ID A0A0A6YWI7_MOUSE Unreviewed; 189 AA.
AC A0A0A6YWI7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 5.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
DE Flags: Fragment;
GN Name=Exo1 {ECO:0000313|Ensembl:ENSMUSP00000141568.2,
GN ECO:0000313|MGI:MGI:1349427};
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 {ECO:0000313|Ensembl:ENSMUSP00000141568.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000141568.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000141568.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000141568.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000141568.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: 5'->3' double-stranded DNA exonuclease which may also possess
CC a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in
CC DNA mismatch repair. {ECO:0000256|RuleBase:RU910737}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU910737};
CC Note=Binds 2 magnesium ions per subunit. They probably participate in
CC the reaction catalyzed by the enzyme. May bind an additional third
CC magnesium ion after substrate binding. {ECO:0000256|RuleBase:RU910737};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU910737}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC subfamily. {ECO:0000256|RuleBase:RU910737}.
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DR AlphaFoldDB; A0A0A6YWI7; -.
DR SMR; A0A0A6YWI7; -.
DR ProteomicsDB; 351032; -.
DR Antibodypedia; 34705; 437 antibodies from 34 providers.
DR Ensembl; ENSMUST00000193858.2; ENSMUSP00000141568.2; ENSMUSG00000039748.12.
DR AGR; MGI:1349427; -.
DR MGI; MGI:1349427; Exo1.
DR VEuPathDB; HostDB:ENSMUSG00000039748; -.
DR GeneTree; ENSGT00510000047676; -.
DR ChiTaRS; Exo1; mouse.
DR Proteomes; UP000000589; Chromosome 1.
DR Bgee; ENSMUSG00000039748; Expressed in epiblast (generic) and 195 other cell types or tissues.
DR ExpressionAtlas; A0A0A6YWI7; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035312; F:5'-3' DNA exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd09857; PIN_EXO1; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR044752; PIN-like_EXO1.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR019974; XPG_CS.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR11081:SF8; EXONUCLEASE 1; 1.
DR PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 1: Evidence at protein level;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU910737};
KW DNA excision {ECO:0000256|RuleBase:RU910737};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU910737};
KW DNA-binding {ECO:0000256|RuleBase:RU910737};
KW Excision nuclease {ECO:0000256|RuleBase:RU910737};
KW Exonuclease {ECO:0000256|RuleBase:RU910737};
KW Hydrolase {ECO:0000256|RuleBase:RU910737};
KW Magnesium {ECO:0000256|RuleBase:RU910737};
KW Metal-binding {ECO:0000256|RuleBase:RU910737};
KW Nuclease {ECO:0000256|RuleBase:RU910737};
KW Nucleus {ECO:0000256|RuleBase:RU910737};
KW Proteomics identification {ECO:0007829|EPD:A0A0A6YWI7,
KW ECO:0007829|ProteomicsDB:A0A0A6YWI7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 1..83
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 98..168
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT NON_TER 189
FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000141568.2"
SQ SEQUENCE 189 AA; 20790 MW; 135EDB2E0C756246 CRC64;
MGIQGLLQFI QEASEPVNVK KYKGQAVAVD TYCWLHKGAI ACAEKLAKGE PTDRRRQSNL
LKGKQLLREG KVSEARDCFA RSINITHAMA HKVIKAARAL GVDCLVAPYE ADAQLAYLNK
AGIVQAVITE DSDLLAFGCK KVILKMDQFG NGLEVDQARL GMCKQLGDVF TEEKFRYMCI
LSGCDYLAS
//
