ID Q3TBY2_MOUSE Unreviewed; 410 AA. AC Q3TBY2; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 02-OCT-2024, entry version 86. DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029}; DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029}; DE Flags: Fragment; GN Name=Pole {ECO:0000313|MGI:MGI:1196391}; 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|EMBL:BAE42175.1}; RN [1] {ECO:0000313|EMBL:BAE42175.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42175.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAE42175.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42175.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare RT full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAE42175.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42175.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R., RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing RT pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAE42175.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42175.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAE42175.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42175.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [6] {ECO:0000313|EMBL:BAE42175.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42175.1}; RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F., RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M., RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K., RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T., RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAE42175.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42175.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] {ECO:0000313|EMBL:BAE42175.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42175.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). CC -!- FUNCTION: DNA polymerase II participates in chromosomal DNA CC replication. {ECO:0000256|RuleBase:RU365029}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, CC ChEBI:CHEBI:173112; EC=2.7.7.7; CC Evidence={ECO:0000256|RuleBase:RU365029}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|RuleBase:RU365029}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365029}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. CC {ECO:0000256|RuleBase:RU365029}. 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 EMBL; AK171004; BAE42175.1; -; mRNA. DR AlphaFoldDB; Q3TBY2; -. DR PeptideAtlas; Q3TBY2; -. DR AGR; MGI:1196391; -. DR MGI; MGI:1196391; Pole. DR ChiTaRS; Pole; mouse. DR GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0008310; F:single-stranded DNA 3'-5' DNA exonuclease activity; IEA:TreeGrafter. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006287; P:base-excision repair, gap-filling; IEA:TreeGrafter. DR GO; GO:0045004; P:DNA replication proofreading; IEA:TreeGrafter. DR GO; GO:0006272; P:leading strand elongation; IEA:TreeGrafter. DR GO; GO:0000278; P:mitotic cell cycle; IEA:TreeGrafter. DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IEA:TreeGrafter. DR InterPro; IPR013697; DNA_pol_e_suA_C. DR InterPro; IPR029703; POL2. DR PANTHER; PTHR10670; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1. DR PANTHER; PTHR10670:SF1; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1. DR Pfam; PF08490; DUF1744; 1. DR Pfam; PF22912; zf-DPOE; 1. PE 2: Evidence at transcript level; KW 4Fe-4S {ECO:0000256|RuleBase:RU365029}; KW DNA replication {ECO:0000256|RuleBase:RU365029}; KW DNA-binding {ECO:0000256|RuleBase:RU365029}; KW DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU365029}; KW Iron {ECO:0000256|RuleBase:RU365029}; KW Iron-sulfur {ECO:0000256|RuleBase:RU365029}; KW Metal-binding {ECO:0000256|RuleBase:RU365029}; KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU365029}; KW Nucleus {ECO:0000256|RuleBase:RU365029}; KW Transferase {ECO:0000256|RuleBase:RU365029}; KW Zinc {ECO:0000256|RuleBase:RU365029}; KW Zinc-finger {ECO:0000256|RuleBase:RU365029}. FT DOMAIN 19..51 FT /note="DNA polymerase epsilon catalytic subunit A C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF08490" FT REGION 62..95 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 141..168 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 72..95 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 149..168 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAE42175.1" SQ SEQUENCE 410 AA; 46424 MW; 6F6C58F59DEA1AC3 CRC64; SFSMLGSLGD CLNPLEVHFI HSKEIFHSLT ISFSRCWEFL LWMDPSNYGG IKGKVPSSIH CGQVKEQDSQ AREETDEEEE DKEKDEEEEG MGESEVEDLL ENNWNILQFL PQAASCQSYF LMIVSAYIVA VYQSMKEELR HSAPGSTPVK RKGASQFSQE SEGATGSLPG MITFSQDYVA NELTQSFFTI TQKIQKKVTG SRNTTEPSEM FPILPGSHLL LNNPALEFIK YVCKVLSLDT NITNQVNKLN RDLLRLVDVG EFSEEAQFRD PCHSYVLPEV ICHSCNFCRD LDLCKDSSFS QDGAILPQWL CSNCQAPYDS SAIESALVEA LQRKLMAFTL QDLVCLKCRG MKETHMPVYC SCAGDFTLTI RTEVFMEQIR IFQNIAKYYS MSYLQETIEW LLQTSPVSNC //