ID OGG1_RAT Reviewed; 345 AA. AC O70249; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 155. DE RecName: Full=N-glycosylase/DNA lyase; 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; Synonyms=Mmh, Ogh1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Hepatoma; RX PubMed=9801319; DOI=10.1093/nar/26.22.5199; RA Prieto Alamo M.J., Jurado J., Francastel E., Laval F.; RT "Rat 7,8-dihydro-8-oxoguanine DNA glycosylase: substrate specificity, RT kinetics and cleavagemechanism at an apurinic site."; RL Nucleic Acids Res. 26:5199-5202(1998). 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. 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, nucleoplasm {ECO:0000250}. Nucleus CC speckle {ECO:0000250}. Nucleus matrix {ECO:0000250}. Note=Together with CC APEX1 is recruited to nuclear speckles in UVA-irradiated cells. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-1 OGG1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF029690; AAC77525.1; -; mRNA. DR RefSeq; NP_110497.1; NM_030870.1. DR AlphaFoldDB; O70249; -. DR SMR; O70249; -. DR STRING; 10116.ENSRNOP00000070483; -. DR PhosphoSitePlus; O70249; -. DR PaxDb; 10116-ENSRNOP00000011352; -. DR Ensembl; ENSRNOT00000085766.2; ENSRNOP00000070483.1; ENSRNOG00000052140.2. DR Ensembl; ENSRNOT00055013181; ENSRNOP00055010558; ENSRNOG00055007846. DR Ensembl; ENSRNOT00060023192; ENSRNOP00060018391; ENSRNOG00060013588. DR Ensembl; ENSRNOT00065047651; ENSRNOP00065039081; ENSRNOG00065027639. DR GeneID; 81528; -. DR KEGG; rno:81528; -. DR AGR; RGD:621168; -. DR CTD; 4968; -. DR RGD; 621168; Ogg1. DR eggNOG; KOG2875; Eukaryota. DR GeneTree; ENSGT00640000091554; -. DR HOGENOM; CLU_027543_1_1_1; -. DR InParanoid; O70249; -. DR OMA; GYAQEYL; -. DR OrthoDB; 118473at2759; -. DR PhylomeDB; O70249; -. DR Reactome; R-RNO-110329; Cleavage of the damaged pyrimidine. DR Reactome; R-RNO-110330; Recognition and association of DNA glycosylase with site containing an affected purine. DR Reactome; R-RNO-110331; Cleavage of the damaged purine. DR Reactome; R-RNO-110357; Displacement of DNA glycosylase by APEX1. DR Reactome; R-RNO-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway. DR PRO; PR:O70249; -. DR Proteomes; UP000002494; Chromosome 4. DR Bgee; ENSRNOG00000052140; Expressed in thymus and 20 other cell types or tissues. DR GO; GO:0005739; C:mitochondrion; ISO:RGD. DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB. DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0032991; C:protein-containing complex; ISO:RGD. DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; ISO:RGD. DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0003684; F:damaged DNA binding; IDA:RGD. DR GO; GO:0019104; F:DNA N-glycosylase activity; IDA:RGD. DR GO; GO:0008017; F:microtubule binding; ISO:RGD. DR GO; GO:0032357; F:oxidized purine DNA binding; ISO:RGD. DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IDA:RGD. DR GO; GO:0006284; P:base-excision repair; IDA:RGD. DR GO; GO:0006285; P:base-excision repair, AP site formation; IBA:GO_Central. DR GO; GO:0071276; P:cellular response to cadmium ion; IEP:RGD. DR GO; GO:0006974; P:DNA damage response; ISO:RGD. DR GO; GO:0006281; P:DNA repair; ISO:RGD. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD. DR GO; GO:1901291; P:negative regulation of double-strand break repair via single-strand annealing; ISO:RGD. DR GO; GO:0006289; P:nucleotide-excision repair; ISO:RGD. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0032355; P:response to estradiol; IDA:RGD. DR GO; GO:0045471; P:response to ethanol; IEP:RGD. DR GO; GO:0051593; P:response to folic acid; IEP:RGD. DR GO; GO:0009416; P:response to light stimulus; IEP:RGD. DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB. DR GO; GO:0009314; P:response to radiation; ISS:UniProtKB. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. DR CDD; cd00056; ENDO3c; 1. DR Gene3D; 3.30.310.40; -; 1. DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR003265; HhH-GPD_domain. DR InterPro; IPR023170; HhH_base_excis_C. DR InterPro; IPR004577; Ogg1. DR InterPro; IPR012904; OGG_N. DR NCBIfam; TIGR00588; ogg; 1. DR PANTHER; PTHR10242; 8-OXOGUANINE DNA GLYCOSYLASE; 1. DR PANTHER; PTHR10242:SF2; N-GLYCOSYLASE_DNA LYASE; 1. DR Pfam; PF00730; HhH-GPD; 1. DR Pfam; PF07934; OGG_N; 1. DR SMART; SM00478; ENDO3c; 1. DR SUPFAM; SSF48150; DNA-glycosylase; 1. DR SUPFAM; SSF55945; TATA-box binding protein-like; 1. DR Genevisible; O70249; RN. PE 2: Evidence at transcript level; KW DNA damage; DNA repair; Glycosidase; Hydrolase; Lyase; KW Multifunctional enzyme; Nucleus; Reference proteome. FT CHAIN 1..345 FT /note="N-glycosylase/DNA lyase" FT /id="PRO_0000058593" FT ACT_SITE 249 FT /note="Schiff-base intermediate with DNA" FT /evidence="ECO:0000250" FT BINDING 149 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250" FT BINDING 154 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250" FT BINDING 204 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250" FT BINDING 266 FT /ligand="8-oxoguanine" FT /ligand_id="ChEBI:CHEBI:52617" FT /evidence="ECO:0000250" FT BINDING 268 FT /ligand="8-oxoguanine" FT /ligand_id="ChEBI:CHEBI:52617" FT /evidence="ECO:0000250" FT BINDING 270 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250" FT BINDING 287 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250" FT BINDING 315 FT /ligand="8-oxoguanine" FT /ligand_id="ChEBI:CHEBI:52617" FT /evidence="ECO:0000250" FT BINDING 319 FT /ligand="8-oxoguanine" FT /ligand_id="ChEBI:CHEBI:52617" FT /evidence="ECO:0000250" SQ SEQUENCE 345 AA; 38711 MW; B7FDF8C782644C41 CRC64; MLFSSSLSSS MRHRTLTSSP ALWASIPCPR SELRLDLVLA SGQSFRWREQ SPAHWSGVLA DQVWTLTQTE DQLYCTVYRG DKGQVGRPTL EELETLHKYF QLDVSLTQLY SHWASVDSHF QSVAQKFQGV RLLRQDPTEC LFSFICSSNN NIARITGMVE RLCQAFGPRL VQLDDVTYHG FPNLHALAGP EVETHLRKLG LGYRARYVCA SAKAILEEQG GPAWLQQLRV ASYEEAHKAL CTLPGVGTKV ADCICLMALD KPQAVPVDIH VWQIAHRDYG WQPKTSQTKG PSPLANKELG NFFRNLWGPY AGWAQAVLFS ADLRQQNLSR EPPAKRKKGS KKTEG //