UNG_ARATH
ID UNG_ARATH Reviewed; 330 AA.
AC Q9LIH6;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Uracil-DNA glycosylase, mitochondrial {ECO:0000303|PubMed:20056608};
DE Short=AtUNG {ECO:0000303|PubMed:20056608};
DE Short=UDG;
DE EC=3.2.2.27 {ECO:0000269|PubMed:20056608};
DE Flags: Precursor;
GN Name=UNG {ECO:0000303|PubMed:20056608};
GN OrderedLocusNames=At3g18630 {ECO:0000312|Araport:AT3G18630};
GN ORFNames=K24M9.12 {ECO:0000312|EMBL:BAB02221.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF ASP-173, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20056608; DOI=10.1074/jbc.m109.067173;
RA Cordoba-Canero D., Dubois E., Ariza R.R., Doutriaux M.P., Roldan-Arjona T.;
RT "Arabidopsis uracil DNA glycosylase (UNG) is required for base excision
RT repair of uracil and increases plant sensitivity to 5-fluorouracil.";
RL J. Biol. Chem. 285:7475-7483(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=19625491; DOI=10.1093/nar/gkp606;
RA Boesch P., Ibrahim N., Paulus F., Cosset A., Tarasenko V., Dietrich A.;
RT "Plant mitochondria possess a short-patch base excision DNA repair
RT pathway.";
RL Nucleic Acids Res. 37:5690-5700(2009).
CC -!- FUNCTION: Excises uracil residues from the DNA which can arise as a
CC result of misincorporation of dUMP residues by DNA polymerase or due to
CC deamination of cytosine. More active on U:G, U:T and U:C mispairs than
CC on U:A pairs. Highly specific for uracil and no activity with 5-
CC substituted uracil or cytosine derivatives. Required for initiation of
CC base excision repair (BER) of uracil. {ECO:0000269|PubMed:19625491,
CC ECO:0000269|PubMed:20056608}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded
CC DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27;
CC Evidence={ECO:0000269|PubMed:20056608};
CC -!- ACTIVITY REGULATION: Inhidited by the small peptide uracil-DNA-
CC glycosylase inhibitor (Ugi). {ECO:0000269|PubMed:20056608}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19625491}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under standard growth
CC conditions. Increased resistance to 5-fluorouracil cytotoxicity.
CC {ECO:0000269|PubMed:20056608}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000305}.
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DR EMBL; AP001303; BAB02221.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76124.1; -; Genomic_DNA.
DR EMBL; BT029175; ABJ17110.1; -; mRNA.
DR EMBL; AY084956; AAM61517.1; -; mRNA.
DR RefSeq; NP_188493.1; NM_112749.5.
DR AlphaFoldDB; Q9LIH6; -.
DR SMR; Q9LIH6; -.
DR STRING; 3702.AT3G18630.1; -.
DR iPTMnet; Q9LIH6; -.
DR PaxDb; Q9LIH6; -.
DR PRIDE; Q9LIH6; -.
DR ProteomicsDB; 245277; -.
DR EnsemblPlants; AT3G18630.1; AT3G18630.1; AT3G18630.
DR GeneID; 821394; -.
DR Gramene; AT3G18630.1; AT3G18630.1; AT3G18630.
DR KEGG; ath:AT3G18630; -.
DR Araport; AT3G18630; -.
DR TAIR; locus:2086904; AT3G18630.
DR eggNOG; KOG2994; Eukaryota.
DR HOGENOM; CLU_032162_2_1_1; -.
DR InParanoid; Q9LIH6; -.
DR OMA; PDNGYLM; -.
DR OrthoDB; 832568at2759; -.
DR PhylomeDB; Q9LIH6; -.
DR BRENDA; 3.2.2.27; 399.
DR PRO; PR:Q9LIH6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIH6; baseline and differential.
DR Genevisible; Q9LIH6; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:TAIR.
DR GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; IBA:GO_Central.
DR CDD; cd10027; UDG-F1-like; 1.
DR Gene3D; 3.40.470.10; -; 1.
DR HAMAP; MF_00148; UDG; 1.
DR InterPro; IPR002043; UDG_fam1.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR PANTHER; PTHR11264; PTHR11264; 1.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SUPFAM; SSF52141; SSF52141; 1.
DR TIGRFAMs; TIGR00628; ung; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Hydrolase; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 50..330
FT /note="Uracil-DNA glycosylase, mitochondrial"
FT /id="PRO_0000433479"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03166"
FT MUTAGEN 173
FT /note="D->N: Strongly reduced glycosylase activity."
FT /evidence="ECO:0000269|PubMed:20056608"
SQ SEQUENCE 330 AA; 36289 MW; 696BC91977309E19 CRC64;
MASSTPKTLM DFFQPAKRLK ASPSSSSFPA VSVAGGSRDL GSVANSPPRV TVTTSVADDS
SGLTPEQIAR AEFNKFVAKS KRNLAVCSER VTKAKSEGNC YVPLSELLVE ESWLKALPGE
FHKPYAKSLS DFLEREIITD SKSPLIYPPQ HLIFNALNTT PFDRVKTVII GQDPYHGPGQ
AMGLSFSVPE GEKLPSSLLN IFKELHKDVG CSIPRHGNLQ KWAVQGVLLL NAVLTVRSKQ
PNSHAKKGWE QFTDAVIQSI SQQKEGVVFL LWGRYAQEKS KLIDATKHHI LTAAHPSGLS
ANRGFFDCRH FSRANQLLEE MGIPPIDWQL
