DPB3_SCHPO
ID DPB3_SCHPO Reviewed; 87 AA.
AC C6Y4D0;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=DNA polymerase epsilon subunit C {ECO:0000303|PubMed:29109278};
DE AltName: Full=DNA polymerase II subunit C {ECO:0000303|PubMed:29109278};
GN Name=dpb3 {ECO:0000303|PubMed:29109278};
GN Synonyms=daf1 {ECO:0000303|PubMed:29109278}; ORFNames=SPCC16C4.22;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0007744|PDB:5Y26, ECO:0007744|PDB:5Y27}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH DPB4, INTERACTION
RP WITH DPB4 AND CDC20, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=29109278; DOI=10.1073/pnas.1712961114;
RA He H., Li Y., Dong Q., Chang A.Y., Gao F., Chi Z., Su M., Zhang F., Ban H.,
RA Martienssen R., Chen Y.H., Li F.;
RT "Coordinated regulation of heterochromatin inheritance by Dpb3-Dpb4
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:12524-12529(2017).
CC -!- FUNCTION: As accessory component of the DNA polymerase epsilon (DNA
CC polymerase II) participates in chromosomal DNA replication. It is
CC required during synthesis of the leading and lagging DNA strands at the
CC replication fork and binds at/or near replication origins and moves
CC along DNA with the replication fork. It has 3'-5' proofreading
CC exonuclease activity that correct errors arising during DNA
CC replication. It is also involved in DNA synthesis during DNA repair (By
CC similarity). The dpb3-dpb4 dimer associates with histone deacetylases,
CC chromatin remodelers, and histones and plays a crucial role in the
CC inheritance of histone hypoacetylation and H3K9 methylation in
CC heterochromatin (PubMed:29109278). The dpb3-dpb4 dimer is also required
CC for the recruitment of sir2 to heterochromatin (PubMed:29109278).
CC {ECO:0000250|UniProtKB:P27344, ECO:0000269|PubMed:29109278}.
CC -!- SUBUNIT: DNA polymerase epsilon is a heterotetramer consisting of
CC cdc20/Pol2, dpb2, dpb3, and dpb4 (By similarity). Forms also a
CC heterodimer consisting dpb3 and dpb4 (PubMed:29109278). Interacts
CC directly with cdc20/pol2 and dpb4 (PubMed:29109278).
CC {ECO:0000250|UniProtKB:P27344, ECO:0000269|PubMed:29109278}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27344}.
CC -!- DISRUPTION PHENOTYPE: Displays partial loss of silencing in otr region
CC as well as significant loss of silencing in mating-type and telomere
CC (PubMed:29109278). Decreases H3K9 methylation more than 50%, whereas
CC histone acetylation at the pericentromeric region is significantly
CC increased (PubMed:29109278). Results in partial dissociation of swi6
CC from heterochromatin (PubMed:29109278). {ECO:0000269|PubMed:29109278}.
CC -!- CAUTION: SPAC17G8.03c was previously identified as the homolog of
CC budding yeast DBP3 in fission yeast. However, it was further
CC demonstrated that SPCC16C4.22 is the true ortholog of DBP3.
CC {ECO:0000269|PubMed:29109278}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329672; CBA11517.1; -; Genomic_DNA.
DR RefSeq; XP_002788949.1; XM_002788903.2.
DR PDB; 5Y26; X-ray; 2.00 A; B=1-87.
DR PDB; 5Y27; X-ray; 1.90 A; B=1-87.
DR PDBsum; 5Y26; -.
DR PDBsum; 5Y27; -.
DR AlphaFoldDB; C6Y4D0; -.
DR SMR; C6Y4D0; -.
DR BioGRID; 1028329; 5.
DR STRING; 4896.SPCC16C4.22.1; -.
DR MaxQB; C6Y4D0; -.
DR PaxDb; C6Y4D0; -.
DR EnsemblFungi; SPCC16C4.22.1; SPCC16C4.22.1:pep; SPCC16C4.22.
DR PomBase; SPCC16C4.22; dpb3.
DR VEuPathDB; FungiDB:SPCC16C4.22; -.
DR eggNOG; KOG1658; Eukaryota.
DR HOGENOM; CLU_045277_12_1_1; -.
DR InParanoid; C6Y4D0; -.
DR OMA; LATEMFL; -.
DR Reactome; R-SPO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SPO-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-SPO-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-SPO-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SPO-68952; DNA replication initiation.
DR Reactome; R-SPO-68962; Activation of the pre-replicative complex.
DR PRO; PR:C6Y4D0; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IPI:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; IC:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0140529; P:CMG complex assembly; IC:PomBase.
DR GO; GO:1902983; P:DNA strand elongation involved in mitotic DNA replication; IC:PomBase.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:PomBase.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IC:PomBase.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..87
FT /note="DNA polymerase epsilon subunit C"
FT /id="PRO_0000389112"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:5Y27"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:5Y27"
FT HELIX 30..57
FT /evidence="ECO:0007829|PDB:5Y27"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:5Y27"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:5Y27"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:5Y27"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:5Y27"
SQ SEQUENCE 87 AA; 10113 MW; 282CC03EA63EB434 CRC64;
MEKTYGKTVL PLSRVKRIIK QDEDVHYCSN ASALLISVAT ELFVEKLATE AYQLAKLQKR
KGIRYRDVED VVRKDDQFEF LSDLFSI
