ID A0A0A6YWI7_MOUSE Unreviewed; 189 AA. AC A0A0A6YWI7; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 5. DT 24-JUL-2024, entry version 55. 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|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {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 (APR-2024) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; A0A0A6YWI7; -. DR SMR; A0A0A6YWI7; -. DR ProteomicsDB; 351032; -. DR Antibodypedia; 34705; 397 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 Endonuclease {ECO:0000256|ARBA:ARBA00022759}; 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|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 //