ID   SMUG1_BOVIN             Reviewed;         272 AA.
AC   Q59I47; A6QLX7;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Single-strand selective monofunctional uracil DNA glycosylase;
DE            EC=3.2.2.-;
GN   Name=SMUG1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=15771722; DOI=10.1111/j.1365-2052.2005.01231.x;
RA   Ihara N., Fujita T., Shiga K., Itoh M., Watanabe T., Sugimoto Y.;
RT   "Linkage analysis reveals two independent loci for ocular disorders in a
RT   local Japanese Black cattle population.";
RL   Anim. Genet. 36:132-134(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal brain;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q53HV7}.
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; AB195271; BAD91385.1; -; mRNA.
DR   EMBL; BC148122; AAI48123.1; -; mRNA.
DR   RefSeq; NP_001014958.1; NM_001014958.1.
DR   RefSeq; XP_005206225.1; XM_005206168.2.
DR   RefSeq; XP_005206226.1; XM_005206169.3.
DR   RefSeq; XP_015326436.1; XM_015470950.1.
DR   AlphaFoldDB; Q59I47; -.
DR   SMR; Q59I47; -.
DR   STRING; 9913.ENSBTAP00000029297; -.
DR   PaxDb; Q59I47; -.
DR   PRIDE; Q59I47; -.
DR   Ensembl; ENSBTAT00000029297; ENSBTAP00000029297; ENSBTAG00000021974.
DR   GeneID; 539771; -.
DR   KEGG; bta:539771; -.
DR   CTD; 23583; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021974; -.
DR   VGNC; VGNC:35039; SMUG1.
DR   eggNOG; ENOG502QT20; Eukaryota.
DR   GeneTree; ENSGT00390000004897; -.
DR   HOGENOM; CLU_071760_2_0_1; -.
DR   InParanoid; Q59I47; -.
DR   OMA; VANYCPL; -.
DR   OrthoDB; 960725at2759; -.
DR   TreeFam; TF324356; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000021974; Expressed in subcutaneous adipose tissue and 102 other tissues.
DR   ExpressionAtlas; Q59I47; baseline and differential.
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; IDA:HGNC-UCL.
DR   GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IBA:GO_Central.
DR   GO; GO:0017065; F:single-strand selective uracil DNA N-glycosylase activity; ISS:HGNC-UCL.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; ISS:HGNC-UCL.
DR   GO; GO:0006284; P:base-excision repair; ISS:HGNC-UCL.
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..272
FT                   /note="Single-strand selective monofunctional uracil DNA
FT                   glycosylase"
FT                   /id="PRO_0000071991"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..189
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   272 AA;  30040 MW;  803EC9A29D9D3E16 CRC64;
     MAVPQPFPSG PHLQPAGALM EPQPSPRSLA EGFLQEELRL NDELRQLQFS ELVGIVYNPV
     EYAWEPHRSY VTRYCQGPKQ VLFLGMNPGP FGMAQTGVPF GEVSVVRDWL GLGGPVRTPP
     QEHPKRPVLG LECPQSEVSG ARFWGFFRNL CGQPEVFFRH CFVHNLCPLL LLAPSGRNIT
     PAELPAKQRE QLLGVCDAAL CRQVQLLGVR LVVGVGRVAE QRARRALASL MPEVQVEGLL
     HPSPRSPQAN KGWEAVAKER LNELGLLPLL TS