ID   3MG_RAT                 Reviewed;         317 AA.
AC   P23571;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 140.
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;
DE   Flags: Fragment;
GN   Name=Mpg;
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].
RX   PubMed=1698614; DOI=10.1002/j.1460-2075.1990.tb07534.x;
RA   O'Connor T.R., Laval F.;
RT   "Isolation and structure of a cDNA expressing a mammalian 3-methyladenine-
RT   DNA glycosylase.";
RL   EMBO J. 9:3337-3342(1990).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAA39814.1; Type=Frameshift; Evidence={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; X56420; CAA39814.1; ALT_FRAME; mRNA.
DR   PIR; S12059; S12059.
DR   STRING; 10116.ENSRNOP00000027940; -.
DR   PaxDb; P23571; -.
DR   PRIDE; P23571; -.
DR   UCSC; RGD:3106; rat.
DR   RGD; 3106; Mpg.
DR   eggNOG; KOG4486; Eukaryota.
DR   InParanoid; P23571; -.
DR   Reactome; R-RNO-110331; Cleavage of the damaged purine.
DR   Reactome; R-RNO-110357; Displacement of DNA glycosylase by APEX1.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003905; F:alkylbase DNA N-glycosylase activity; ISO:RGD.
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; ISO:RGD.
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..317
FT                   /note="DNA-3-methyladenine glycosylase"
FT                   /id="PRO_0000100067"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29372"
FT   MOD_RES         258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29372"
FT   NON_TER         1
SQ   SEQUENCE   317 AA;  34814 MW;  613849E4ADEF1BDB CRC64;
     SKEPVSVVLP DAEHPAFPGR TRRPGNARAG SQVTGSREVG QMPAPLSRKI GQKKQQLAQS
     EQQQTPKEKL SSTPGLLRSI YFSSPEDRPA RLGPEYFDQP AVTLARAFLG QVLVRRLADG
     TELRGRIVET EAYLGPEDEA AHSRGGRQTP RNRGMFMKPG TLYVYLIYGM YFCLNVSSQG
     AGACVLLRAL EPLEGLETMR QLRNSLRKST VGRSLKDREL CNGPSKLCQA LARSKSFDQR
     DLAQDEAVWL EHGPLESSSP AVVAAAAGIG HAGEWTQKPL RFYVQGSPWV SVVDRVAEQM
     YQPQQTACSD XALIVQK