ID   DPOE3_PONAB             Reviewed;         147 AA.
AC   Q5R4W3;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR861128; CAH93203.1; -; mRNA.
DR   RefSeq; NP_001126884.1; NM_001133412.1.
DR   AlphaFoldDB; Q5R4W3; -.
DR   SMR; Q5R4W3; -.
DR   STRING; 9601.ENSPPYP00000021877; -.
DR   Ensembl; ENSPPYT00000022775; ENSPPYP00000021877; ENSPPYG00000019522.
DR   GeneID; 100173898; -.
DR   KEGG; pon:100173898; -.
DR   CTD; 54107; -.
DR   eggNOG; KOG0870; Eukaryota.
DR   GeneTree; ENSGT00940000161417; -.
DR   HOGENOM; CLU_066247_7_2_1; -.
DR   InParanoid; Q5R4W3; -.
DR   OMA; KQNHRTI; -.
DR   OrthoDB; 1572458at2759; -.
DR   TreeFam; TF103008; -.
DR   Proteomes; UP000001595; Chromosome 9.
DR   GO; GO:0140672; C:ATAC complex; IEA:Ensembl.
DR   GO; GO:0008622; C:epsilon DNA polymerase complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:Ensembl.
DR   GO; GO:0043966; P:histone H3 acetylation; IEA:Ensembl.
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_0000208343"
FT   REGION          93..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          85..144
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