DPOD4_BOVIN
ID DPOD4_BOVIN Reviewed; 107 AA.
AC Q3T0X9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=DNA polymerase delta subunit 4;
DE AltName: Full=DNA polymerase delta subunit p12;
GN Name=POLD4;
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] {ECO:0000312|EMBL:AAI02213.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI02213.1};
RC TISSUE=Ileum {ECO:0000312|EMBL:AAI02213.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 51-66, IDENTIFICATION IN POL-DELTA COMPLEX, AND MASS
RP SPECTROMETRY.
RC TISSUE=Thymus;
RX PubMed=10751307; DOI=10.1074/jbc.m001217200;
RA Liu L., Mo J.-Y., Rodriguez-Belmonte E.M., Lee M.Y.W.T.;
RT "Identification of a fourth subunit of mammalian DNA polymerase delta.";
RL J. Biol. Chem. 275:18739-18744(2000).
CC -!- FUNCTION: As a component of the tetrameric DNA polymerase delta 4
CC complex (Pol-delta4), plays a role in high fidelity genome replication
CC and repair. Within this complex, increases the rate of DNA synthesis
CC and decreases fidelity by regulating POLD1 polymerase and proofreading
CC 3' to 5' exonuclease activity. Pol-delta4 participates in Okazaki
CC fragment processing, through both the short flap pathway, as well as a
CC nick translation system. Under conditions of DNA replication stress,
CC required for the repair of broken replication forks through break-
CC induced replication (BIR), a mechanism that may induce segmental
CC genomic duplications of up to 200 kb. Involved in Pol-delta4
CC translesion synthesis (TLS) of templates carrying O6-methylguanine or
CC abasic sites. Its degradation in response to DNA damage is required for
CC the inhibition of fork progression and cell survival.
CC {ECO:0000250|UniProtKB:Q9HCU8}.
CC -!- SUBUNIT: Component of the tetrameric DNA polymerase delta complex (Pol-
CC delta4), which consists of POLD1/p125, POLD2/p50, POLD3/p66/p68 and
CC POLD4/p12, with POLD1 bearing DNA polymerase and 3' to 5' proofreading
CC exonuclease activities. Within this complex, directly interacts with
CC POLD1 and POLD2. Directly interacts with PCNA, as do POLD1 and POLD3;
CC this interaction stimulates Pol-delta4 polymerase activity. As POLD1
CC and POLD2, directly interacts with WRNIP1; this interaction stimulates
CC DNA polymerase delta-mediated DNA synthesis, independently of the
CC presence of PCNA, possibly by increasing initiation frequency. Upon
CC genotoxic stress induced by DNA damaging agents or by replication
CC stress, POLD4 is proteolytically degraded and Pol-delta4 is converted
CC into a trimeric form of the complex (Pol-delta3) that has an increased
CC proofreading activity. The DNA polymerase delta complex interacts with
CC POLDIP2; this interaction is probably mediated through direct binding
CC to POLD2. {ECO:0000250|UniProtKB:Q9HCU8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HCU8}.
CC Note=Partially recruited to DNA damage sites within 2 hours following
CC UV irradiation, before degradation. {ECO:0000250|UniProtKB:Q9HCU8}.
CC -!- PTM: Ubiquitinated; undergoes 'Lys-48'-linked ubiquitination in
CC response to UV irradiation, leading to proteasomal degradation. This
CC modification is partly mediated by RNF8 and by the DCX(DTL) E3
CC ubiquitin ligase complex (also called CRL4(CDT2)). Efficient
CC degradation requires the presence of PCNA and is required for the
CC inhibition of fork progression after DNA damage.
CC {ECO:0000250|UniProtKB:Q9HCU8}.
CC -!- SIMILARITY: Belongs to the DNA polymerase delta subunit 4 family.
CC {ECO:0000255}.
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DR EMBL; BC102212; AAI02213.1; -; mRNA.
DR RefSeq; NP_001069949.1; NM_001076481.2.
DR AlphaFoldDB; Q3T0X9; -.
DR SMR; Q3T0X9; -.
DR IntAct; Q3T0X9; 1.
DR STRING; 9913.ENSBTAP00000023866; -.
DR PaxDb; Q3T0X9; -.
DR PRIDE; Q3T0X9; -.
DR GeneID; 617899; -.
DR KEGG; bta:617899; -.
DR CTD; 57804; -.
DR eggNOG; ENOG502SC9I; Eukaryota.
DR HOGENOM; CLU_132157_0_0_1; -.
DR InParanoid; Q3T0X9; -.
DR OrthoDB; 1544583at2759; -.
DR TreeFam; TF103004; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0043625; C:delta DNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0071897; P:DNA biosynthetic process; IDA:UniProtKB.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR InterPro; IPR007218; DNA_pol_delta_4.
DR PANTHER; PTHR14303; PTHR14303; 1.
DR Pfam; PF04081; DNA_pol_delta_4; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA damage; DNA excision; DNA repair;
KW DNA replication; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..107
FT /note="DNA polymerase delta subunit 4"
FT /id="PRO_0000228673"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..16
FT /note="PCNA-interaction protein motif (PIP box)"
FT /evidence="ECO:0000250|UniProtKB:Q9HCU8"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 107 AA; 12342 MW; 52D9488C4A60B18A CRC64;
MGRKRLITDS YPVVKRREGS AGHSKGELAP DLGEEPLPLS VDEEELELLR QFDLAWQYGP
CTGITRLQRW HRAEQMGLKP PPEVHQVLQS HPGDPRFQCS LWHFYPL
