DPOD2_XENLA
ID DPOD2_XENLA Reviewed; 463 AA.
AC O93610; Q5D0A2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=DNA polymerase delta subunit 2;
DE AltName: Full=XlCdc1;
GN Name=pold2; Synonyms=cdc1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10196469; DOI=10.1016/s0378-1119(99)00058-x;
RA Reynolds N., MacNeill S.A.;
RT "Characterisation of XlCdc1, a Xenopus homologue of the small (PolD2)
RT subunit of DNA polymerase delta; identification of ten conserved regions I-
RT X based on protein sequence comparisons across ten eukaryotic species.";
RL Gene 230:15-22(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: As a component of the trimeric and tetrameric DNA polymerase
CC delta complexes (Pol-delta3 and Pol-delta4, respectively), plays a role
CC in high fidelity genome replication, including in lagging strand
CC synthesis, and repair. Pol-delta3 and Pol-delta4 are characterized by
CC the absence or the presence of POLD4. They exhibit differences in
CC catalytic activity. Most notably, Pol-delta3 shows higher proofreading
CC activity than Pol-delta4. Although both Pol-delta3 and Pol-delta4
CC process Okazaki fragments in vitro, Pol-delta3 may also be better
CC suited to fulfill this task, exhibiting near-absence of strand
CC displacement activity compared to Pol-delta4 and stalling on encounter
CC with the 5'-blocking oligonucleotides. Pol-delta3 idling process may
CC avoid the formation of a gap, while maintaining a nick that can be
CC readily ligated. Along with DNA polymerase kappa, DNA polymerase delta
CC carries out approximately half of nucleotide excision repair (NER)
CC synthesis following UV irradiation. Under conditions of DNA replication
CC stress, required for the repair of broken replication forks through
CC break-induced replication (BIR). Involved in the translesion synthesis
CC (TLS) of templates carrying O6-methylguanine or abasic sites performed
CC by Pol-delta4, independently of DNA polymerase zeta (REV3L) or eta
CC (POLH). Facilitates abasic site bypass by DNA polymerase delta by
CC promoting extension from the nucleotide inserted opposite the lesion.
CC Also involved in TLS as a component of the POLZ complex. Along with
CC POLD3, dramatically increases the efficiency and processivity of DNA
CC synthesis of the minimal DNA polymerase zeta complex, consisting of
CC only REV3L and REV7. {ECO:0000250|UniProtKB:P49005}.
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. Following stress caused by DNA damaging agents
CC or by replication stress, POLD4 is degraded and Pol-delta4 is converted
CC into a trimeric form of the complex (Pol-delta3), which consists of
CC POLD1, POLD2 and POLD3. Pol-delta3 is the major form occurring at S
CC phase replication sites, as well as DNA damage sites. Also observed as
CC a dimeric complex with POLD2 (Pol-delta2 complex). Component of the DNA
CC polymerase zeta complex (POLZ), which consists of REV3L, MAD2L2, POLD2
CC and POLD3, with REV3L bearing DNA polymerase catalytic activity.
CC {ECO:0000250|UniProtKB:P49005}.
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; AJ010836; CAA09373.1; -; mRNA.
DR EMBL; BC047262; AAH47262.1; -; mRNA.
DR RefSeq; NP_001080101.1; NM_001086632.1.
DR AlphaFoldDB; O93610; -.
DR SMR; O93610; -.
DR BioGRID; 98035; 1.
DR IntAct; O93610; 2.
DR MaxQB; O93610; -.
DR DNASU; 379793; -.
DR GeneID; 379793; -.
DR KEGG; xla:379793; -.
DR CTD; 379793; -.
DR Xenbase; XB-GENE-999393; pold2.L.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 379793; Expressed in oocyte and 19 other tissues.
DR GO; GO:0043625; C:delta DNA polymerase complex; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW DNA damage; DNA excision; DNA repair; DNA replication; Nucleus;
KW Reference proteome.
FT CHAIN 1..463
FT /note="DNA polymerase delta subunit 2"
FT /id="PRO_0000096168"
SQ SEQUENCE 463 AA; 50648 MW; 77026EF1897A638D CRC64;
MFTDLAISGG PGLLTAPSEV QSTFTRVSNT QYSNCSSIFR LGERTFTRQY AHIYATRLEQ
MRPLLIKSAK QRWGDDIAVR KLCELQGGEK CCVIGTLFKS MELQPSILRE ISEEHNLLPQ
PARQKYISDS DELILEDELQ RIKLEGATDV QQLVTGAVLA VLGAEEDAGK FVVEDFCLTS
LPVQSPLPRL SEDRFVLLTS GLGLGGGSGD SLMGLQLLLD LVTGQAGAEE DQGCAARISR
VILAGNLLSE NTQGKDSLNK AKYLSKKTQA ASVEAVKMLD EILLQMSGSV SVDVMPGAFD
PTNYILPQQP LHRCMFPQSA LYSTLQLVTN PYEAEIDGVR FLGTSGQNIG DIYKYSSMQD
YLDILEWTLQ VGHLCPTAPD TLGCYPFYKS DPFILQNCPH VYFCGSAPKF SCKEVTGAEG
QRVLLLTVPE FCSTQTACLV NLRTLQCQPI SFSGFGADDE LGD
