DPOD2_RAT
ID DPOD2_RAT Reviewed; 469 AA.
AC Q6AXY4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=DNA polymerase delta subunit 2;
DE AltName: Full=DNA polymerase delta subunit p50;
GN Name=Pold2;
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=Testis;
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 INTERACTION WITH KCTD10.
RC STRAIN=Wistar;
RX PubMed=15982757; DOI=10.1016/j.bbaexp.2005.05.005;
RA Zhou J., Ren K., Liu X., Xiong X., Hu X., Zhang J.;
RT "A novel PDIP1-related protein, KCTD10, that interacts with proliferating
RT cell nuclear antigen and DNA polymerase delta.";
RL Biochim. Biophys. Acta 1729:200-203(2005).
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. Pol-delta3 and Pol-
CC delta4 are characterized by the absence or the presence of POLD4. They
CC exhibit differences in catalytic activity. Most notably, Pol-delta3
CC shows higher proofreading activity than Pol-delta4. Although both Pol-
CC delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3
CC may also be better suited to fulfill this task, exhibiting near-absence
CC of 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. Under conditions of DNA
CC replication stress, required for the repair of broken replication forks
CC through break-induced replication (BIR). Involved in the translesion
CC synthesis (TLS) of templates carrying O6-methylguanine or abasic sites
CC performed by Pol-delta4, independently of DNA polymerase zeta (REV3L)
CC or eta (POLH). Facilitates abasic site bypass by DNA polymerase delta
CC by promoting extension from the nucleotide inserted opposite the
CC lesion. Also involved in TLS as a component of the DNA polymerase zeta
CC complex. Along with POLD3, 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:P49005}.
CC -!- SUBUNIT: Component of both the DNA polymerase delta and DNA polymerase
CC zeta complexes. Component of the tetrameric DNA polymerase delta
CC complex (Pol-delta4), which consists of POLD1/p125, POLD2/p50,
CC POLD3/p66/p68 and POLD4/p12, with POLD1 bearing DNA polymerase and 3'
CC to 5' proofreading exonuclease activities. Within Pol-delta4, directly
CC interacts with POLD1, POLD3 and POLD4. Following stress caused by DNA
CC damaging agents or by replication stress, POLD4 is degraded and Pol-
CC delta4 is converted into a trimeric form of the complex (Pol-delta3),
CC which consists of POLD1, POLD2 and POLD3. Pol-delta3 is the major form
CC occurring at S phase replication sites, as well as DNA damage sites.
CC Also observed as a dimeric complex with POLD2 (Pol-delta2 complex).
CC Pol-delta2 is relatively insensitive to the PCNA stimulation (2-5-fold)
CC compared to Pol-delta4 that is stimulated by over 50-fold. Contrary to
CC the other components of Pol-delta4, does not directly interact with
CC PCNA. As POLD1 and POLD4, directly interacts with WRNIP1; this
CC interaction stimulates DNA polymerase delta-mediated DNA synthesis,
CC independently of the presence of PCNA. This stimulation may be due
CC predominantly to an increase of initiation frequency and also to
CC increased processivity. Directly interacts with POLDIP2 and POLDIP3.
CC Directly interacts with KCTD13/PDIP1; in the presence of PCNA, this
CC interaction may stimulate DNA polymerase activity. Component of the
CC tetrameric Pol-zeta complex (Pol-zeta4), which consists of REV3L,
CC MAD2L2, POLD2 and POLD3, with REV3L bearing DNA polymerase catalytic
CC activity (By similarity). Interacts with KCTD10 (PubMed:15982757).
CC {ECO:0000250|UniProtKB:P49005, ECO:0000269|PubMed:15982757}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49005}.
CC Note=Recruited to DNA damage sites within 2 hours following UV
CC irradiation. {ECO:0000250|UniProtKB:P49005}.
CC -!- SIMILARITY: Belongs to the DNA polymerase delta/II small subunit
CC family. {ECO:0000305}.
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DR EMBL; BC079267; AAH79267.1; -; mRNA.
DR RefSeq; NP_001013068.1; NM_001013050.1.
DR AlphaFoldDB; Q6AXY4; -.
DR SMR; Q6AXY4; -.
DR BioGRID; 253015; 1.
DR ComplexPortal; CPX-2099; DNA polymerase delta complex.
DR STRING; 10116.ENSRNOP00000019288; -.
DR SwissPalm; Q6AXY4; -.
DR PaxDb; Q6AXY4; -.
DR PRIDE; Q6AXY4; -.
DR GeneID; 289758; -.
DR KEGG; rno:289758; -.
DR UCSC; RGD:1304954; rat.
DR CTD; 5425; -.
DR RGD; 1304954; Pold2.
DR VEuPathDB; HostDB:ENSRNOG00000014098; -.
DR eggNOG; KOG2732; Eukaryota.
DR InParanoid; Q6AXY4; -.
DR OMA; DPANFML; -.
DR OrthoDB; 736068at2759; -.
DR PhylomeDB; Q6AXY4; -.
DR TreeFam; TF101073; -.
DR Reactome; R-RNO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-RNO-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-RNO-174414; Processive synthesis on the C-strand of the telomere.
DR Reactome; R-RNO-174417; Telomere C-strand (Lagging Strand) Synthesis.
DR Reactome; R-RNO-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-RNO-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-RNO-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
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-69091; Polymerase switching.
DR Reactome; R-RNO-69166; Removal of the Flap Intermediate.
DR Reactome; R-RNO-69183; Processive synthesis on the lagging strand.
DR PRO; PR:Q6AXY4; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000014098; Expressed in testis and 20 other tissues.
DR Genevisible; Q6AXY4; RN.
DR GO; GO:0043625; C:delta DNA polymerase complex; IDA:RGD.
DR GO; GO:0042575; C:DNA polymerase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0016035; C:zeta DNA polymerase complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0071897; P:DNA biosynthetic process; ISO:RGD.
DR GO; GO:0006260; P:DNA replication; IDA:RGD.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IMP:RGD.
DR GO; GO:0042276; P:error-prone translesion synthesis; ISO:RGD.
DR CDD; cd07387; MPP_PolD2_C; 1.
DR InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR InterPro; IPR040663; DNA_pol_D_N.
DR InterPro; IPR024826; DNA_pol_delta/II_ssu.
DR InterPro; IPR041863; PolD2_C.
DR PANTHER; PTHR10416; PTHR10416; 1.
DR Pfam; PF18018; DNA_pol_D_N; 1.
DR Pfam; PF04042; DNA_pol_E_B; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA damage; DNA excision; DNA repair; DNA replication;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..469
FT /note="DNA polymerase delta subunit 2"
FT /id="PRO_0000248589"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P49005"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49005"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49005"
SQ SEQUENCE 469 AA; 51346 MW; E6619AD76045911A CRC64;
MFSEQAAQRA HTLLSPPSAS NATFARVPVA TYTNSSQPFR LGERSFNRQY AHIYATRLIQ
MRPFLVSRAQ QHWGSQVEVK KLCELQPGEQ CCVVGTLFKA MPLQPSILRE ISEEHNLIPQ
PPRSKYIHPD DELVLEDELQ RIKLKGTIDV SKLVTGTVLA VFGSVKDDGK FQVEDHCFAD
LAPQNPVPPL DTDRFVLLVS GLGLGGGGGE SLLGTQLLVD VVTGQLGDEG EQCSAAHVSR
VILAGNLLSH NTQSRDSINK AKYLTKKTQA ASVEAVKMLD EILLQLSASV PVDVMPGEFD
PTNYTLPQQP LHPCMFPLAT AYATLQLVTN PYQATIDGVR FLGTSGQNVS DIFRYSSMED
HLEILEWTLR VRHISPTAPD TLGCYPFYKT DPFIFAECPH VYFCGNTPSF GSKVIRGPED
QAVLLVAVPD FSSTQTACLV NLRGLTCQPI SFAGFGAEQD DLEDLGLGP
