DPOE3_BOVIN
ID DPOE3_BOVIN Reviewed; 147 AA.
AC Q3SZN5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=DNA polymerase epsilon subunit 3;
DE AltName: Full=DNA polymerase II subunit 3;
GN Name=POLE3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; BT030577; ABQ13017.1; -; mRNA.
DR EMBL; BC102772; AAI02773.1; -; mRNA.
DR RefSeq; NP_001029562.1; NM_001034390.1.
DR AlphaFoldDB; Q3SZN5; -.
DR SMR; Q3SZN5; -.
DR STRING; 9913.ENSBTAP00000000316; -.
DR PaxDb; Q3SZN5; -.
DR PRIDE; Q3SZN5; -.
DR Ensembl; ENSBTAT00000000316; ENSBTAP00000000316; ENSBTAG00000000252.
DR GeneID; 510678; -.
DR KEGG; bta:510678; -.
DR CTD; 54107; -.
DR VEuPathDB; HostDB:ENSBTAG00000000252; -.
DR VGNC; VGNC:33120; POLE3.
DR eggNOG; KOG0870; Eukaryota.
DR GeneTree; ENSGT00940000161417; -.
DR HOGENOM; CLU_066247_7_2_1; -.
DR InParanoid; Q3SZN5; -.
DR OMA; KQNHRTI; -.
DR OrthoDB; 1572458at2759; -.
DR TreeFam; TF103008; -.
DR Reactome; R-BTA-68962; Activation of the pre-replicative complex.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000000252; Expressed in caput epididymis and 108 other tissues.
DR GO; GO:0140672; C:ATAC complex; IEA:Ensembl.
DR GO; GO:0008623; C:CHRAC; IBA:GO_Central.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; ISS:UniProtKB.
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:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; IEA:Ensembl.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IEA:Ensembl.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:Ensembl.
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 2: Evidence at transcript 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..147
FT /note="DNA polymerase epsilon subunit 3"
FT /id="PRO_0000328526"
FT REGION 93..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 85..146
FT /evidence="ECO:0000255"
FT COMPBIAS 93..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..147
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 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRF9"
SQ SEQUENCE 147 AA; 16860 MW; DC0A4D2097046569 CRC64;
MAERPEDLNL PNAVITRIIK EALPDGVNIS KEARSAISRA ASVFVLYATS CANNFAMKGK
RKTLNASDVL SAMEEMEFQR FVTPLKEALE AYRREQKGKK EASEQKKKDK DKKTDSEEQD
KSRDEDNDED EERLEEEEQN EEEEVDN
