O08760 (OGG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleoplasm 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.
Tissue specificity	Highest expression in testis.
Sequence similarities	Belongs to the type-1 OGG1 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Molecular function	Glycosidase Hydrolase Lyase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	acute inflammatory response Inferred from electronic annotation. Source: Compara base-excision repair Inferred from direct assay Ref.4. Source: MGI cellular response to cadmium ion Inferred from electronic annotation. Source: Compara 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-dependent Inferred from sequence or structural similarity. Source: UniProtKB response to drug Inferred from electronic annotation. Source: Compara response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to folic acid Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from sequence or structural similarity. Source: UniProtKB response to radiation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	mitochondrion Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI nuclear matrix Inferred from sequence or structural similarity. Source: UniProtKB nuclear speck Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	8-oxo-7,8-dihydroguanine DNA N-glycosylase activity Inferred from mutant phenotype PubMed 12447686. Source: MGI damaged DNA binding Inferred from electronic annotation. Source: Compara microtubule binding Inferred from direct assay PubMed 15725623. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 345	345	N-glycosylase/DNA lyase		PRO_0000058592
Sites
	Active site	249	1	Schiff-base intermediate with DNA By similarity
	Binding site	149	1	DNA By similarity
	Binding site	154	1	DNA By similarity
	Binding site	204	1	DNA By similarity
	Binding site	266	1	8-oxoguanine; via carbonyl oxygen By similarity
	Binding site	268	1	8-oxoguanine By similarity
	Binding site	270	1	DNA By similarity
	Binding site	287	1	DNA By similarity
	Binding site	315	1	8-oxoguanine By similarity
	Binding site	319	1	8-oxoguanine By similarity
Experimental info
	Sequence conflict	10	1	S → Q in AAB61289. Ref.1
	Sequence conflict	23 – 25	3	WAS → SVA in AAB61289. Ref.1
	Sequence conflict	239	1	A → G in AAB61289. Ref.1
	Sequence conflict	299	1	L → S in CAA73883. Ref.6
	Sequence conflict	329	1	S → F in AAB81133. Ref.4
	Sequence conflict	336	1	R → H in CAA73883. Ref.6
	Sequence conflict	336	1	R → H in CAB65240. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	O08760 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 75BB0DDB084E4947	FASTA	345	38,883
	10 20 30 40 50 60 MLFRSWLPSS MRHRTLSSSP ALWASIPCPR SELRLDLVLA SGQSFRWKEQ SPAHWSGVLA 70 80 90 100 110 120 DQVWTLTQTE DQLYCTVYRG DDSQVSRPTL EELETLHKYF QLDVSLAQLY SHWASVDSHF 130 140 150 160 170 180 QRVAQKFQGV RLLRQDPTEC LFSFICSSNN NIARITGMVE RLCQAFGPRL IQLDDVTYHG 190 200 210 220 230 240 FPNLHALAGP EAETHLRKLG LGYRARYVRA SAKAILEEQG GPAWLQQLRV APYEEAHKAL 250 260 270 280 290 300 CTLPGVGAKV ADCICLMALD KPQAVPVDVH VWQIAHRDYG WHPKTSQAKG PSPLANKELG 310 320 330 340 NFFRNLWGPY AGWAQAVLFS ADLRQPSLSR EPPAKRKKGS KRPEG

References

[1]	"Cloning and characterization of mammalian 8-hydroxyguanine-specific DNA glycosylase/apurinic, apyrimidinic lyase, a functional mutM homologue." Aburatani H., Hippo Y., Ishida T., Takashima R., Matsuba C., Kodama T., Takao M., Yasui A., Yamamoto K., Asano M., Fukasawa K., Yoshinari T., Inoue H., Otsuka E., Nishimura S. Cancer Res. 57:2151-2156(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer." Lu R., Nash H.M., Verdine G.L. Curr. Biol. 7:397-407(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites." Bjoras M., Luna L., Johnsen B.E., Hoff E., Haug T., Rognes T., Seeberg E. EMBO J. 16:6314-6322(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[4]	"Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase." Rosenquist T.A., Zharkov D.O., Grollman A.P. Proc. Natl. Acad. Sci. U.S.A. 94:7429-7434(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Genomic structure and chromosomal localization of the mouse Ogg1 gene that is involved in the repair of 8-hydroxyguanine in DNA damage." Tani M., Shinmura K., Kohno T., Takenoshita S., Nagamachi Y., Yokota J. Mamm. Genome 9:32-37(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: C3H/HeN. Tissue: Melanoma.
[6]	Radicella J.P., Reille F., Dherin C., Boiteux S. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J.
[7]	"Complete genomic DNA sequence of the Mus musculus 8-oxoguanine DNA glycosylase 1 gene (OGH1)." Johnsen B., Luna L., Rognes T., Seeberg E. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/Sv. Tissue: Embryonic stem cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF003596 mRNA. Translation: AAB61289.1. Y11247 mRNA. Translation: CAA72117.1. U88621 mRNA. Translation: AAB68616.1. U96711 mRNA. Translation: AAB81133.1. AF000669 mRNA. Translation: AAB63151.1. AF012916 , AF012912, AF012913, AF012914, AF012915 Genomic DNA. Translation: AAB94512.1. Y13479 mRNA. Translation: CAA73883.1. AJ001307 Genomic DNA. Translation: CAB65240.1.
IPI	IPI00309197.
PIR	T46962.
RefSeq	NP_035087.3. NM_010957.4.
UniGene	Mm.43612.
3D structure databases
ProteinModelPortal	O08760.
SMR	O08760. Positions 13-323.
ModBase	Search...
Protein-protein interaction databases
IntAct	O08760. 2 interactions.
STRING	10090.ENSMUSP00000032406.
PTM databases
PhosphoSite	O08760.
Proteomic databases
PRIDE	O08760.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000032406; ENSMUSP00000032406; ENSMUSG00000030271.
GeneID	18294.
KEGG	mmu:18294.
Organism-specific databases
CTD	4968.
MGI	MGI:1097693. Ogg1.
Phylogenomic databases
eggNOG	COG0122.
HOVERGEN	HBG001047.
InParanoid	O08760.
KO	K03660.
OMA	PLIFCQD.
OrthoDB	EOG4P8FJN.
Gene expression databases
ArrayExpress	O08760.
Bgee	O08760.
CleanEx	MM_OGG1.
Genevestigator	O08760.
GermOnline	ENSMUSG00000030271. Mus musculus.
Family and domain databases
Gene3D	1.10.1670.10. 1 hit. 1.10.340.30. 1 hit.
InterPro	IPR011257. DNA_glycosylase. IPR003265. HhH-GPD_domain. IPR023170. HTH_base_excis_C. IPR004577. Ogg. IPR012904. OGG_N. [Graphical view]
Pfam	PF00730. HhH-GPD. 1 hit. PF07934. OGG_N. 1 hit. [Graphical view]
SMART	SM00478. ENDO3c. 1 hit. [Graphical view]
SUPFAM	SSF48150. DNA_glycsylse. 1 hit.
TIGRFAMs	TIGR00588. ogg. 1 hit.
ProtoNet	Search...
Other
NextBio	293744.
SOURCE	Search...

Entry information

Entry name

OGG1_MOUSE

Accession

Primary (citable) accession number: O08760
Secondary accession number(s): O08733 , O08910, O08991, O35617, O35915, Q9QXE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	April 3, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program