3MG_MOUSE
ID 3MG_MOUSE Reviewed; 333 AA.
AC Q04841; A2AVE7; Q64182;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=DNA-3-methyladenine glycosylase;
DE EC=3.2.2.21;
DE AltName: Full=3-alkyladenine DNA glycosylase;
DE AltName: Full=3-methyladenine DNA glycosidase;
DE AltName: Full=ADPG;
DE AltName: Full=N-methylpurine-DNA glycosylase;
GN Name=Mpg; Synonyms=Mid1;
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 [GENOMIC DNA].
RC STRAIN=FEB/N; TISSUE=Spleen;
RX PubMed=7832991; DOI=10.1089/dna.1995.14.37;
RA Tatsuka M., Ibeanu G.C., Izumi T., Narayan S., Ramana C.V., Kim N.K.,
RA Kang W., Roy G., Mitra S.;
RT "Structural organization of the mouse DNA repair gene, N-methylpurine-DNA
RT glycosylase.";
RL DNA Cell Biol. 14:37-45(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8435858; DOI=10.1093/carcin/14.2.175;
RA Engelward B.P., Boosalis M.S., Chen B.J., Deng Z., Siciliano M.J.,
RA Samson L.D.;
RT "Cloning and characterization of a mouse 3-methyladenine/7-methyl-
RT guanine/3-methylguanine DNA glycosylase cDNA whose gene maps to chromosome
RT 11.";
RL Carcinogenesis 14:175-181(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8589517; DOI=10.1007/bf00356165;
RA Kielman M.F., Smits R., Bernini L.F.;
RT "Structure of the mouse 3-methyladenine DNA glycosylase gene and exact
RT localization upstream of the alpha-globin gene cluster on chromosome 11.";
RL Mamm. Genome 6:499-504(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 250-324.
RX PubMed=8318735; DOI=10.1007/bf00357090;
RA Kielman M.F., Smits R., Devi T.S., Fodde R., Bernini L.F.;
RT "Homology of a 130-kb region enclosing the alpha-globin gene cluster, the
RT alpha-locus controlling region, and two non-globin genes in human and
RT mouse.";
RL Mamm. Genome 4:314-323(1993).
CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-
CC methyladenine, and 7-methylguanine from the damaged DNA polymer formed
CC by alkylation lesions.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-
CC methylguanine, 7-methylguanine and 7-methyladenine.; EC=3.2.2.21;
CC -!- ACTIVITY REGULATION: Binding to SSBP1 in mitochondria inhibits
CC glycosylase activity in the context of a single-stranded DNA (ssDNA),
CC but not a double-stranded DNA (dsDNA) substrates. {ECO:0000250}.
CC -!- SUBUNIT: Binds MBD1. Binds SSBP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion matrix,
CC mitochondrion nucleoid {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG 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; X74509; CAA52615.1; -; Genomic_DNA.
DR EMBL; X75038; CAA52615.1; JOINED; Genomic_DNA.
DR EMBL; X75039; CAA52615.1; JOINED; Genomic_DNA.
DR EMBL; X75040; CAA52615.1; JOINED; Genomic_DNA.
DR EMBL; U10420; AAA19487.1; -; mRNA.
DR EMBL; S81162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S81120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S81133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S81134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014754; AAH14754.1; -; mRNA.
DR EMBL; M99625; AAA02577.1; -; mRNA.
DR CCDS; CCDS24520.1; -.
DR PIR; A49003; A49003.
DR PIR; I62129; I62129.
DR RefSeq; NP_034952.2; NM_010822.3.
DR AlphaFoldDB; Q04841; -.
DR SMR; Q04841; -.
DR STRING; 10090.ENSMUSP00000020528; -.
DR iPTMnet; Q04841; -.
DR PhosphoSitePlus; Q04841; -.
DR EPD; Q04841; -.
DR MaxQB; Q04841; -.
DR PaxDb; Q04841; -.
DR PeptideAtlas; Q04841; -.
DR PRIDE; Q04841; -.
DR ProteomicsDB; 285945; -.
DR Antibodypedia; 1865; 419 antibodies from 36 providers.
DR DNASU; 268395; -.
DR Ensembl; ENSMUST00000020528; ENSMUSP00000020528; ENSMUSG00000020287.
DR GeneID; 268395; -.
DR KEGG; mmu:268395; -.
DR UCSC; uc007ijd.2; mouse.
DR CTD; 4350; -.
DR MGI; MGI:97073; Mpg.
DR VEuPathDB; HostDB:ENSMUSG00000020287; -.
DR eggNOG; KOG4486; Eukaryota.
DR GeneTree; ENSGT00390000009825; -.
DR HOGENOM; CLU_060471_0_0_1; -.
DR InParanoid; Q04841; -.
DR OMA; PICAPRV; -.
DR OrthoDB; 1500650at2759; -.
DR PhylomeDB; Q04841; -.
DR TreeFam; TF331768; -.
DR Reactome; R-MMU-110331; Cleavage of the damaged purine.
DR Reactome; R-MMU-110357; Displacement of DNA glycosylase by APEX1.
DR BioGRID-ORCS; 268395; 3 hits in 110 CRISPR screens.
DR PRO; PR:Q04841; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q04841; protein.
DR Bgee; ENSMUSG00000020287; Expressed in parotid gland and 242 other tissues.
DR ExpressionAtlas; Q04841; baseline and differential.
DR Genevisible; Q04841; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003905; F:alkylbase DNA N-glycosylase activity; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0052822; F:DNA-3-methylguanine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0052821; F:DNA-7-methyladenine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0043916; F:DNA-7-methylguanine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006284; P:base-excision repair; IMP:MGI.
DR CDD; cd00540; AAG; 1.
DR Gene3D; 3.10.300.10; -; 1.
DR HAMAP; MF_00527; 3MGH; 1.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR InterPro; IPR003180; MPG.
DR InterPro; IPR036995; MPG_sf.
DR PANTHER; PTHR10429; PTHR10429; 1.
DR Pfam; PF02245; Pur_DNA_glyco; 1.
DR SUPFAM; SSF50486; SSF50486; 1.
DR TIGRFAMs; TIGR00567; 3mg; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; DNA damage; DNA repair; Hydrolase; Mitochondrion;
KW Mitochondrion nucleoid; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..333
FT /note="DNA-3-methyladenine glycosylase"
FT /id="PRO_0000100066"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29372"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29372"
FT CONFLICT 14
FT /note="A -> S (in Ref. 1; CAA52615, 2; AAA19487 and 5;
FT AAH14754)"
FT /evidence="ECO:0000305"
FT CONFLICT 319..324
FT /note="PQQTAC -> LANSLL (in Ref. 6; AAA02577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 36472 MW; 195E96174BFA0576 CRC64;
MPARGGSARP GRGALKPVSV TLLPDTEQPP FLGRARRPGN ARAGSLVTGY HEVGQMPAPL
SRKIGQKKQR LADSEQQQTP KERLLSTPGL RRSIYFSSPE DHSGRLGPEF FDQPAVTLAR
AFLGQVLVRR LADGTELRGR IVETEAYLGP EDEAAHSRGG RQTPRNRGMF MKPGTLYVYL
IYGMYFCLNV SSQGAGACVL LRALEPLEGL ETMRQLRNSL RKSTVGRSLK DRELCSGPSK
LCQALAIDKS FDQRDLAQDD AVWLEHGPLE SSSPAVVVAA ARIGIGHAGE WTQKPLRFYV
QGSPWVSVVD RVAEQMDQPQ QTACSEGLLI VQK
