OGG1_MOUSE
ID OGG1_MOUSE Reviewed; 345 AA.
AC O08760; O08733; O08910; O08991; O35617; O35915; Q9QXE8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 178.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9187114;
RA Aburatani H., Hippo Y., Ishida T., Takashima R., Matsuba C., Kodama T.,
RA Takao M., Yasui A., Yamamoto K., Asano M., Fukasawa K., Yoshinari T.,
RA Inoue H., Otsuka E., Nishimura S.;
RT "Cloning and characterization of mammalian 8-hydroxyguanine-specific DNA
RT glycosylase/apurinic, apyrimidinic lyase, a functional mutM homologue.";
RL Cancer Res. 57:2151-2156(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9197244; DOI=10.1016/s0960-9822(06)00187-4;
RA Lu R., Nash H.M., Verdine G.L.;
RT "A mammalian DNA repair enzyme that excises oxidatively damaged guanines
RT maps to a locus frequently lost in lung cancer.";
RL Curr. Biol. 7:397-407(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=9321410; DOI=10.1093/emboj/16.20.6314;
RA Bjoras M., Luna L., Johnsen B.E., Hoff E., Haug T., Rognes T., Seeberg E.;
RT "Opposite base-dependent reactions of a human base excision repair enzyme
RT on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites.";
RL EMBO J. 16:6314-6322(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9207108; DOI=10.1073/pnas.94.14.7429;
RA Rosenquist T.A., Zharkov D.O., Grollman A.P.;
RT "Cloning and characterization of a mammalian 8-oxoguanine DNA
RT glycosylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7429-7434(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=C3H/HeN; TISSUE=Melanoma;
RX PubMed=9434942; DOI=10.1007/s003359900675;
RA Tani M., Shinmura K., Kohno T., Takenoshita S., Nagamachi Y., Yokota J.;
RT "Genomic structure and chromosomal localization of the mouse Ogg1 gene that
RT is involved in the repair of 8-hydroxyguanine in DNA damage.";
RL Mamm. Genome 9:32-37(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Radicella J.P., Reille F., Dherin C., Boiteux S.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Embryonic stem cell;
RA Johnsen B., Luna L., Rognes T., Seeberg E.;
RT "Complete genomic DNA sequence of the Mus musculus 8-oxoguanine DNA
RT glycosylase 1 gene (OGH1).";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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 -!- TISSUE SPECIFICITY: Highest expression in testis.
CC -!- SIMILARITY: Belongs to the type-1 OGG1 family. {ECO:0000305}.
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DR EMBL; AF003596; AAB61289.1; -; mRNA.
DR EMBL; Y11247; CAA72117.1; -; mRNA.
DR EMBL; U88621; AAB68616.1; -; mRNA.
DR EMBL; U96711; AAB81133.1; -; mRNA.
DR EMBL; AF000669; AAB63151.1; -; mRNA.
DR EMBL; AF012916; AAB94512.1; -; Genomic_DNA.
DR EMBL; AF012912; AAB94512.1; JOINED; Genomic_DNA.
DR EMBL; AF012913; AAB94512.1; JOINED; Genomic_DNA.
DR EMBL; AF012914; AAB94512.1; JOINED; Genomic_DNA.
DR EMBL; AF012915; AAB94512.1; JOINED; Genomic_DNA.
DR EMBL; Y13479; CAA73883.1; -; mRNA.
DR EMBL; AJ001307; CAB65240.1; -; Genomic_DNA.
DR CCDS; CCDS20414.1; -.
DR PIR; T46962; T46962.
DR RefSeq; NP_035087.3; NM_010957.4.
DR PDB; 6G3X; X-ray; 2.10 A; A/B/C=11-325.
DR PDB; 6G3Y; X-ray; 2.51 A; A/B/C=9-325.
DR PDB; 6G40; X-ray; 2.49 A; A/B/C=9-325.
DR PDBsum; 6G3X; -.
DR PDBsum; 6G3Y; -.
DR PDBsum; 6G40; -.
DR AlphaFoldDB; O08760; -.
DR SMR; O08760; -.
DR BioGRID; 201906; 9.
DR IntAct; O08760; 2.
DR STRING; 10090.ENSMUSP00000032406; -.
DR PhosphoSitePlus; O08760; -.
DR EPD; O08760; -.
DR PaxDb; O08760; -.
DR PeptideAtlas; O08760; -.
DR PRIDE; O08760; -.
DR ProteomicsDB; 289970; -.
DR Antibodypedia; 25518; 490 antibodies from 39 providers.
DR DNASU; 18294; -.
DR Ensembl; ENSMUST00000032406; ENSMUSP00000032406; ENSMUSG00000030271.
DR GeneID; 18294; -.
DR KEGG; mmu:18294; -.
DR UCSC; uc009dfh.2; mouse.
DR CTD; 4968; -.
DR MGI; MGI:1097693; Ogg1.
DR VEuPathDB; HostDB:ENSMUSG00000030271; -.
DR eggNOG; KOG2875; Eukaryota.
DR GeneTree; ENSGT00640000091554; -.
DR HOGENOM; CLU_027543_3_2_1; -.
DR InParanoid; O08760; -.
DR OMA; YAQTYVF; -.
DR OrthoDB; 1079482at2759; -.
DR PhylomeDB; O08760; -.
DR TreeFam; TF323702; -.
DR Reactome; R-MMU-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-MMU-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-MMU-110331; Cleavage of the damaged purine.
DR Reactome; R-MMU-110357; Displacement of DNA glycosylase by APEX1.
DR Reactome; R-MMU-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
DR BioGRID-ORCS; 18294; 4 hits in 106 CRISPR screens.
DR PRO; PR:O08760; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O08760; protein.
DR Bgee; ENSMUSG00000030271; Expressed in spermatocyte and 121 other tissues.
DR ExpressionAtlas; O08760; baseline and differential.
DR Genevisible; O08760; MM.
DR GO; GO:0005739; C:mitochondrion; IMP:MGI.
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; IMP:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IMP:MGI.
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; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0019104; F:DNA N-glycosylase activity; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0000702; F:oxidized base lesion DNA N-glycosylase activity; TAS:MGI.
DR GO; GO:0032357; F:oxidized purine DNA binding; ISO:MGI.
DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IDA:MGI.
DR GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:0006284; P:base-excision repair; IDA:MGI.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IBA:GO_Central.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:1901291; P:negative regulation of double-strand break repair via single-strand annealing; ISO:MGI.
DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0032355; P:response to estradiol; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0051593; P:response to folic acid; IEA:Ensembl.
DR GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
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; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000058592"
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"
FT CONFLICT 10
FT /note="S -> Q (in Ref. 1; AAB61289)"
FT /evidence="ECO:0000305"
FT CONFLICT 23..25
FT /note="WAS -> SVA (in Ref. 1; AAB61289)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="A -> G (in Ref. 1; AAB61289)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="L -> S (in Ref. 6; CAA73883)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="S -> F (in Ref. 4; AAB81133)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="R -> H (in Ref. 6; CAA73883 and 7; CAB65240)"
FT /evidence="ECO:0000305"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:6G3X"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:6G3X"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:6G3X"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6G40"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:6G3X"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:6G3X"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:6G3X"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:6G3X"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:6G3X"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:6G3X"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 152..166
FT /evidence="ECO:0007829|PDB:6G3X"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:6G3X"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:6G3X"
FT STRAND 284..290
FT /evidence="ECO:0007829|PDB:6G40"
FT HELIX 293..307
FT /evidence="ECO:0007829|PDB:6G3X"
FT HELIX 311..323
FT /evidence="ECO:0007829|PDB:6G3X"
SQ SEQUENCE 345 AA; 38883 MW; 75BB0DDB084E4947 CRC64;
MLFRSWLPSS MRHRTLSSSP ALWASIPCPR SELRLDLVLA SGQSFRWKEQ SPAHWSGVLA
DQVWTLTQTE DQLYCTVYRG DDSQVSRPTL EELETLHKYF QLDVSLAQLY SHWASVDSHF
QRVAQKFQGV RLLRQDPTEC LFSFICSSNN NIARITGMVE RLCQAFGPRL IQLDDVTYHG
FPNLHALAGP EAETHLRKLG LGYRARYVRA SAKAILEEQG GPAWLQQLRV APYEEAHKAL
CTLPGVGAKV ADCICLMALD KPQAVPVDVH VWQIAHRDYG WHPKTSQAKG PSPLANKELG
NFFRNLWGPY AGWAQAVLFS ADLRQPSLSR EPPAKRKKGS KRPEG
