SMUG1_MOUSE
ID SMUG1_MOUSE Reviewed; 279 AA.
AC Q6P5C5; Q9DBV1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Single-strand selective monofunctional uracil DNA glycosylase;
DE EC=3.2.2.-;
GN Name=Smug1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK004735; BAB23517.1; -; mRNA.
DR EMBL; BC050253; AAH50253.1; -; mRNA.
DR EMBL; BC062960; AAH62960.1; -; mRNA.
DR CCDS; CCDS27898.1; -.
DR RefSeq; NP_082161.2; NM_027885.3.
DR RefSeq; XP_006521478.1; XM_006521415.3.
DR RefSeq; XP_011244033.1; XM_011245731.2.
DR RefSeq; XP_011244034.1; XM_011245732.2.
DR RefSeq; XP_011244035.1; XM_011245733.2.
DR RefSeq; XP_017172241.1; XM_017316752.1.
DR AlphaFoldDB; Q6P5C5; -.
DR SMR; Q6P5C5; -.
DR IntAct; Q6P5C5; 1.
DR STRING; 10090.ENSMUSP00000065835; -.
DR iPTMnet; Q6P5C5; -.
DR PhosphoSitePlus; Q6P5C5; -.
DR EPD; Q6P5C5; -.
DR MaxQB; Q6P5C5; -.
DR PaxDb; Q6P5C5; -.
DR PeptideAtlas; Q6P5C5; -.
DR PRIDE; Q6P5C5; -.
DR ProteomicsDB; 257531; -.
DR Antibodypedia; 27322; 289 antibodies from 31 providers.
DR DNASU; 71726; -.
DR Ensembl; ENSMUST00000064067; ENSMUSP00000065835; ENSMUSG00000036061.
DR Ensembl; ENSMUST00000229371; ENSMUSP00000155594; ENSMUSG00000036061.
DR Ensembl; ENSMUST00000229377; ENSMUSP00000155700; ENSMUSG00000036061.
DR GeneID; 71726; -.
DR KEGG; mmu:71726; -.
DR UCSC; uc007xxh.1; mouse.
DR CTD; 23583; -.
DR MGI; MGI:1918976; Smug1.
DR VEuPathDB; HostDB:ENSMUSG00000036061; -.
DR eggNOG; ENOG502QT20; Eukaryota.
DR GeneTree; ENSGT00390000004897; -.
DR HOGENOM; CLU_071760_2_0_1; -.
DR InParanoid; Q6P5C5; -.
DR OMA; VANYCPL; -.
DR OrthoDB; 960725at2759; -.
DR PhylomeDB; Q6P5C5; -.
DR TreeFam; TF324356; -.
DR BRENDA; 3.2.2.27; 3474.
DR Reactome; R-MMU-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-MMU-110357; Displacement of DNA glycosylase by APEX1.
DR BioGRID-ORCS; 71726; 5 hits in 107 CRISPR screens.
DR ChiTaRS; Smug1; mouse.
DR PRO; PR:Q6P5C5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q6P5C5; protein.
DR Bgee; ENSMUSG00000036061; Expressed in secondary oocyte and 223 other tissues.
DR ExpressionAtlas; Q6P5C5; baseline and differential.
DR Genevisible; Q6P5C5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:HGNC-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0019104; F:DNA N-glycosylase activity; ISS:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000702; F:oxidized base lesion DNA N-glycosylase activity; ISA:MGI.
DR GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; ISO:MGI.
DR GO; GO:0017065; F:single-strand selective uracil DNA N-glycosylase activity; ISS:HGNC-UCL.
DR GO; GO:0003697; F:single-stranded DNA binding; ISA:MGI.
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 GO; GO:0006281; P:DNA repair; ISA:MGI.
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 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA-binding; Hydrolase; Nucleus;
KW Reference proteome.
FT CHAIN 1..279
FT /note="Single-strand selective monofunctional uracil DNA
FT glycosylase"
FT /id="PRO_0000071993"
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"
FT CONFLICT 239
FT /note="L -> H (in Ref. 1; BAB23517)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 30654 MW; B7B70857B8351AED CRC64;
MAASQTFPLG PTHEPASALM EPLPCTRSLA EGFLEEELRL NAELSQLQFP EPVGVIYNPV
DYAWEPHRNY VTRYCQGPKE VLFLGMNPGP FGMAQTGVPF GEVNVVRDWL GVGGPVLTPP
QEHPKRPVLG LECPQSEVSG ARFWGFFRTL CGQPQVFFRH CFVHNLCPLL FLAPSGRNLT
PAELPAKQRE QLLSICDAAL CRQVQLLGVR LVVGVGRLAE QRARRALAGL TPEVQVEGLL
HPSPRSAQAN KGWEAAARER LQELGLLPLL TDEGSARPT
