DPOD2_BOVIN
ID DPOD2_BOVIN Reviewed; 469 AA.
AC P49004; Q29RZ3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=DNA polymerase delta subunit 2;
DE AltName: Full=DNA polymerase delta subunit p50;
GN Name=POLD2;
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 [MRNA], PROTEIN SEQUENCE OF 5-40; 49-57; 62-80;
RP 102-132; 146-162; 316-330; 341-354; 359-366 AND 444-459, AND BLOCKED
RP N-TERMINUS.
RC TISSUE=Thymus;
RX PubMed=8530069; DOI=10.1006/geno.1995.1229;
RA Zhang J., Tan C.-K., McMullen B., Downey K.M., So A.G.;
RT "Cloning of the cDNAs for the small subunits of bovine and human DNA
RT polymerase delta and chromosomal location of the human gene (POLD2).";
RL Genomics 29:179-186(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 100-109; 268-277 AND 341-354, IDENTIFICATION IN
RP POL-DELTA COMPLEX, AND MASS 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: 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 (By similarity).
CC {ECO:0000250|UniProtKB:P49005, ECO:0000250|UniProtKB:Q6AXY4}.
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 -!- PTM: The N-terminus is blocked most probably through acetylation, as
CC has been shown for the human ortholog. {ECO:0000305|PubMed:8530069}.
CC -!- SIMILARITY: Belongs to the DNA polymerase delta/II small subunit
CC family. {ECO:0000305}.
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DR EMBL; U21091; AAC48475.1; -; mRNA.
DR EMBL; BC113315; AAI13316.1; -; mRNA.
DR PIR; I46076; I46076.
DR RefSeq; NP_776853.2; NM_174428.3.
DR RefSeq; XP_015325451.1; XM_015469965.1.
DR RefSeq; XP_015325452.1; XM_015469966.1.
DR AlphaFoldDB; P49004; -.
DR SMR; P49004; -.
DR CORUM; P49004; -.
DR IntAct; P49004; 1.
DR STRING; 9913.ENSBTAP00000016237; -.
DR PaxDb; P49004; -.
DR PRIDE; P49004; -.
DR Ensembl; ENSBTAT00000016237; ENSBTAP00000016237; ENSBTAG00000012241.
DR GeneID; 281991; -.
DR KEGG; bta:281991; -.
DR CTD; 5425; -.
DR VEuPathDB; HostDB:ENSBTAG00000012241; -.
DR VGNC; VGNC:33114; POLD2.
DR eggNOG; KOG2732; Eukaryota.
DR GeneTree; ENSGT00390000006780; -.
DR HOGENOM; CLU_021763_0_0_1; -.
DR InParanoid; P49004; -.
DR OrthoDB; 736068at2759; -.
DR TreeFam; TF101073; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000012241; Expressed in laryngeal cartilage and 106 other tissues.
DR ExpressionAtlas; P49004; baseline and differential.
DR GO; GO:0043625; C:delta DNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0042575; C:DNA polymerase complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0071897; P:DNA biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
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; Direct protein sequencing; DNA damage; DNA excision;
KW DNA repair; DNA replication; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..469
FT /note="DNA polymerase delta subunit 2"
FT /id="PRO_0000096165"
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"
FT CONFLICT 45
FT /note="S -> T (in Ref. 1; AAC48475)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="L -> F (in Ref. 1; AAC48475)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="F -> S (in Ref. 1; AAC48475)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="R -> G (in Ref. 1; AAC48475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 50997 MW; BABBD7F6C133F96E CRC64;
MFSEQAAQRA HTLLSPPSAS NATFARVPVV TYTNSSQPFR LGERSFSRQY AHIYATRLIQ
MRPFLVSRAQ QRWGSGVLVK KLCELQPGEK CCVVGTLFKA MPLQPSILRE VSEEHNLLPQ
PPRSKYIHPD DELILEDELQ RIKLEGTIDV SKLVTGTVLA VLGSAGDDGK FLVEDHCFAG
LAPQKPACPL DTDRFVLLVS GLGLGGGGGE SLLGTQLLVD VVTGQLGDEG EQCSAAHVSR
VILAGNLLSH NTQSRDSINK AKYLTKKTQA ASVEAVKMLD EILLQLSASV PVDVMPGEFD
PTNYTLPQQP LHPCMFPLAT AYSTLQLVTN PYQATIDGVR FLGTSGQNVS DIFRYSSMED
HLEILEWTLQ VRHISPTAPD TLGCYPFYKT DPFIFPECPH VYFCGNTPSF GSKIIQGPED
QTVLLVAVPD FSTTQTACLV NLRSLACQPI SFSGFGAEDE DLGGLGLGP
