OGG1_RAT
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 03-AUG-2022, entry version 146.
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}.
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DR EMBL; AF029690; AAC77525.1; -; mRNA.
DR RefSeq; NP_110497.1; NM_030870.1.
DR AlphaFoldDB; O70249; -.
DR SMR; O70249; -.
DR STRING; 10116.ENSRNOP00000011352; -.
DR PhosphoSitePlus; O70249; -.
DR PaxDb; O70249; -.
DR Ensembl; ENSRNOT00000085766; ENSRNOP00000070483; ENSRNOG00000052140.
DR GeneID; 81528; -.
DR KEGG; rno:81528; -.
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; YAQTYVF; -.
DR OrthoDB; 1079482at2759; -.
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 tissues.
DR Genevisible; O70249; RN.
DR GO; GO:0005739; C:mitochondrion; IDA: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; IDA: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:0002526; P:acute inflammatory response; IEP:RGD.
DR GO; GO:0007568; P:aging; 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:cellular response to DNA damage stimulus; 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:0033683; P:nucleotide-excision repair, DNA incision; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; 1.10.1670.10; -; 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 Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF07934; OGG_N; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
DR TIGRFAMs; TIGR00588; ogg; 1.
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
