DPA_ARATH
ID DPA_ARATH Reviewed; 292 AA.
AC Q9FNY3; Q9LZ55;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Transcription factor-like protein DPA;
DE AltName: Full=DP-like protein A;
DE Short=AtDPbA;
DE AltName: Full=E2F dimerization partner protein A;
DE Short=AtDP2a;
GN Name=DPA; Synonyms=DP2, DP2A; OrderedLocusNames=At5g02470;
GN ORFNames=T22P11.60;
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 [MRNA], AND INTERACTION WITH E2FA AND E2FB.
RC STRAIN=cv. Columbia;
RX PubMed=11108847; DOI=10.1016/s0014-5793(00)02238-9;
RA Magyar Z., Atanassova A., De Veylder L., Rombauts S., Inze D.;
RT "Characterization of two distinct DP-related genes from Arabidopsis
RT thaliana.";
RL FEBS Lett. 486:79-87(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Rossignol P.;
RT "E2F family transcription factors: AtE2F-a and AtDP-a, induce Arabidopsis
RT leaf cells to re-enter S phase.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=11669580; DOI=10.1023/a:1011848528377;
RA de Jager S.M., Menges M., Bauer U.M., Murra J.A.;
RT "Arabidopsis E2F1 binds a sequence present in the promoter of S-phase-
RT regulated gene AtCDC6 and is a member of a multigene family with
RT differential activities.";
RL Plant Mol. Biol. 47:555-568(2001).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11889041; DOI=10.1093/emboj/21.6.1360;
RA De Veylder L., Beeckman T., Beemster G.T., de Almeida Engler J.,
RA Ormenese S., Maes S., Naudts M., Van Der Schueren E., Jacqmard A.,
RA Engler G., Inze D.;
RT "Control of proliferation, endoreduplication and differentiation by the
RT Arabidopsis E2Fa-DPa transcription factor.";
RL EMBO J. 21:1360-1368(2002).
RN [9]
RP INTERACTION WITH E2FA; E2FB AND E2FC, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11786543; DOI=10.1074/jbc.m110616200;
RA Mariconti L., Pellegrini B., Cantoni R., Stevens R., Bergounioux C.,
RA Cella R., Albani D.;
RT "The E2F family of transcription factors from Arabidopsis thaliana. Novel
RT and conserved components of the retinoblastoma/E2F pathway in plants.";
RL J. Biol. Chem. 277:9911-9919(2002).
RN [10]
RP FUNCTION, INTERACTION WITH E2FA; E2FB AND E2FC, AND SUBCELLULAR LOCATION.
RX PubMed=11891240; DOI=10.1104/pp.010642;
RA Kosugi S., Ohashi Y.;
RT "Interaction of the Arabidopsis E2F and DP proteins confers their
RT concomitant nuclear translocation and transactivation.";
RL Plant Physiol. 128:833-843(2002).
RN [11]
RP INDUCTION BY ERF114.
RX PubMed=23616605; DOI=10.1104/pp.113.214049;
RA Mehrnia M., Balazadeh S., Zanor M.I., Mueller-Roeber B.;
RT "EBE, an AP2/ERF transcription factor highly expressed in proliferating
RT cells, affects shoot architecture in Arabidopsis.";
RL Plant Physiol. 162:842-857(2013).
CC -!- FUNCTION: Involved in the regulation of the G1/S transition. Increases
CC the DNA binding and the transactivation activities of E2F proteins
CC after heterodimerization. The complex DPA/E2FA promotes cell division
CC and acts as a regulator of the endocycle. Positively regulates the
CC activity of S phase-specific genes. {ECO:0000269|PubMed:11889041,
CC ECO:0000269|PubMed:11891240}.
CC -!- SUBUNIT: Heterodimer with E2F. Interacts preferentially with E2FA and
CC E2FB, but also with E2FC. {ECO:0000269|PubMed:11108847,
CC ECO:0000269|PubMed:11786543, ECO:0000269|PubMed:11891240}.
CC -!- INTERACTION:
CC Q9FNY3; Q9FNY0: E2FA; NbExp=6; IntAct=EBI-1774763, EBI-1774747;
CC Q9FNY3; Q9FV71: E2FB; NbExp=10; IntAct=EBI-1774763, EBI-1774719;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891240}. Nucleus
CC {ECO:0000269|PubMed:11891240}. Note=Interaction with E2F stimulates the
CC nuclear translocation.
CC -!- TISSUE SPECIFICITY: Strongly expressed in the actively dividing tissues
CC of the shoot apical meristem, young leaf primordia, the vascular
CC tissues of the maturing leaf primordia and axillary buds.
CC {ECO:0000269|PubMed:11889041}.
CC -!- DEVELOPMENTAL STAGE: Expressed in a cell cycle-dependent manner. Low
CC expression at the G1/S transition and increases during the S phase.
CC S/G2 transitions. {ECO:0000269|PubMed:11669580}.
CC -!- INDUCTION: Up-regulated by the transcription factor ERF114.
CC {ECO:0000269|PubMed:23616605}.
CC -!- DOMAIN: The DIM domain (143-214) is necessary but not sufficient for
CC heterodimerization.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB85984.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ294531; CAC15483.1; -; mRNA.
DR EMBL; AJ319027; CAC87459.1; -; mRNA.
DR EMBL; AL162971; CAB85984.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED90475.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90476.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90477.1; -; Genomic_DNA.
DR EMBL; BT005286; AAO63350.1; -; mRNA.
DR EMBL; AK117135; BAC41813.1; -; mRNA.
DR PIR; T48268; T48268.
DR RefSeq; NP_195867.2; NM_120325.4.
DR RefSeq; NP_851027.1; NM_180696.2.
DR RefSeq; NP_851028.1; NM_180697.3.
DR AlphaFoldDB; Q9FNY3; -.
DR SMR; Q9FNY3; -.
DR BioGRID; 16265; 23.
DR IntAct; Q9FNY3; 11.
DR MINT; Q9FNY3; -.
DR STRING; 3702.AT5G02470.2; -.
DR iPTMnet; Q9FNY3; -.
DR PaxDb; Q9FNY3; -.
DR PRIDE; Q9FNY3; -.
DR ProteomicsDB; 220293; -.
DR EnsemblPlants; AT5G02470.1; AT5G02470.1; AT5G02470.
DR EnsemblPlants; AT5G02470.2; AT5G02470.2; AT5G02470.
DR EnsemblPlants; AT5G02470.3; AT5G02470.3; AT5G02470.
DR GeneID; 830987; -.
DR Gramene; AT5G02470.1; AT5G02470.1; AT5G02470.
DR Gramene; AT5G02470.2; AT5G02470.2; AT5G02470.
DR Gramene; AT5G02470.3; AT5G02470.3; AT5G02470.
DR KEGG; ath:AT5G02470; -.
DR Araport; AT5G02470; -.
DR TAIR; locus:2181788; AT5G02470.
DR eggNOG; KOG2829; Eukaryota.
DR HOGENOM; CLU_039874_4_0_1; -.
DR InParanoid; Q9FNY3; -.
DR OMA; GWGLREF; -.
DR OrthoDB; 1046304at2759; -.
DR PhylomeDB; Q9FNY3; -.
DR PRO; PR:Q9FNY3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNY3; baseline and differential.
DR Genevisible; Q9FNY3; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070176; C:DRM complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd14458; DP_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.20.140.80; -; 1.
DR InterPro; IPR037241; E2F-DP_heterodim.
DR InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
DR InterPro; IPR038168; TF_DP_C_sf.
DR InterPro; IPR014889; Transc_factor_DP_C.
DR InterPro; IPR015648; Transcrpt_fac_DP.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12548; PTHR12548; 1.
DR Pfam; PF08781; DP; 1.
DR Pfam; PF02319; E2F_TDP; 1.
DR PIRSF; PIRSF009404; Transcription_factor_DP; 1.
DR SMART; SM01138; DP; 1.
DR SMART; SM01372; E2F_TDP; 1.
DR SUPFAM; SSF144074; SSF144074; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Activator; Cell cycle; Coiled coil; Cytoplasm; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..292
FT /note="Transcription factor-like protein DPA"
FT /id="PRO_0000405866"
FT DNA_BIND 51..135
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 163..184
FT /evidence="ECO:0000255"
FT MOTIF 101..135
FT /note="DEF box"
FT /evidence="ECO:0000250"
SQ SEQUENCE 292 AA; 33038 MW; 644324E13561FEC5 CRC64;
MSMEMELFVT PEKQRQHPSV SVEKTPVRRK LIVDDDSEIG SEKKGQSRTS GGGLRQFSVM
VCQKLEAKKI TTYKEVADEI ISDFATIKQN AEKPLNENEY NEKNIRRRVY DALNVFMALD
IIARDKKEIR WKGLPITCKK DVEEVKMDRN KVMSSVQKKA AFLKELREKV SSLESLMSRN
QEMVVKTQGP AEGFTLPFIL LETNPHAVVE IEISEDMQLV HLDFNSTPFS VHDDAYILKL
MQEQKQEQNR VSSSSSTHHQ SQHSSAHSSS SSCIASGTSG PVCWNSGSID TR
