DPOE3_RAT
ID DPOE3_RAT Reviewed; 145 AA.
AC Q642A5;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=DNA polymerase epsilon subunit 3;
DE AltName: Full=DNA polymerase II subunit 3;
DE AltName: Full=DNA polymerase epsilon subunit p17;
GN Name=Pole3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Accessory component of the DNA polymerase epsilon complex (By
CC similarity). Participates in DNA repair and in chromosomal DNA
CC replication (By similarity). Forms a complex with CHRAC1 and binds
CC naked DNA, which is then incorporated into chromatin, aided by the
CC nucleosome-remodeling activity of ISWI/SNF2H and ACF1 (By similarity).
CC Does not enhance nucleosome sliding activity of the ACF-5 ISWI
CC chromatin remodeling complex (By similarity).
CC {ECO:0000250|UniProtKB:Q04603, ECO:0000250|UniProtKB:Q9NRF9}.
CC -!- SUBUNIT: Component of the DNA polymerase epsilon complex consisting of
CC four subunits: the catalytic subunit POLE and the accessory subunits
CC POLE2, POLE3 and POLE4. Interaction with POLE4 is a prerequisite for
CC further binding with POLE and POLE2. Heterodimer with CHRAC1; binds to
CC DNA (By similarity). Component of the CHRAC ISWI chromatin remodeling
CC complex at least composed of SMARCA5/SNF2H, BAZ1A/ACF1, CHRAC1 and
CC POLE3; the complex preferentially binds DNA through the CHRAC1-POLE3
CC heterodimer and possesses ATP-dependent nucleosome-remodeling activity
CC (By similarity). Within the complex, the heterodimer with CHRAC1
CC interacts with SMARCA5/SNF2H; the interaction is direct and enhances
CC nucleosome sliding activity by the SMARCA5/SNF2H and BAZ1A/ACF1
CC interaction (By similarity). Within the complex, the heterodimer with
CC CHRAC1 interacts with BAZ1A/ACF1; the interactions are direct (By
CC similarity). {ECO:0000250|UniProtKB:Q9NRF9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; BC081988; AAH81988.1; -; mRNA.
DR EMBL; BC083800; AAH83800.1; -; mRNA.
DR RefSeq; NP_001007653.1; NM_001007652.2.
DR RefSeq; XP_002726991.1; XM_002726945.5.
DR RefSeq; XP_002729875.1; XM_002729829.5.
DR AlphaFoldDB; Q642A5; -.
DR SMR; Q642A5; -.
DR STRING; 10116.ENSRNOP00000006416; -.
DR iPTMnet; Q642A5; -.
DR PhosphoSitePlus; Q642A5; -.
DR jPOST; Q642A5; -.
DR PaxDb; Q642A5; -.
DR PRIDE; Q642A5; -.
DR Ensembl; ENSRNOT00000006416; ENSRNOP00000006416; ENSRNOG00000004843.
DR GeneID; 100362333; -.
DR GeneID; 298098; -.
DR KEGG; rno:100362333; -.
DR KEGG; rno:298098; -.
DR UCSC; RGD:1359475; rat.
DR CTD; 54107; -.
DR RGD; 1359475; Pole3.
DR eggNOG; KOG0870; Eukaryota.
DR GeneTree; ENSGT00940000161417; -.
DR HOGENOM; CLU_066247_7_2_1; -.
DR InParanoid; Q642A5; -.
DR OMA; KQNHRTI; -.
DR OrthoDB; 1572458at2759; -.
DR PhylomeDB; Q642A5; -.
DR TreeFam; TF103008; -.
DR Reactome; R-RNO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-RNO-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-RNO-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-RNO-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-RNO-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-RNO-5696400; Dual Incision in GG-NER.
DR Reactome; R-RNO-6782135; Dual incision in TC-NER.
DR Reactome; R-RNO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-RNO-68952; DNA replication initiation.
DR Reactome; R-RNO-68962; Activation of the pre-replicative complex.
DR PRO; PR:Q642A5; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004843; Expressed in testis and 19 other tissues.
DR Genevisible; Q642A5; RN.
DR GO; GO:0140672; C:ATAC complex; ISO:RGD.
DR GO; GO:0008623; C:CHRAC; IBA:GO_Central.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; ISS:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; ISO:RGD.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; ISO:RGD.
DR GO; GO:0006261; P:DNA-templated DNA replication; ISO:RGD.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:RGD.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; ISO:RGD.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:RGD.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NRF9"
FT CHAIN 2..145
FT /note="DNA polymerase epsilon subunit 3"
FT /id="PRO_0000208344"
FT REGION 93..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 85..144
FT /evidence="ECO:0000255"
FT COMPBIAS 93..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..145
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRF9"
FT MOD_RES 83
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRF9"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 145 AA; 16674 MW; 6CB14ED20FE15EC1 CRC64;
MAERPEDLNL PNAVITRIIK EALPDGVNIS KEARSAISRA ASVFVLYATS CANNFAMKGK
RKTLNASDVL SAMEEMEFQR FVTPLKEALE AYRREQKGKK EASEQKKKDK DKKDCEEQDK
SREEEDEDEE RLDEEEQNEE EEVDN
