DPOD3_BOVIN
ID DPOD3_BOVIN Reviewed; 466 AA.
AC P84798;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=DNA polymerase delta subunit 3;
DE AltName: Full=DNA polymerase delta subunit p66;
DE AltName: Full=p68;
GN Name=POLD3;
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 GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 25-47; 77-89; 110-123; 132-143 AND 190-198,
RP IDENTIFICATION IN POL-DELTA COMPLEX, AND MASS SPECTROMETRY.
RC TISSUE=Thymus {ECO:0000269|PubMed:10751307};
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: Accessory component of both the DNA polymerase delta complex
CC and the DNA polymerase zeta complex. As a component of the trimeric and
CC tetrameric DNA polymerase delta complexes (Pol-delta3 and Pol-delta4,
CC respectively), plays a role in high fidelity genome replication,
CC including in lagging strand synthesis, and repair. Required for optimal
CC Pol-delta activity. Stabilizes the Pol-delta complex and plays a major
CC role in Pol-delta stimulation by PCNA. Pol-delta3 and Pol-delta4 are
CC characterized by the absence or the presence of POLD4. They exhibit
CC differences in catalytic activity. Most notably, Pol-delta3 shows
CC higher proofreading activity than Pol-delta4. Although both Pol-delta3
CC and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may also
CC be better suited to fulfill this task, exhibiting near-absence of
CC strand displacement activity compared to Pol-delta4 and stalling on
CC encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling
CC process may avoid the formation of a gap, while maintaining a nick that
CC can be readily ligated. Along with DNA polymerase kappa, DNA polymerase
CC delta carries out approximately half of nucleotide excision repair
CC (NER) synthesis following UV irradiation. In this context, POLD3, along
CC with PCNA and RFC1-replication factor C complex, is required to recruit
CC POLD1, the catalytic subunit of the polymerase delta complex, to DNA
CC damage sites. Under conditions of DNA replication stress, required for
CC the repair of broken replication forks through break-induced
CC replication (BIR). Involved in the translesion synthesis (TLS) of
CC templates carrying O6-methylguanine or abasic sites performed by Pol-
CC delta4, independently of DNA polymerase zeta (REV3L) or eta (POLH).
CC Facilitates abasic site bypass by DNA polymerase delta by promoting
CC extension from the nucleotide inserted opposite the lesion. Also
CC involved in TLS, as a component of the tetrametric DNA polymerase zeta
CC complex. Along with POLD2, dramatically increases the efficiency and
CC processivity of DNA synthesis of the DNA polymerase zeta complex
CC compared to the minimal zeta complex, consisting of only REV3L and
CC REV7. {ECO:0000250|UniProtKB:Q15054}.
CC -!- SUBUNIT: Component of both the DNA polymerase delta and DNA polymerase
CC zeta complexes. 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 POLD2. Following stress caused by DNA damaging agents or by replication
CC stress, POLD4 is degraded and Pol-delta4 is converted into a trimeric
CC form of the complex (Pol-delta3), which consists of POLD1, POLD2 and
CC POLD3. Pol-delta3 is the major form occurring at S phase replication
CC sites, as well as DNA damage sites. Directly interacts with PCNA, as do
CC POLD1 and POLD4; this interaction stimulates Pol-delta polymerase
CC activity. Component of the DNA polymerase zeta complex (POLZ), which
CC consists of REV3L, MAD2L2, POLD2 and POLD3, with REV3L bearing DNA
CC polymerase catalytic activity. The DNA polymerase delta complex
CC interacts with POLDIP2; this interaction is probably mediated through
CC direct binding to POLD2. {ECO:0000250|UniProtKB:Q15054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9EQ28}. Nucleus
CC {ECO:0000250|UniProtKB:Q9EQ28}. Note=Partially colocalizes with PCNA
CC and POLD1 at S phase replication sites. Recruited to DNA damage sites
CC within 2 hours following UV irradiation.
CC {ECO:0000250|UniProtKB:Q15054}.
CC -!- DOMAIN: The PIP-box mediates the interaction with PCNA.
CC {ECO:0000250|UniProtKB:Q15054}.
CC -!- PTM: Ubiquitinated, but not targeted to the proteasome. Sumoylated.
CC Sumoylation by SUMO3 may be predominant.
CC {ECO:0000250|UniProtKB:Q15054}.
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DR AlphaFoldDB; P84798; -.
DR SMR; P84798; -.
DR IntAct; P84798; 1.
DR STRING; 9913.ENSBTAP00000042403; -.
DR PaxDb; P84798; -.
DR PRIDE; P84798; -.
DR Ensembl; ENSBTAT00000044966; ENSBTAP00000042403; ENSBTAG00000016869.
DR VEuPathDB; HostDB:ENSBTAG00000016869; -.
DR VGNC; VGNC:33115; POLD3.
DR eggNOG; ENOG502QPSW; Eukaryota.
DR GeneTree; ENSGT01050000245211; -.
DR InParanoid; P84798; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000016869; Expressed in spermatid and 105 other tissues.
DR ExpressionAtlas; P84798; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043625; C:delta DNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0071897; P:DNA biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
DR GO; GO:1904161; P:DNA synthesis involved in UV-damage excision repair; IBA:GO_Central.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR Gene3D; 3.90.1030.20; -; 1.
DR InterPro; IPR019038; POLD3.
DR InterPro; IPR041913; POLD3_sf.
DR PANTHER; PTHR17598; PTHR17598; 1.
DR Pfam; PF09507; CDC27; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; DNA damage;
KW DNA excision; DNA repair; DNA replication; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15054"
FT CHAIN 2..466
FT /note="DNA polymerase delta subunit 3"
FT /id="PRO_0000228672"
FT REGION 145..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 456..463
FT /note="PIP-box"
FT /evidence="ECO:0000250|UniProtKB:Q15054"
FT COMPBIAS 149..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..368
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15054"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15054"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15054"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15054"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15054"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15054"
FT CROSSLNK 259
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15054"
FT CROSSLNK 259
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15054"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15054"
FT CROSSLNK 433
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15054"
FT CROSSLNK 433
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15054"
SQ SEQUENCE 466 AA; 52074 MW; C8DBEE242B4F430A CRC64;
MADQFYLENI DEFVTDQNKI VTYKWLSYTL GVHVNQAKQM LYDYVERKRK ENSGAQLHVT
YLVSGSLIQN GHSCHKVAVV REDKLEAVKS KLAVTASVHV YSIQKAMLKD SGPLFNTDYD
ILKSNLQNCS KFSAIQCAAA VPRAPAESSS SEKLEQSDPP VSPEMQASDE LTTNGHGPPV
PKQSSQQPKG IMGMFASKAA SKAQDANKET KTEAKEVMNS EKNNENLLLS GYWESMIVLF
QAQCINKLKV NLDSEQEVKE EKKVEQPPLS VTEPKLAAPV DLKKSSKKAE PVRMQQKEKK
RRKQMELSDD ETKETENMKK KRRRIKLPES DSSEDEVIPD SPGAYEAESP SPPPPSPSPE
PVLKTEPEPP PVKGSDGENK RKRKRVLKSK TFTDEEGCMV TEKVYESESC TDSEEELKMK
TSSVHRPPAM AVKKEPKEER KGPKKGTAAM GKANRQVAIT GFFQRK
