F4HW04 (DPOE1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA polymerase epsilon catalytic subunit A
EC=2.7.7.7

Alternative name(s):
DNA polymerase 2 a
Short name=AtPOL2a
DNA polymerase II subunit a
Protein ABA OVERLY SENSITIVE a
Protein EARLY IN SHORT DAYS 7
Protein EMBRYO DEFECTIVE 142
Protein EMBRYO DEFECTIVE 2284
Protein EMBRYO DEFECTIVE 529
Protein TILTED 1

Gene names

Name:	POL2A
Synonyms:	ABO4, EMB142, EMB2284, EMB529, ESD7, TIL1
Ordered Locus Names:	At1g08260
ORF Names:	T23G18.21

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	2161 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA polymerase II participates in chromosomal DNA replication. Required for the timing and determination of cell fate during plant embryogenesis and root pole development, by promoting cell cycle and cell type patterning. Necessary for proper shoot (SAM) and root apical meristem (RAM) functions. Involved in maintaining epigenetic states, controlling hypersensitive response (HR), and mediating abscisic acid (ABA) signaling. Required for flowering repression through a mechanism involving epigenetic gene silencing. May participate in processes involved in chromatin-mediated cellular memory. Ref.3 Ref.4 Ref.5 Ref.6
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Cofactor	Binds 1 4Fe-4S cluster By similarity.
Subunit structure	Heterotetramer By similarity. Subunit of the DNA polymerase II. Interacts with DPB2 and LHP1/TFL2. Ref.4 Ref.6
Subcellular location	Nucleus By similarity.
Tissue specificity	Mostly expressed at low levels in inflorescence (floral meristem and flowers until anthesis), and, to a lower extent, in roots, seeds and leaves. Ref.3 Ref.6
Developmental stage	Present in actively dividing cells such as root and shoot meristematic regions, young leaves and stems, inflorescences and siliques. Ref.6
Domain	The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes By similarity. The DNA polymerase activity domain resides in the N-terminal half of the protein, while the C-terminus is necessary for complexing subunits B and C By similarity.
Disruption phenotype	Lethal, with sporophytic embryo-defective with an arrest at the globular stage during embryo development. Abnormal cell division characterized by several rounds of mitosis with aberrant planes of division. Ref.3 Ref.4 Ref.6
Sequence similarities	Belongs to the DNA polymerase type-B family. Contains 1 CysA-type zinc finger.
Sequence caution	The sequence AAF18240.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	4Fe-4S DNA-binding Iron Iron-sulfur Metal-binding Zinc
Molecular function	DNA-directed DNA polymerase Nucleotidyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	epsilon DNA polymerase complex Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2161	2161	DNA polymerase epsilon catalytic subunit A		PRO_0000420240
Regions
	Zinc finger	2038 – 2068	31	CysA-type
	Motif	5 – 12	8	Nuclear localization signal 1 By similarity
	Motif	1137 – 1144	8	Nuclear localization signal 2 By similarity
	Motif	1239 – 1246	8	Nuclear localization signal 3 By similarity
	Motif	2099 – 2116	18	CysB motif
	Motif	2130 – 2137	8	Nuclear localization signal 4 By similarity
Sites
	Metal binding	2038	1	Zinc By similarity
	Metal binding	2041	1	Zinc By similarity
	Metal binding	2063	1	Zinc By similarity
	Metal binding	2068	1	Zinc By similarity
	Metal binding	2099	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	2102	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	2114	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	2116	1	Iron-sulfur (4Fe-4S) By similarity
Experimental info
	Mutagenesis	469	1	G → R in til1-4; lengthening of the cell cycle during embryo development and alters cell type patterning of the hypophyseal lineage in the root, leading to a displacement of the root pole from its normal position on top of the suspensor. Slow growing roots, slightly delayed flowering, altered floral phyllotaxis, a reduced number of ovules, abnormally developing ovules, and reduced fertility. Ref.3
	Mutagenesis	992	1	G → R in esd7-1; early flowering independently of photoperiod, shortened inflorescence internodes and altered flowers, leaves and roots development. Enrichement in acetylated H3 and trimethylated H3 'Lys-4' (H3K4me3) activating epigenetic marks of the chromatin of FT and AG loci. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	F4HW04 [UniParc]. Last modified June 28, 2011. Version 1. Checksum: 0D17C1600609CD2B	FASTA	2,161	248,897
	10 20 30 40 50 60 MSGDNRRRDR KDTRWSKKPK VVNTAEDELE SKLGFGLFSE GETRLGWLLT FSSSSWEDRD 70 80 90 100 110 120 TGKVYSCVDL YFVTQDGFSF KTKYKFRPYF YAATKDKMEL ELEAYLRRRY ERQVADIEIV 130 140 150 160 170 180 EKEDLDLKNH LSGLQKKYLK ISFDTVQQLM EVKRDLLHIV ERNQAKFDAL EAYESILAGK 190 200 210 220 230 240 REQRPQDCLD SIVDLREYDV PYHVRFAIDN DVRSGQWYNV SISSTDVILE KRTDLLQRAE 250 260 270 280 290 300 VRVCAFDIET TKLPLKFPDA EYDQIMMISY MVDGQGFLII NRECVGEDVE DLEYTPKPEF 310 320 330 340 350 360 EGYFKVTNVK NEVELLQRWF YHMQELKPGI YVTYNGDFFD WPFIERRASH HGIKMNEELG 370 380 390 400 410 420 FRCDQNQGEC RAKFACHLDC FAWVKRDSYL PQGSHGLKAV TKAKLGYDPL EVNPEDMVRF 430 440 450 460 470 480 AMEKPQTMAS YSVSDAVATY YLYMTYVNPF IFSLATIIPM VPDEVLRKGS GTLCEMLLMV 490 500 510 520 530 540 EAYKANVVCP NKNQADPEKF YQNQLLESET YIGGHVECLE SGVFRSDIPT SFKLDSSAYQ 550 560 570 580 590 600 QLIDNLGRDL EYAITVEGKM RMDSISNYDE VKDEIKEKLE KLRDDPIREE GPLIYHLDVA 610 620 630 640 650 660 AMYPNIILTN RLQPPSIVTD EICTACDFNR PGKTCLRKLE WVWRGVTFMG KKSDYYHLKK 670 680 690 700 710 720 QIESEFVDAG ANIMSSKSFL DLPKVDQQSK LKERLKKYCQ KAYKRVLDKP ITEVREAGIC 730 740 750 760 770 780 MRENPFYVDT VRSFRDRRYE YKTLNKVWKG KLSEAKASGN SIKIQEAQDM VVVYDSLQLA 790 800 810 820 830 840 HKCILNSFYG YVMRKGARWY SMEMAGVVTY TGAKIIQNAR LLIERIGKPL ELDTDGIWCC 850 860 870 880 890 900 LPGSFPENFT FKTIDMKKLT ISYPCVMLNV DVAKNNTNDQ YQTLVDPVRK TYKSHSECSI 910 920 930 940 950 960 EFEVDGPYKA MIIPASKEEG ILIKKRYAVF NHDGTLAELK GFEIKRRGEL KLIKVFQAEL 970 980 990 1000 1010 1020 FDKFLHGSTL EECYSAVAAV ADRWLDLLDN QGKDIADSEL LDYISESSTM SKSLADYGEQ 1030 1040 1050 1060 1070 1080 KSCAVTTAKR LAEFLGVTMV KDKGLRCQYI VACEPKGTPV SERAVPVAIF TTNPEVMKFH 1090 1100 1110 1120 1130 1140 LRKWCKTSSD VGIRLIIDWS YYKQRLSSAI QKVITIPAAM QKVANPVPRV LHPDWLHKKV 1150 1160 1170 1180 1190 1200 REKDDKFRQR KLVDMFSSAN KDVVLDTDLP VTKDNVEDIE DFCKENRPSV KGPKPIARSY 1210 1220 1230 1240 1250 1260 EVNKKQSECE QQESWDTEFH DISFQNIDKS VNYQGWLELK KRKWKVTLEK KKKRRLGDLR 1270 1280 1290 1300 1310 1320 SSNQVDTHEI NQKVGQGRGG VGSYFRRPEE ALTSSHWQII QLVPSPQSGQ FFAWVVVEGL 1330 1340 1350 1360 1370 1380 MLKIPLSIPR VFYINSKVPI DEYFQGKCVN KILPHGRPCY SLTEVKIQED QFKKESKKRA 1390 1400 1410 1420 1430 1440 ALLADPGVEG IYETKVPLEF SAICQIGCVC KIDNKAKHRN TQDGWEVGEL HMKTTTECHY 1450 1460 1470 1480 1490 1500 LKRSIPLVYL YNSTSTGRAI YVLYCHVSKL MSAVVVDPFN GNELLPSALE RQFRDSCLEL 1510 1520 1530 1540 1550 1560 SLDSLSWDGI RFQVHYVDHP EAAKKIIQRA ISEYREENCG PTVAVIECPD FTFMKEGIKA 1570 1580 1590 1600 1610 1620 LDDFPCVRIP FNDDDNSYQP VSWQRPAAKI AMFRCAAAFQ WLDRRITQSR YAHVPLGNFG 1630 1640 1650 1660 1670 1680 LDWLTFTIDI FLSRALRDQQ QVLWVSDNGV PDLGGINNEE AFFADEVQQT SLVFPGAYRK 1690 1700 1710 1720 1730 1740 VSVELKIHNL AVNALLKSNL VNEMEGGGFM GFEQDVNPRG INSNDNTSFD ETTGCAQAFR 1750 1760 1770 1780 1790 1800 VLKQLIHSCL TDVRKSKNIY ADSILQRLSW WLCSPSSKLH DPALHLMLHK VMQKVFALLL 1810 1820 1830 1840 1850 1860 TDLRRLGAII IYADFSKVII DTVKFDLSAA KAYCESLLST VRNSDIFEWI LLEPVHYWHS 1870 1880 1890 1900 1910 1920 LLFMDQYNYA GIRADDEISL DEVTIEPKWS VARHLPEYIE RDFIIIIAKF IFDPWKFAIE 1930 1940 1950 1960 1970 1980 NKKGSSESLE AQMIEYLREQ IGSTFINMLV KKVDDIMSHM KEINVSDASR VSGQAPKGDY 1990 2000 2010 2020 2030 2040 SLEFIQVISA VLALDQNVQQ DVLVMRKSLL KYIKVKECAA EAEFLDPGPS FILPNVACSN 2050 2060 2070 2080 2090 2100 CDAYRDLDIC RDPALLTEKE WSCADTQCGK IYDREQMESS LLEMVRQRER MYHMQDVVCI 2110 2120 2130 2140 2150 2160 RCNQVKAAHL TEQCECSGSF RCKESGSEFS KRMEIFMDIA KRQKFRLLEE YISWIIYGPS Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Interactions between the cell cycle and embryonic patterning in Arabidopsis uncovered by a mutation in DNA polymerase epsilon." Jenik P.D., Jurkuta R.E.J., Barton M.K. Plant Cell 17:3362-3377(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-469, TISSUE SPECIFICITY.
[4]	"Genetic analysis of two Arabidopsis DNA polymerase epsilon subunits during early embryogenesis." Ronceret A., Guilleminot J., Lincker F., Gadea-Vacas J., Delorme V., Bechtold N., Pelletier G., Delseny M., Chaboute M.-E., Devic M. Plant J. 44:223-236(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY CELL CYCLE, INTERACTION WITH DPB2, GENE FAMILY, NOMENCLATURE.
[5]	"Epigenetic regulation, somatic homologous recombination, and abscisic acid signaling are influenced by DNA polymerase epsilon mutation in Arabidopsis." Yin H., Zhang X., Liu J., Wang Y., He J., Yang T., Hong X., Yang Q., Gong Z. Plant Cell 21:386-402(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: cv. Columbia GL1.
[6]	"EARLY IN SHORT DAYS 7 (ESD7) encodes the catalytic subunit of DNA polymerase epsilon and is required for flowering repression through a mechanism involving epigenetic gene silencing." del Olmo I., Lopez-Gonzalez L., Martin-Trillo M.M., Martinez-Zapater J.M., Pineiro M., Jarillo J.A. Plant J. 61:623-636(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-992, DISRUPTION PHENOTYPE, INTERACTION WITH LHP1/TFL2, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC011438 Genomic DNA. Translation: AAF18240.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE28266.1.
IPI	IPI00534868. IPI01019887.
RefSeq	NP_172303.5. NM_100699.5.
UniGene	At.42268. At.51528.
3D structure databases
HSSP	HSSP built from PDB template 1QHT based on UniProtKB Q56366.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT1G08260.1-P.
Proteomic databases
PRIDE	F4HW04.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G08260.1; AT1G08260.1; AT1G08260.
GeneID	837346.
KEGG	ath:AT1G08260.
Organism-specific databases
TAIR	At1g08260.
Phylogenomic databases
eggNOG	COG0417.
InParanoid	Q9SGD5.
KO	K02324.
OMA	QEESQDL.
ProtClustDB	CLSN2681171.
Family and domain databases
InterPro	IPR006172. DNA-dir_DNA_pol_B. IPR006133. DNA-dir_DNA_pol_B_exonuc. IPR006134. DNA-dir_DNA_pol_B_multi_dom. IPR013697. DNA_pol_e_suA_C. IPR012337. RNaseH-like_dom. [Graphical view]
Pfam	PF00136. DNA_pol_B. 1 hit. PF03104. DNA_pol_B_exo1. 1 hit. PF08490. DUF1744. 1 hit. [Graphical view]
SMART	SM00486. POLBc. 1 hit. [Graphical view]
SUPFAM	SSF53098. RNaseH_fold. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DPOE1_ARATH

Accession

Primary (citable) accession number: F4HW04
Secondary accession number(s): B3H4I0, Q9SGD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2012
Last sequence update:	June 28, 2011
Last modified:	May 1, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program