ID   SMUG1_RAT               Reviewed;         278 AA.
AC   Q811Q1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Single-strand selective monofunctional uracil-DNA glycosylase;
DE            EC=3.2.2.-;
GN   Name=Smug1;
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], AND FUNCTION.
RC   STRAIN=Wistar; TISSUE=Kidney;
RX   PubMed=12718543; DOI=10.1021/bi0273213;
RA   Masaoka A., Matsubara M., Hasegawa R., Tanaka T., Kurisu S., Terato H.,
RA   Ohyama Y., Karino N., Matsuda A., Ide H.;
RT   "Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA
RT   glycosylase in repair of 5-formyluracil and other oxidized and deaminated
RT   base lesions.";
RL   Biochemistry 42:5003-5012(2003).
CC   -!- FUNCTION: Recognizes base lesions in the genome and initiates base
CC       excision DNA repair. Acts as a monofunctional DNA glycosylase specific
CC       for uracil (U) residues in DNA with a preference for single-stranded
CC       DNA substrates. The activity is greater toward mismatches (U/G)
CC       compared to matches (U/A). Excises uracil (U), 5-formyluracil (fU) and
CC       uracil derivatives bearing an oxidized group at C5 [5-hydroxyuracil
CC       (hoU) and 5-hydroxymethyluracil (hmU)] in ssDNA and dsDNA, but not
CC       analogous cytosine derivatives (5-hydroxycytosine and 5-
CC       formylcytosine), nor other oxidized bases. The activity is damage-
CC       specific and salt-dependent. The substrate preference is the following:
CC       ssDNA > dsDNA (G pair) = dsDNA (A pair) at low salt concentration, and
CC       dsDNA (G pair) > dsDNA (A pair) > ssDNA at high salt concentration.
CC       {ECO:0000269|PubMed:12718543}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q53HV7}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       SMUG1 family.
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DR   EMBL; AY191521; AAO38671.1; -; mRNA.
DR   RefSeq; NP_808795.1; NM_177934.3.
DR   RefSeq; XP_008763971.1; XM_008765749.2.
DR   RefSeq; XP_017450389.1; XM_017594900.1.
DR   RefSeq; XP_017450390.1; XM_017594901.1.
DR   RefSeq; XP_017450391.1; XM_017594902.1.
DR   AlphaFoldDB; Q811Q1; -.
DR   SMR; Q811Q1; -.
DR   STRING; 10116.ENSRNOP00000052164; -.
DR   PaxDb; Q811Q1; -.
DR   Ensembl; ENSRNOT00000082149; ENSRNOP00000069685; ENSRNOG00000036842.
DR   GeneID; 315344; -.
DR   KEGG; rno:315344; -.
DR   CTD; 23583; -.
DR   RGD; 631403; Smug1.
DR   eggNOG; ENOG502QT20; Eukaryota.
DR   GeneTree; ENSGT00390000004897; -.
DR   InParanoid; Q811Q1; -.
DR   OMA; VANYCPL; -.
DR   OrthoDB; 960725at2759; -.
DR   PhylomeDB; Q811Q1; -.
DR   TreeFam; TF324356; -.
DR   BRENDA; 3.2.2.27; 5301.
DR   Reactome; R-RNO-110329; Cleavage of the damaged pyrimidine.
DR   Reactome; R-RNO-110357; Displacement of DNA glycosylase by APEX1.
DR   PRO; PR:Q811Q1; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000036842; Expressed in stomach and 19 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; ISS:HGNC-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0019104; F:DNA N-glycosylase activity; ISO:RGD.
DR   GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IDA:RGD.
DR   GO; GO:0017065; F:single-strand selective uracil DNA N-glycosylase activity; IDA:HGNC-UCL.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:HGNC-UCL.
DR   GO; GO:0006284; P:base-excision repair; IDA:HGNC-UCL.
DR   GO; GO:0006281; P:DNA repair; IDA:RGD.
DR   CDD; cd19374; UDG-F3_SMUG1-like; 1.
DR   Gene3D; 3.40.470.10; -; 1.
DR   InterPro; IPR039134; SMUG1.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   PANTHER; PTHR13235; PTHR13235; 1.
DR   SUPFAM; SSF52141; SSF52141; 1.
PE   2: Evidence at transcript level;
KW   DNA damage; DNA repair; DNA-binding; Hydrolase; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..278
FT                   /note="Single-strand selective monofunctional uracil-DNA
FT                   glycosylase"
FT                   /id="PRO_0000071994"
FT   REGION          173..187
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   278 AA;  30562 MW;  C1A047F60AB76F56 CRC64;
     MAVSQTFPPG PAHEPASALM EPCARSLAEG FLEEELRLNA ELSQLQFPEP VGVIYNPVDY
     AWEPHRNYVT RYCQGPKEVL FLGMNPGPFG MAQTGVPFGE VNVVRDWLGI GGSVLSPPQE
     HPKRPVLGLE CPQSEVSGAR FWGFFRTLCG QPQVFFRHCF VHNLCPLLFL APSGRNLTPA
     DLPAKHREQL LSICDAALCR QVQLLGVRLV VGVGRLAEQR ARRALAGLTP EVQVEGLLHP
     SPRSPQANKG WETAARERLQ ELGLLPLLTD EGSVRPTP