UNG_CAEEL
ID UNG_CAEEL Reviewed; 282 AA.
AC Q9U221; H8ESG8; H8ESG9; Q95Q13;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166};
DE Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166};
DE EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166, ECO:0000269|PubMed:18524757, ECO:0000269|PubMed:20493785};
GN Name=ung-1 {ECO:0000312|WormBase:Y56A3A.29a};
GN ORFNames=Y56A3A.29 {ECO:0000312|WormBase:Y56A3A.29a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=18524757; DOI=10.1093/mutage/gen030;
RA Nakamura N., Morinaga H., Kikuchi M., Yonekura S., Ishii N., Yamamoto K.,
RA Yonei S., Zhang Q.M.;
RT "Cloning and characterization of uracil-DNA glycosylase and the biological
RT consequences of the loss of its function in the nematode Caenorhabditis
RT elegans.";
RL Mutagenesis 23:407-413(2008).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=20493785; DOI=10.1016/j.dnarep.2010.04.009;
RA Skjeldam H.K., Kassahun H., Fensgaard O., SenGupta T., Babaie E.,
RA Lindvall J.M., Arczewska K., Nilsen H.;
RT "Loss of Caenorhabditis elegans UNG-1 uracil-DNA glycosylase affects
RT apoptosis in response to DNA damaging agents.";
RL DNA Repair 9:861-870(2010).
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. {ECO:0000255|HAMAP-Rule:MF_03166,
CC ECO:0000269|PubMed:18524757, ECO:0000269|PubMed:20493785}.
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:0000255|HAMAP-Rule:MF_03166,
CC ECO:0000269|PubMed:18524757, ECO:0000269|PubMed:20493785};
CC -!- ACTIVITY REGULATION: Inhibited by UGI, a B.subtilis bacteriophage PBS2
CC peptide inhibitor. {ECO:0000269|PubMed:18524757,
CC ECO:0000269|PubMed:20493785}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 26 degrees Celsius.
CC {ECO:0000269|PubMed:18524757};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03166}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03166, ECO:0000269|PubMed:20493785}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=a {ECO:0000312|WormBase:Y56A3A.29a};
CC IsoId=Q9U221-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y56A3A.29b};
CC IsoId=Q9U221-2; Sequence=VSP_058449, VSP_058450;
CC Name=c {ECO:0000312|WormBase:Y56A3A.29c};
CC IsoId=Q9U221-3; Sequence=VSP_058448, VSP_058449, VSP_058450;
CC Name=d {ECO:0000312|WormBase:Y56A3A.29d};
CC IsoId=Q9U221-4; Sequence=VSP_058448;
CC -!- DISRUPTION PHENOTYPE: Severe loss of unracil exision activity.
CC Increased number of germ-cell corpses in response DNA damage induced by
CC ionizing radiation. {ECO:0000269|PubMed:20493785}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000255|HAMAP-Rule:MF_03166}.
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DR EMBL; BX284603; CAB60520.1; -; Genomic_DNA.
DR EMBL; BX284603; CAC42381.1; -; Genomic_DNA.
DR EMBL; BX284603; CCG28084.1; -; Genomic_DNA.
DR EMBL; BX284603; CCG28085.1; -; Genomic_DNA.
DR RefSeq; NP_001255148.1; NM_001268219.1. [Q9U221-4]
DR RefSeq; NP_001255149.1; NM_001268220.1. [Q9U221-3]
DR RefSeq; NP_499560.1; NM_067159.5. [Q9U221-1]
DR RefSeq; NP_499561.1; NM_067160.4. [Q9U221-2]
DR AlphaFoldDB; Q9U221; -.
DR SMR; Q9U221; -.
DR STRING; 6239.Y56A3A.29a; -.
DR EPD; Q9U221; -.
DR PaxDb; Q9U221; -.
DR PeptideAtlas; Q9U221; -.
DR EnsemblMetazoa; Y56A3A.29a.1; Y56A3A.29a.1; WBGene00013241. [Q9U221-1]
DR EnsemblMetazoa; Y56A3A.29b.1; Y56A3A.29b.1; WBGene00013241. [Q9U221-2]
DR EnsemblMetazoa; Y56A3A.29c.1; Y56A3A.29c.1; WBGene00013241. [Q9U221-3]
DR EnsemblMetazoa; Y56A3A.29d.1; Y56A3A.29d.1; WBGene00013241. [Q9U221-4]
DR GeneID; 176633; -.
DR KEGG; cel:CELE_Y56A3A.29; -.
DR UCSC; Y56A3A.29a; c. elegans.
DR CTD; 176633; -.
DR WormBase; Y56A3A.29a; CE22594; WBGene00013241; ung-1. [Q9U221-1]
DR WormBase; Y56A3A.29b; CE28139; WBGene00013241; ung-1. [Q9U221-2]
DR WormBase; Y56A3A.29c; CE47304; WBGene00013241; ung-1. [Q9U221-3]
DR WormBase; Y56A3A.29d; CE47197; WBGene00013241; ung-1. [Q9U221-4]
DR eggNOG; KOG2994; Eukaryota.
DR GeneTree; ENSGT00390000003405; -.
DR InParanoid; Q9U221; -.
DR OMA; PDNGYLM; -.
DR OrthoDB; 832568at2759; -.
DR PhylomeDB; Q9U221; -.
DR Reactome; R-CEL-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-CEL-110357; Displacement of DNA glycosylase by APEX1.
DR PRO; PR:Q9U221; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00013241; Expressed in embryo and 4 other tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:WormBase.
DR GO; GO:0006284; P:base-excision repair; IDA:WormBase.
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 Alternative splicing; DNA damage; DNA repair; Hydrolase; Mitochondrion;
KW Nucleus; Reference proteome.
FT CHAIN 1..282
FT /note="Uracil-DNA glycosylase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436926"
FT REGION 15..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03166"
FT VAR_SEQ 1..44
FT /note="Missing (in isoform c and isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_058448"
FT VAR_SEQ 63..95
FT /note="GESWSKLLEEEFKKGYISKIEKFLNSEVNKGKQ -> DRPSVSAECSQVVGM
FT QMLLEMQHGARKFRSKPD (in isoform b and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058449"
FT VAR_SEQ 96..282
FT /note="Missing (in isoform b and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058450"
SQ SEQUENCE 282 AA; 31894 MW; A0814C43077E64BE CRC64;
MSKTVRIPDM FLKASAASKR KSASNTENIP EKVPAGNENQ EVKKMKLQAP EPTEILLKSL
LTGESWSKLL EEEFKKGYIS KIEKFLNSEV NKGKQVFPPP TQIFTTFNLL PFDEISVVII
GQDPYHDDNQ AHGLSFSVQK GVKPPPSLKN IYKELESDIE GFKRPDHGNL LGWTRQGVFM
LNATLTVRAH EANSHAKIGW QTFTDTVIRI ISRQSEKPIV FLLWGGFAHK KEELIDTKKH
VVIKTAHPSP LSARKWWGCK CFSKCNTELE NSGRNPINWA DL
