Entry euk: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   10-MAY-2017, entry version 50.
DE   RecName: Full=DNA polymerase epsilon catalytic subunit A;
DE            EC=2.7.7.7;
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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
RP   WITH 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
RT   during 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
RT   acid 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
RP   WITH 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.,
RA   Martinez-Zapater J.M., 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
CC       fate during plant embryogenesis and root pole development, by
CC       promoting cell cycle and cell type patterning. Necessary for
CC       proper shoot (SAM) and root apical meristem (RAM) functions.
CC       Involved in maintaining epigenetic states, controlling
CC       hypersensitive response (HR), and mediating abscisic acid (ABA)
CC       signaling. Required for flowering repression through a mechanism
CC       involving epigenetic gene silencing. May participate in processes
CC       involved in chromatin-mediated cellular memory.
CC       {ECO:0000269|PubMed:16212602, ECO:0000269|PubMed:16278345,
CC       ECO:0000269|PubMed:19244142, ECO:0000269|PubMed:19947980}.
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC   -!- SUBUNIT: Heterotetramer (By similarity). Subunit of the DNA
CC       polymerase II (PubMed:16212602, PubMed:19947980). Interacts (via
CC       C-terminus) with DPB2 (PubMed:16212602). Interacts with LHP1/TFL2
CC       (PubMed:19947980). {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
CC       inflorescence (floral meristem and flowers until anthesis), and,
CC       to a lower extent, in roots, seeds and leaves.
CC       {ECO:0000269|PubMed:16278345, ECO:0000269|PubMed:19947980}.
CC   -!- DEVELOPMENTAL STAGE: Present in actively dividing cells such as
CC       root and shoot meristematic regions, young leaves and stems,
CC       inflorescences and siliques. {ECO:0000269|PubMed:19947980}.
CC   -!- INDUCTION: Follows a cell-cycle-dependent expression with a
CC       maximal induction in the S phase and another induction at the G2/M
CC       transition. {ECO:0000269|PubMed:16212602}.
CC   -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for
CC       the formation of polymerase complexes. {ECO:0000250}.
CC   -!- DOMAIN: The DNA polymerase activity domain resides in the N-
CC       terminal half of the protein, while the C-terminus is necessary
CC       for complexing subunits B and C. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Lethal, with sporophytic embryo-defective
CC       with an arrest at the globular stage during embryo development.
CC       Abnormal cell division characterized by several rounds of mitosis
CC       with aberrant 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.
CC       {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   UniGene; At.42268; -.
DR   ProteinModelPortal; F4HW04; -.
DR   SMR; F4HW04; -.
DR   STRING; 3702.AT1G08260.1; -.
DR   PaxDb; F4HW04; -.
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   eggNOG; COG0417; LUCA.
DR   InParanoid; F4HW04; -.
DR   KO; K02324; -.
DR   OMA; CENKSMS; -.
DR   OrthoDB; EOG0936001P; -.
DR   Reactome; R-ATH-174430; Telomere C-strand synthesis initiation.
DR   Reactome; R-ATH-68952; DNA replication initiation.
DR   Reactome; R-ATH-68962; Activation of the pre-replicative complex.
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; IDA: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; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 2.
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; IPR013697; DNA_pol_e_suA_C.
DR   InterPro; IPR023211; DNA_pol_palm_dom.
DR   InterPro; IPR029703; POL2.
DR   InterPro; IPR012337; RNaseH-like_dom.
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; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Complete proteome; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotidyltransferase; Nucleus; Reference proteome; Transferase;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   2161       DNA polymerase epsilon catalytic subunit
FT                                A.
FT                                /FTId=PRO_0000420240.
FT   ZN_FING    2038   2068       CysA-type.
FT   MOTIF         5     12       Nuclear localization signal 1.
FT                                {ECO:0000250}.
FT   MOTIF      1137   1144       Nuclear localization signal 2.
FT                                {ECO:0000250}.
FT   MOTIF      1239   1246       Nuclear localization signal 3.
FT                                {ECO:0000250}.
FT   MOTIF      2099   2116       CysB motif.
FT   MOTIF      2130   2137       Nuclear localization signal 4.
FT                                {ECO:0000250}.
FT   METAL      2038   2038       Zinc. {ECO:0000250}.
FT   METAL      2041   2041       Zinc. {ECO:0000250}.
FT   METAL      2063   2063       Zinc. {ECO:0000250}.
FT   METAL      2068   2068       Zinc. {ECO:0000250}.
FT   METAL      2099   2099       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL      2102   2102       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL      2114   2114       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL      2116   2116       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   MUTAGEN     469    469       G->R: In til1-4; lengthening of the cell
FT                                cycle during embryo development and
FT                                alters cell type patterning of the
FT                                hypophyseal lineage in the root, leading
FT                                to a displacement of the root pole from
FT                                its normal position on top of the
FT                                suspensor. Slow growing roots, slightly
FT                                delayed flowering, altered floral
FT                                phyllotaxis, a reduced number of ovules,
FT                                abnormally developing ovules, and reduced
FT                                fertility. {ECO:0000269|PubMed:16278345}.
FT   MUTAGEN     992    992       G->R: In esd7-1; early flowering
FT                                independently of photoperiod, shortened
FT                                inflorescence internodes and altered
FT                                flowers, leaves and roots development.
FT                                Enrichement in acetylated H3 and
FT                                trimethylated H3 'Lys-4' (H3K4me3)
FT                                activating epigenetic marks of the
FT                                chromatin of FT and AG loci.
FT                                {ECO:0000269|PubMed:19947980}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       239    843       ismart:POLBc [T]
FT   MYHIT      1509   1872       ipfam:DUF1744 [T]
FT   MYHIT        74    400       ipfam:DNA_pol_B_exo1 [T]
FT   MYHIT       746   1076       ipfam:DNA_pol_B [T]
FT   MYHIT      1488   1872       ismart:DUF1744 [T]
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
//