DPOE3_DROME
ID DPOE3_DROME Reviewed; 128 AA.
AC Q9V444;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=DNA polymerase epsilon subunit 3 {ECO:0000305};
DE AltName: Full=Chromatin accessibility complex 14kD protein {ECO:0000312|FlyBase:FBgn0043002};
DE AltName: Full=Histone-fold protein CHRAC subunit {ECO:0000303|PubMed:24703848};
GN Name=Chrac-14 {ECO:0000303|PubMed:10856248,
GN ECO:0000312|FlyBase:FBgn0043002};
GN Synonyms=CHRAC {ECO:0000312|FlyBase:FBgn0043002},
GN CHRAC14 {ECO:0000303|PubMed:18327268, ECO:0000312|FlyBase:FBgn0043002},
GN DNApolE3 {ECO:0000305}, mary {ECO:0000312|FlyBase:FBgn0043002};
GN ORFNames=CG13399 {ECO:0000312|FlyBase:FBgn0043002};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:CAB70602.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-17; 21-31 AND 40-128,
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE CHRAC COMPLEX,
RP INTERACTION WITH CHRAC-16 AND ISWI, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=10856248; DOI=10.1093/emboj/19.12.3049;
RA Corona D.F., Eberharter A., Budde A., Deuring R., Ferrari S.,
RA Varga-Weisz P., Wilm M., Tamkun J., Becker P.B.;
RT "Two histone fold proteins, CHRAC-14 and CHRAC-16, are developmentally
RT regulated subunits of chromatin accessibility complex (CHRAC).";
RL EMBO J. 19:3049-3059(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAL48592.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL48592.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL48592.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000312|EMBL:ANY27634.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ANY27634.1};
RA Wan K., Booth B., Spirohn K., Hao T., Hu Y., Calderwood M., Hill D.,
RA Mohr S., Vidal M., Celniker S., Perrimon N.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE CHRAC COMPLEX, INTERACTION WITH CHRAC-16,
RP AND SUBCELLULAR LOCATION.
RX PubMed=11447119; DOI=10.1093/emboj/20.14.3781;
RA Eberharter A., Ferrari S., Laengst G., Straub T., Imhof A., Varga-Weisz P.,
RA Wilm M., Becker P.B.;
RT "Acf1, the largest subunit of CHRAC, regulates ISWI-induced nucleosome
RT remodelling.";
RL EMBO J. 20:3781-3788(2001).
RN [7] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, IDENTIFICATION IN
RP THE ATAC COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=18327268; DOI=10.1038/nsmb.1397;
RA Suganuma T., Gutierrez J.L., Li B., Florens L., Swanson S.K.,
RA Washburn M.P., Abmayr S.M., Workman J.L.;
RT "ATAC is a double histone acetyltransferase complex that stimulates
RT nucleosome sliding.";
RL Nat. Struct. Mol. Biol. 15:364-372(2008).
RN [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CID, AND SUBCELLULAR LOCATION.
RX PubMed=24703848; DOI=10.1016/j.celrep.2014.03.008;
RA Mathew V., Pauleau A.L., Steffen N., Bergner A., Becker P.B., Erhardt S.;
RT "The histone-fold protein CHRAC14 influences chromatin composition in
RT response to DNA damage.";
RL Cell Rep. 7:321-330(2014).
RN [9] {ECO:0007744|PDB:2BYK, ECO:0007744|PDB:2BYM}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 7-99 IN COMPLEX WITH CHRAC-16,
RP FUNCTION, INTERACTION WITH ACF, AND MUTAGENESIS OF 2-VAL--LEU-8 AND
RP 109-SER--GLU-128.
RX PubMed=16260604; DOI=10.1128/mcb.25.22.9886-9896.2005;
RA Hartlepp K.F., Fernandez-Tornero C., Eberharter A., Grune T., Muller C.W.,
RA Becker P.B.;
RT "The histone fold subunits of Drosophila CHRAC facilitate nucleosome
RT sliding through dynamic DNA interactions.";
RL Mol. Cell. Biol. 25:9886-9896(2005).
CC -!- FUNCTION: Accessory component of the DNA polymerase epsilon complex (By
CC similarity). Participates in DNA repair and in chromosomal DNA
CC replication (By similarity). Histone-like protein which promotes
CC nucleosome sliding of ATP-dependent nucleosome remodeling complexes
CC (PubMed:10856248, PubMed:11447119, PubMed:18327268). Part of the
CC chromatin-accessibility complex (CHRAC) which uses energy/ATP to
CC increase the general accessibility of DNA in chromatin
CC (PubMed:10856248, PubMed:11447119). As an heterodimer with Chrac-16,
CC binds DNA and facilitates nucleosome sliding by Acf (PubMed:16260604).
CC Has a role in DNA damage response by preventing cid mislocalization to
CC chromatin (PubMed:24703848). {ECO:0000250|UniProtKB:Q04603,
CC ECO:0000250|UniProtKB:Q9NRF9, ECO:0000269|PubMed:10856248,
CC ECO:0000269|PubMed:11447119, ECO:0000269|PubMed:16260604,
CC ECO:0000269|PubMed:18327268, ECO:0000269|PubMed:24703848}.
CC -!- SUBUNIT: Homodimer (PubMed:18327268). Component of the DNA polymerase
CC epsilon complex consisting of four subunits: the catalytic subunit
CC PolE1/DNApol-epsilon255 and the accessory subunits PolE2/DNApol-
CC epsilon58, Chrac-14/DNApolE3 and PolE4 (By similarity). Component of
CC the chromatin accessibility complex (CHRAC), composed of Chrac-14,
CC Chrac-16, Acf and Iswi (PubMed:10856248, PubMed:11447119). Forms an
CC heterodimer with Chrac-16 (PubMed:10856248, PubMed:16260604). The
CC Chrac-14/Chrac-16 heterodimer interacts with Acf (via N-terminus)
CC (PubMed:16260604). Interacts directly with Iswi and this interaction is
CC further stabilized by association with Chrac-16 (PubMed:10856248).
CC Component of the Ada2a-containing (ATAC) complex composed of at least
CC Ada2a, Atac1, Hcf, Ada3, Gcn5, Mocs2B, Charac-14, Atac3, Atac2, NC2beta
CC and wds (PubMed:18327268). Interacts with cid (PubMed:24703848).
CC {ECO:0000250|UniProtKB:Q9NRF9, ECO:0000269|PubMed:10856248,
CC ECO:0000269|PubMed:11447119, ECO:0000269|PubMed:16260604,
CC ECO:0000269|PubMed:18327268, ECO:0000269|PubMed:24703848}.
CC -!- INTERACTION:
CC Q9V444; Q9V452: Chrac-16; NbExp=10; IntAct=EBI-138718, EBI-193917;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10856248,
CC ECO:0000269|PubMed:11447119, ECO:0000269|PubMed:18327268,
CC ECO:0000269|PubMed:24703848}.
CC -!- DEVELOPMENTAL STAGE: Expressed in oocytes and in the early embryo and
CC down-regulated afterwards (at protein level).
CC {ECO:0000269|PubMed:10856248}.
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DR EMBL; AJ271141; CAB70602.1; -; mRNA.
DR EMBL; AE014134; AAO41168.1; -; Genomic_DNA.
DR EMBL; AY070970; AAL48592.1; -; mRNA.
DR EMBL; KX531824; ANY27634.1; -; mRNA.
DR RefSeq; NP_476646.2; NM_057298.4.
DR PDB; 2BYK; X-ray; 2.40 A; B/D=1-128.
DR PDB; 2BYM; X-ray; 2.80 A; B/D=1-128.
DR PDBsum; 2BYK; -.
DR PDBsum; 2BYM; -.
DR AlphaFoldDB; Q9V444; -.
DR SMR; Q9V444; -.
DR IntAct; Q9V444; 22.
DR STRING; 7227.FBpp0099655; -.
DR PaxDb; Q9V444; -.
DR PRIDE; Q9V444; -.
DR EnsemblMetazoa; FBtr0100268; FBpp0099657; FBgn0043002.
DR GeneID; 3772329; -.
DR KEGG; dme:Dmel_CG13399; -.
DR UCSC; CG13399-RA; d. melanogaster.
DR CTD; 3772329; -.
DR FlyBase; FBgn0043002; Chrac-14.
DR VEuPathDB; VectorBase:FBgn0043002; -.
DR eggNOG; KOG0870; Eukaryota.
DR HOGENOM; CLU_066247_7_4_1; -.
DR InParanoid; Q9V444; -.
DR OMA; KQNHRTI; -.
DR OrthoDB; 1572458at2759; -.
DR PhylomeDB; Q9V444; -.
DR Reactome; R-DME-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-DME-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-DME-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-DME-5696400; Dual Incision in GG-NER.
DR Reactome; R-DME-6782135; Dual incision in TC-NER.
DR Reactome; R-DME-68952; DNA replication initiation.
DR Reactome; R-DME-68962; Activation of the pre-replicative complex.
DR SignaLink; Q9V444; -.
DR BioGRID-ORCS; 3772329; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; Q9V444; -.
DR GenomeRNAi; 3772329; -.
DR PRO; PR:Q9V444; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0043002; Expressed in egg cell and 45 other tissues.
DR GO; GO:0140672; C:ATAC complex; IDA:FlyBase.
DR GO; GO:0008623; C:CHRAC; IDA:FlyBase.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; ISS:FlyBase.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:FlyBase.
DR GO; GO:0071480; P:cellular response to gamma radiation; IMP:FlyBase.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IMP:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR GO; GO:0006261; P:DNA-templated DNA replication; ISS:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IDA:FlyBase.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
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; Direct protein sequencing; Nucleus; Reference proteome.
FT CHAIN 1..128
FT /note="DNA polymerase epsilon subunit 3"
FT /id="PRO_0000448437"
FT REGION 98..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 2..18
FT /note="Missing: When in a heterodimer with Chrac-16,
FT reduces Acf binding but does not affect DNA binding or Acf
FT nucleosome sliding activity."
FT /evidence="ECO:0000269|PubMed:16260604"
FT MUTAGEN 109..128
FT /note="Missing: When in a heterodimer with Chrac-16,
FT reduces DNA binding and is less able to stimulate Acf
FT nucleosome sliding activity."
FT /evidence="ECO:0000269|PubMed:16260604"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:2BYK"
FT HELIX 31..58
FT /evidence="ECO:0007829|PDB:2BYK"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:2BYK"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2BYK"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:2BYK"
SQ SEQUENCE 128 AA; 13844 MW; 153E58AF2296F847 CRC64;
MVERIEDLNL PNAVIGRLIK EALPESASVS KEARAAIARA ASVFAIFVTS SSTALAHKQN
HKTITAKDIL QTLTELDFES FVPSLTQDLE VYRKVVKEKK ESKASKKDSN TAENANASAT
ATAEEAPE
