DDL_ARATH
ID DDL_ARATH Reviewed; 314 AA.
AC Q8W4D8; Q9LJU3;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=FHA domain-containing protein DDL;
DE AltName: Full=Protein DAWDLE;
GN Name=DDL; OrderedLocusNames=At3g20550; ORFNames=K10D20.9;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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 [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16679419; DOI=10.1104/pp.106.076893;
RA Morris E.R., Chevalier D., Walker J.C.;
RT "DAWDLE, a forkhead-associated domain gene, regulates multiple aspects of
RT plant development.";
RL Plant Physiol. 141:932-941(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH DCL1.
RX PubMed=18632581; DOI=10.1073/pnas.0804218105;
RA Yu B., Bi L., Zheng B., Ji L., Chevalier D., Agarwal M., Ramachandran V.,
RA Li W., Lagrange T., Walker J.C., Chen X.;
RT "The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act in
RT small RNA biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10073-10078(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 180-310, INTERACTION WITH DCL1,
RP AND MUTAGENESIS OF ARG-223 AND SER-238.
RX PubMed=23313986; DOI=10.1093/mp/sst007;
RA Machida S., Yuan Y.A.;
RT "Crystal structure of Arabidopsis thaliana Dawdle forkhead-associated
RT domain reveals a conserved phospho-threonine recognition cleft for dicer-
RT like 1 binding.";
RL Mol. Plant 6:1290-1300(2013).
CC -!- FUNCTION: Involved in the microRNA (miRNA) and short interfering RNA
CC (siRNA) biogenesis. May facilitate DCL1 to access or recognize primary
CC miRNAs. Binds RNA non-specifically. {ECO:0000269|PubMed:18632581}.
CC -!- SUBUNIT: Interacts with DCL1 (via N-terminus).
CC {ECO:0000269|PubMed:18632581, ECO:0000269|PubMed:23313986}.
CC -!- INTERACTION:
CC Q8W4D8; Q9SP32: DCL1; NbExp=2; IntAct=EBI-2015534, EBI-632627;
CC Q8W4D8; Q39204: MYC2; NbExp=6; IntAct=EBI-2015534, EBI-1792336;
CC Q8W4D8; Q9LVM5: TTL; NbExp=4; IntAct=EBI-2015534, EBI-1803584;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16679419}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, lateral roots, vascular strands
CC of roots and leaves, vegetative meristems, pollen and developing seeds.
CC {ECO:0000269|PubMed:16679419}.
CC -!- DISRUPTION PHENOTYPE: Delayed growth and reduced fertility. Defective
CC roots, shoots and flowers. Reduced seed set. Reduced levels of primary
CC miRNAs as well as mature miRNAs. {ECO:0000269|PubMed:16679419,
CC ECO:0000269|PubMed:18632581}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01163.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000410; BAB01163.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76394.1; -; Genomic_DNA.
DR EMBL; AY062626; AAL32704.1; -; mRNA.
DR EMBL; BT000005; AAN15324.1; -; mRNA.
DR RefSeq; NP_188691.1; NM_112947.4.
DR PDB; 3VPY; X-ray; 1.70 A; A=180-310.
DR PDBsum; 3VPY; -.
DR AlphaFoldDB; Q8W4D8; -.
DR SMR; Q8W4D8; -.
DR BioGRID; 6933; 14.
DR DIP; DIP-46412N; -.
DR IntAct; Q8W4D8; 13.
DR STRING; 3702.AT3G20550.1; -.
DR iPTMnet; Q8W4D8; -.
DR PaxDb; Q8W4D8; -.
DR PRIDE; Q8W4D8; -.
DR ProteomicsDB; 224064; -.
DR EnsemblPlants; AT3G20550.1; AT3G20550.1; AT3G20550.
DR GeneID; 821601; -.
DR Gramene; AT3G20550.1; AT3G20550.1; AT3G20550.
DR KEGG; ath:AT3G20550; -.
DR Araport; AT3G20550; -.
DR TAIR; locus:2085740; AT3G20550.
DR eggNOG; KOG1882; Eukaryota.
DR HOGENOM; CLU_022457_2_1_1; -.
DR OMA; MTKEKRH; -.
DR OrthoDB; 955935at2759; -.
DR PhylomeDB; Q8W4D8; -.
DR PRO; PR:Q8W4D8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8W4D8; baseline and differential.
DR Genevisible; Q8W4D8; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0035196; P:miRNA processing; IDA:TAIR.
DR GO; GO:0048638; P:regulation of developmental growth; IMP:UniProtKB.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..314
FT /note="FHA domain-containing protein DDL"
FT /id="PRO_0000392079"
FT DOMAIN 219..282
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MUTAGEN 223
FT /note="R->A: Loss of interaction with DCL1."
FT /evidence="ECO:0000269|PubMed:23313986"
FT MUTAGEN 238
FT /note="S->A: Loss of interaction with DCL1."
FT /evidence="ECO:0000269|PubMed:23313986"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:3VPY"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:3VPY"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:3VPY"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3VPY"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:3VPY"
FT STRAND 258..268
FT /evidence="ECO:0007829|PDB:3VPY"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:3VPY"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:3VPY"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:3VPY"
SQ SEQUENCE 314 AA; 36953 MW; 42F3A7C9DFF14B68 CRC64;
MAPSSRSPSP RTKRLRRARG EKEIGRSRER EDDGREREKR NSRERDRDIG RDRDRERKGE
GERDREVGDK RRRSGREDTE KRRRTRTDDE RYSRGRHERS TSPSDRSHRS SRRSPERAIA
SRHDEGSNAR GGSEEPNVEE DSVARMRAVE EALAAKKKEE PSFELSGKLA EETNRYRGIT
LLFNEPPEAR KPSERWRLYV FKDGEPLNEP LCLHRQSCYL FGRERRIADI PTDHPSCSKQ
HAVIQYREME KEKPDGMMGK QVKPYIMDLG STNKTYINES PIEPQRYYEL FEKDTIKFGN
SSREYVLLHE NSAE
