradiol

Inferred from direct assay PubMed 16182450. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 11524300. Source: RGD

response to folic acid

Inferred from expression pattern PubMed 20051376. Source: RGD

response to oxidative stress

Inferred from sequence or structural similarity. Source: UniProtKB

response to radiation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentmitochondrion

Inferred from direct assay PubMed 12060578. Source: RGD

nuclear matrix

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear speck

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 12060578. Source: RGD

   Molecular_function8-oxo-7,8-dihydroguanine DNA N-glycosylase activity

Inferred from electronic annotation. Source: Ensembl

DNA N-glycosylase activity

Inferred from direct assay Ref.1. Source: RGD

damaged DNA binding

Inferred from direct assay Ref.1. Source: RGD

oxidized purine nucleobase lesion DNA N-glycosylase activity

Inferred from direct assay Ref.1. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345N-glycosylase/DNA lyase
PRO_0000058593

Sites

Active site2491Schiff-base intermediate with DNA By similarity
Binding site1491DNA By similarity
Binding site1541DNA By similarity
Binding site2041DNA By similarity
Binding site26618-oxoguanine; via carbonyl oxygen By similarity
Binding site26818-oxoguanine By similarity
Binding site2701DNA By similarity
Binding site2871DNA By similarity
Binding site31518-oxoguanine By similarity
Binding site31918-oxoguanine By similarity

Sequences

Sequence LengthMass (Da)Tools
O70249 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: B7FDF8C782644C41

FASTA34538,711
        10         20         30         40         50         60 
MLFSSSLSSS MRHRTLTSSP ALWASIPCPR SELRLDLVLA SGQSFRWREQ SPAHWSGVLA 

        70         80         90        100        110        120 
DQVWTLTQTE DQLYCTVYRG DKGQVGRPTL EELETLHKYF QLDVSLTQLY SHWASVDSHF 

       130        140        150        160        170        180 
QSVAQKFQGV RLLRQDPTEC LFSFICSSNN NIARITGMVE RLCQAFGPRL VQLDDVTYHG 

       190        200        210        220        230        240 
FPNLHALAGP EVETHLRKLG LGYRARYVCA SAKAILEEQG GPAWLQQLRV ASYEEAHKAL 

       250        260        270        280        290        300 
CTLPGVGTKV ADCICLMALD KPQAVPVDIH VWQIAHRDYG WQPKTSQTKG PSPLANKELG 

       310        320        330        340 
NFFRNLWGPY AGWAQAVLFS ADLRQQNLSR EPPAKRKKGS KKTEG 

« Hide

References

[1]"Rat 7,8-dihydro-8-oxoguanine DNA glycosylase: substrate specificity, kinetics and cleavagemechanism at an apurinic site."
Prieto Alamo M.J., Jurado J., Francastel E., Laval F.
Nucleic Acids Res. 26:5199-5202(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hepatoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF029690 mRNA. Translation: AAC77525.1.
RefSeqNP_110497.1. NM_030870.1.
UniGeneRn.22623.

3D structure databases

ProteinModelPortalO70249.
SMRO70249. Positions 13-323.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteO70249.

Proteomic databases

PRIDEO70249.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID81528.
KEGGrno:81528.

Organism-specific databases

CTD4968.
RGD621168. Ogg1.

Phylogenomic databases

eggNOGCOG0122.
HOGENOMHOG000180756.
HOVERGENHBG001047.
InParanoidO70249.
KOK03660.
PhylomeDBO70249.

Gene expression databases

GenevestigatorO70249.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
InterProIPR011257. DNA_glycosylase.
IPR003265. HhH-GPD_domain.
IPR023170. HTH_base_excis_C.
IPR004577. Ogg.
IPR012904. OGG_N.
[Graphical view]
PfamPF00730. HhH-GPD. 1 hit.
PF07934. OGG_N. 1 hit.
[Graphical view]
SMARTSM00478. ENDO3c. 1 hit.
[Graphical view]
SUPFAMSSF48150. SSF48150. 1 hit.
TIGRFAMsTIGR00588. ogg. 1 hit.
ProtoNetSearch...

Other

NextBio615069.
PROO70249.

Entry information

Entry nameOGG1_RAT
AccessionPrimary (citable) accession number: O70249
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families