DPOE1_ARATH
ID DPOE1_ARATH Reviewed; 2161 AA.
AC F4HW04; B3H4I0; Q9SGD5;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=DNA polymerase epsilon catalytic subunit A;
DE EC=2.7.7.7 {ECO:0000250|UniProtKB:P15436};
DE AltName: Full=DNA polymerase 2 a;
DE Short=AtPOL2a;
DE AltName: Full=DNA polymerase II subunit a;
DE AltName: Full=Protein ABA OVERLY SENSITIVE a;
DE AltName: Full=Protein EARLY IN SHORT DAYS 7;
DE AltName: Full=Protein EMBRYO DEFECTIVE 142;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2284;
DE AltName: Full=Protein EMBRYO DEFECTIVE 529;
DE AltName: Full=Protein TILTED 1;
GN Name=POL2A; Synonyms=ABO4, EMB142, EMB2284, EMB529, ESD7, TIL1;
GN OrderedLocusNames=At1g08260; ORFNames=T23G18.21;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-469, AND TISSUE
RP SPECIFICITY.
RX PubMed=16278345; DOI=10.1105/tpc.105.036889;
RA Jenik P.D., Jurkuta R.E.J., Barton M.K.;
RT "Interactions between the cell cycle and embryonic patterning in
RT Arabidopsis uncovered by a mutation in DNA polymerase epsilon.";
RL Plant Cell 17:3362-3377(2005).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY CELL CYCLE, INTERACTION WITH
RP DPB2, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16212602; DOI=10.1111/j.1365-313x.2005.02521.x;
RA Ronceret A., Guilleminot J., Lincker F., Gadea-Vacas J., Delorme V.,
RA Bechtold N., Pelletier G., Delseny M., Chaboute M.-E., Devic M.;
RT "Genetic analysis of two Arabidopsis DNA polymerase epsilon subunits during
RT early embryogenesis.";
RL Plant J. 44:223-236(2005).
RN [5]
RP FUNCTION.
RC STRAIN=cv. Columbia GL1;
RX PubMed=19244142; DOI=10.1105/tpc.108.061549;
RA Yin H., Zhang X., Liu J., Wang Y., He J., Yang T., Hong X., Yang Q.,
RA Gong Z.;
RT "Epigenetic regulation, somatic homologous recombination, and abscisic acid
RT signaling are influenced by DNA polymerase epsilon mutation in
RT Arabidopsis.";
RL Plant Cell 21:386-402(2009).
RN [6]
RP FUNCTION, MUTAGENESIS OF GLY-992, DISRUPTION PHENOTYPE, INTERACTION WITH
RP LHP1/TFL2, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19947980; DOI=10.1111/j.1365-313x.2009.04093.x;
RA del Olmo I., Lopez-Gonzalez L., Martin-Trillo M.M., Martinez-Zapater J.M.,
RA Pineiro M., Jarillo J.A.;
RT "EARLY IN SHORT DAYS 7 (ESD7) encodes the catalytic subunit of DNA
RT polymerase epsilon and is required for flowering repression through a
RT mechanism involving epigenetic gene silencing.";
RL Plant J. 61:623-636(2010).
CC -!- FUNCTION: DNA polymerase II, which participates in chromosomal DNA
CC replication. Required for the timing and determination of cell fate
CC during plant embryogenesis and root pole development, by promoting cell
CC cycle and cell type patterning. Necessary for proper shoot (SAM) and
CC root apical meristem (RAM) functions. Involved in maintaining
CC epigenetic states, controlling hypersensitive response (HR), and
CC mediating abscisic acid (ABA) signaling. Required for flowering
CC repression through a mechanism involving epigenetic gene silencing. May
CC participate in processes involved in chromatin-mediated cellular
CC memory. {ECO:0000269|PubMed:16212602, ECO:0000269|PubMed:16278345,
CC ECO:0000269|PubMed:19244142, ECO:0000269|PubMed:19947980}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000250|UniProtKB:P15436};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P15436};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P15436};
CC -!- SUBUNIT: Heterotetramer (By similarity). Subunit of the DNA polymerase
CC II (PubMed:16212602, PubMed:19947980). Interacts (via C-terminus) with
CC DPB2 (PubMed:16212602). Interacts with LHP1/TFL2 (PubMed:19947980).
CC {ECO:0000250, ECO:0000269|PubMed:16212602,
CC ECO:0000269|PubMed:19947980}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed at low levels in inflorescence
CC (floral meristem and flowers until anthesis), and, to a lower extent,
CC in roots, seeds and leaves. {ECO:0000269|PubMed:16278345,
CC ECO:0000269|PubMed:19947980}.
CC -!- DEVELOPMENTAL STAGE: Present in actively dividing cells such as root
CC and shoot meristematic regions, young leaves and stems, inflorescences
CC and siliques. {ECO:0000269|PubMed:19947980}.
CC -!- INDUCTION: Follows a cell-cycle-dependent expression with a maximal
CC induction in the S phase and another induction at the G2/M transition.
CC {ECO:0000269|PubMed:16212602}.
CC -!- DOMAIN: The DNA polymerase activity domain resides in the N-terminal
CC half of the protein, while the C-terminus is necessary for maintenance
CC of the complex. {ECO:0000250|UniProtKB:P21951}.
CC -!- DOMAIN: The CysA-type zinc finger is required for PCNA-binding.
CC {ECO:0000250|UniProtKB:P15436}.
CC -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC formation of polymerase complexes. {ECO:0000250|UniProtKB:P15436}.
CC -!- DISRUPTION PHENOTYPE: Lethal, with sporophytic embryo-defective with an
CC arrest at the globular stage during embryo development. Abnormal cell
CC division characterized by several rounds of mitosis with aberrant
CC planes of division. {ECO:0000269|PubMed:16212602,
CC ECO:0000269|PubMed:16278345, ECO:0000269|PubMed:19947980}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF18240.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011438; AAF18240.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28266.1; -; Genomic_DNA.
DR RefSeq; NP_172303.5; NM_100699.6.
DR AlphaFoldDB; F4HW04; -.
DR SMR; F4HW04; -.
DR STRING; 3702.AT1G08260.1; -.
DR PaxDb; F4HW04; -.
DR PRIDE; F4HW04; -.
DR ProteomicsDB; 220613; -.
DR EnsemblPlants; AT1G08260.1; AT1G08260.1; AT1G08260.
DR GeneID; 837346; -.
DR Gramene; AT1G08260.1; AT1G08260.1; AT1G08260.
DR KEGG; ath:AT1G08260; -.
DR Araport; AT1G08260; -.
DR TAIR; locus:2199973; AT1G08260.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_1_1; -.
DR InParanoid; F4HW04; -.
DR OMA; MLDQCRY; -.
DR OrthoDB; 39650at2759; -.
DR PRO; PR:F4HW04; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HW04; baseline and differential.
DR Genevisible; F4HW04; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006287; P:base-excision repair, gap-filling; IBA:GO_Central.
DR GO; GO:0045004; P:DNA replication proofreading; IBA:GO_Central.
DR GO; GO:0010086; P:embryonic root morphogenesis; IMP:TAIR.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0048579; P:negative regulation of long-day photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR GO; GO:0051302; P:regulation of cell division; IMP:TAIR.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR013697; DNA_pol_e_suA_C.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR029703; POL2.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10670; PTHR10670; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08490; DUF1744; 1.
DR SMART; SM01159; DUF1744; 1.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; DNA replication; DNA-binding; DNA-directed DNA polymerase; Iron;
KW Iron-sulfur; Metal-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..2161
FT /note="DNA polymerase epsilon catalytic subunit A"
FT /id="PRO_0000420240"
FT ZN_FING 2038..2068
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MOTIF 5..12
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 1137..1144
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250"
FT MOTIF 1239..1246
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000250"
FT MOTIF 2099..2116
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MOTIF 2130..2137
FT /note="Nuclear localization signal 4"
FT /evidence="ECO:0000250"
FT BINDING 2038
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2041
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2063
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2068
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2099
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2116
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MUTAGEN 469
FT /note="G->R: In til1-4; lengthening of the cell cycle
FT during embryo development and alters cell type patterning
FT of the hypophyseal lineage in the root, leading to a
FT displacement of the root pole from its normal position on
FT top of the suspensor. Slow growing roots, slightly delayed
FT flowering, altered floral phyllotaxis, a reduced number of
FT ovules, abnormally developing ovules, and reduced
FT fertility."
FT /evidence="ECO:0000269|PubMed:16278345"
FT MUTAGEN 992
FT /note="G->R: In esd7-1; early flowering independently of
FT photoperiod, shortened inflorescence internodes and altered
FT flowers, leaves and roots development. Enrichement in
FT acetylated H3 and trimethylated H3 'Lys-4' (H3K4me3)
FT activating epigenetic marks of the chromatin of FT and AG
FT loci."
FT /evidence="ECO:0000269|PubMed:19947980"
SQ SEQUENCE 2161 AA; 248897 MW; 0D17C1600609CD2B CRC64;
MSGDNRRRDR KDTRWSKKPK VVNTAEDELE SKLGFGLFSE GETRLGWLLT FSSSSWEDRD
TGKVYSCVDL YFVTQDGFSF KTKYKFRPYF YAATKDKMEL ELEAYLRRRY ERQVADIEIV
EKEDLDLKNH LSGLQKKYLK ISFDTVQQLM EVKRDLLHIV ERNQAKFDAL EAYESILAGK
REQRPQDCLD SIVDLREYDV PYHVRFAIDN DVRSGQWYNV SISSTDVILE KRTDLLQRAE
VRVCAFDIET TKLPLKFPDA EYDQIMMISY MVDGQGFLII NRECVGEDVE DLEYTPKPEF
EGYFKVTNVK NEVELLQRWF YHMQELKPGI YVTYNGDFFD WPFIERRASH HGIKMNEELG
FRCDQNQGEC RAKFACHLDC FAWVKRDSYL PQGSHGLKAV TKAKLGYDPL EVNPEDMVRF
AMEKPQTMAS YSVSDAVATY YLYMTYVNPF IFSLATIIPM VPDEVLRKGS GTLCEMLLMV
EAYKANVVCP NKNQADPEKF YQNQLLESET YIGGHVECLE SGVFRSDIPT SFKLDSSAYQ
QLIDNLGRDL EYAITVEGKM RMDSISNYDE VKDEIKEKLE KLRDDPIREE GPLIYHLDVA
AMYPNIILTN RLQPPSIVTD EICTACDFNR PGKTCLRKLE WVWRGVTFMG KKSDYYHLKK
QIESEFVDAG ANIMSSKSFL DLPKVDQQSK LKERLKKYCQ KAYKRVLDKP ITEVREAGIC
MRENPFYVDT VRSFRDRRYE YKTLNKVWKG KLSEAKASGN SIKIQEAQDM VVVYDSLQLA
HKCILNSFYG YVMRKGARWY SMEMAGVVTY TGAKIIQNAR LLIERIGKPL ELDTDGIWCC
LPGSFPENFT FKTIDMKKLT ISYPCVMLNV DVAKNNTNDQ YQTLVDPVRK TYKSHSECSI
EFEVDGPYKA MIIPASKEEG ILIKKRYAVF NHDGTLAELK GFEIKRRGEL KLIKVFQAEL
FDKFLHGSTL EECYSAVAAV ADRWLDLLDN QGKDIADSEL LDYISESSTM SKSLADYGEQ
KSCAVTTAKR LAEFLGVTMV KDKGLRCQYI VACEPKGTPV SERAVPVAIF TTNPEVMKFH
LRKWCKTSSD VGIRLIIDWS YYKQRLSSAI QKVITIPAAM QKVANPVPRV LHPDWLHKKV
REKDDKFRQR KLVDMFSSAN KDVVLDTDLP VTKDNVEDIE DFCKENRPSV KGPKPIARSY
EVNKKQSECE QQESWDTEFH DISFQNIDKS VNYQGWLELK KRKWKVTLEK KKKRRLGDLR
SSNQVDTHEI NQKVGQGRGG VGSYFRRPEE ALTSSHWQII QLVPSPQSGQ FFAWVVVEGL
MLKIPLSIPR VFYINSKVPI DEYFQGKCVN KILPHGRPCY SLTEVKIQED QFKKESKKRA
ALLADPGVEG IYETKVPLEF SAICQIGCVC KIDNKAKHRN TQDGWEVGEL HMKTTTECHY
LKRSIPLVYL YNSTSTGRAI YVLYCHVSKL MSAVVVDPFN GNELLPSALE RQFRDSCLEL
SLDSLSWDGI RFQVHYVDHP EAAKKIIQRA ISEYREENCG PTVAVIECPD FTFMKEGIKA
LDDFPCVRIP FNDDDNSYQP VSWQRPAAKI AMFRCAAAFQ WLDRRITQSR YAHVPLGNFG
LDWLTFTIDI FLSRALRDQQ QVLWVSDNGV PDLGGINNEE AFFADEVQQT SLVFPGAYRK
VSVELKIHNL AVNALLKSNL VNEMEGGGFM GFEQDVNPRG INSNDNTSFD ETTGCAQAFR
VLKQLIHSCL TDVRKSKNIY ADSILQRLSW WLCSPSSKLH DPALHLMLHK VMQKVFALLL
TDLRRLGAII IYADFSKVII DTVKFDLSAA KAYCESLLST VRNSDIFEWI LLEPVHYWHS
LLFMDQYNYA GIRADDEISL DEVTIEPKWS VARHLPEYIE RDFIIIIAKF IFDPWKFAIE
NKKGSSESLE AQMIEYLREQ IGSTFINMLV KKVDDIMSHM KEINVSDASR VSGQAPKGDY
SLEFIQVISA VLALDQNVQQ DVLVMRKSLL KYIKVKECAA EAEFLDPGPS FILPNVACSN
CDAYRDLDIC RDPALLTEKE WSCADTQCGK IYDREQMESS LLEMVRQRER MYHMQDVVCI
RCNQVKAAHL TEQCECSGSF RCKESGSEFS KRMEIFMDIA KRQKFRLLEE YISWIIYGPS
Y
