DRB4_ARATH
ID DRB4_ARATH Reviewed; 355 AA.
AC Q8H1D4; B5BUY7; Q8VXY2; Q9LZI5;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Double-stranded RNA-binding protein 4;
DE AltName: Full=dsRNA-binding protein 4;
DE Short=AtDRB4;
GN Name=DBR4; OrderedLocusNames=At3g62800; ORFNames=F26K9.230;
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Kobayashi K., Tomita R., Sakamoto M.;
RT "Efficient protocol for exhaustive detection of RNA viruses with the
RT isolation of viral replicative form double-stranded RNA using recombinant
RT plant dsRNA binding protein.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH DCL4; DRB1 AND DRB5.
RX PubMed=15821876; DOI=10.1007/s11103-004-6853-5;
RA Hiraguri A., Itoh R., Kondo N., Nomura Y., Aizawa D., Murai Y., Koiwa H.,
RA Seki M., Shinozaki K., Fukuhara T.;
RT "Specific interactions between Dicer-like proteins and HYL1/DRB-family
RT dsRNA-binding proteins in Arabidopsis thaliana.";
RL Plant Mol. Biol. 57:173-188(2005).
RN [6]
RP FUNCTION.
RX PubMed=16682354; DOI=10.1016/j.cub.2006.03.035;
RA Adenot X., Elmayan T., Lauressergues D., Boutet S., Bouche N.,
RA Gasciolli V., Vaucheret H.;
RT "DRB4-dependent TAS3 trans-acting siRNAs control leaf morphology through
RT AGO7.";
RL Curr. Biol. 16:927-932(2006).
RN [7]
RP FUNCTION, INTERACTION WITH DCL4, AND DISRUPTION PHENOTYPE.
RX PubMed=17221360; DOI=10.1007/s11103-006-9125-8;
RA Nakazawa Y., Hiraguri A., Moriyama H., Fukuhara T.;
RT "The dsRNA-binding protein DRB4 interacts with the Dicer-like protein DCL4
RT in vivo and functions in the trans-acting siRNA pathway.";
RL Plant Mol. Biol. 63:777-785(2007).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18625233; DOI=10.1016/j.febslet.2008.07.004;
RA Curtin S.J., Watson J.M., Smith N.A., Eamens A.L., Blanchard C.L.,
RA Waterhouse P.M.;
RT "The roles of plant dsRNA-binding proteins in RNAi-like pathways.";
RL FEBS Lett. 582:2753-2760(2008).
RN [9]
RP INTERACTION WITH CAULIFLOWER MOSAIC VIRUS TRANSACTIVATOR/VIROPLASMIN
RP PROTEIN.
RX PubMed=18615098; DOI=10.1038/emboj.2008.129;
RA Haas G., Azevedo J., Moissiard G., Geldreich A., Himber C., Bureau M.,
RA Fukuhara T., Keller M., Voinnet O.;
RT "Nuclear import of CaMV P6 is required for infection and suppression of the
RT RNA silencing factor DRB4.";
RL EMBO J. 27:2102-2112(2008).
RN [10]
RP FUNCTION.
RX PubMed=18799732; DOI=10.1073/pnas.0805760105;
RA Qu F., Ye X., Morris T.J.;
RT "Arabidopsis DRB4, AGO1, AGO7, and RDR6 participate in a DCL4-initiated
RT antiviral RNA silencing pathway negatively regulated by DCL1.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:14732-14737(2008).
RN [11]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Double-stranded RNA-binding protein involved in RNA-mediated
CC post-transcriptional gene silencing (PTGS). Functions in the trans-
CC acting small interfering RNAs (ta-siRNAs) biogenesis by binding and
CC assisting DICER-LIKE 4 (DCL4). Required for DCL4 activity. Required for
CC the 21 nucleotide ta-siRNAs production of the TAS3 transcript in leaves
CC but not in flowers. Plays an important role in silencing RNA of both
CC DNA and RNA viruses. Involved with argonaute 7 (AGO7) and RDR6 in
CC turnip crinkle virus (TCV) silencing. May not be directly involved in
CC viral siRNA production. May stabilize the 21 nucleotide viral siRNAs
CC and deliver them to the RISC complex. Targeted by the viral silencing
CC suppressor (VSR) transactivator/viroplasmin (TAV) protein of the
CC cauliflower mosaic virus (CaMV) that inactivates DRB4 function in RNA
CC silencing. Probably not involved in the guide strand selection from RNA
CC duplexes. Involved in leaf morphology through its function in ta-siRNA-
CC mediated silencing. {ECO:0000269|PubMed:16682354,
CC ECO:0000269|PubMed:17221360, ECO:0000269|PubMed:18625233,
CC ECO:0000269|PubMed:18799732}.
CC -!- SUBUNIT: Heterodimer with DRB1 or DRB5. Interacts with DCL4 and
CC cauliflower mosaic virus (CaMV) transactivator/viroplasmin protein.
CC Interaction with CaMV transactivator/viroplasmin protein inhibits RNA
CC silencing ability of DRB4. {ECO:0000269|PubMed:15821876,
CC ECO:0000269|PubMed:17221360, ECO:0000269|PubMed:18615098}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15821876}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8H1D4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H1D4-2; Sequence=VSP_040614;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaf vasculature, shoot apical
CC meristem (SAM) and developing anthers. {ECO:0000269|PubMed:18625233}.
CC -!- DISRUPTION PHENOTYPE: Elongated and downwardly curled rosette leaves.
CC In old plants, rosette and cauline leaves and flowers change to red
CC color. Increased levels of ARF3 and ARF4 transcripts, targeted by TAS1
CC and TAS3, respectively. {ECO:0000269|PubMed:17221360,
CC ECO:0000269|PubMed:18625233}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB83130.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB455097; BAG69145.1; -; mRNA.
DR EMBL; AL162651; CAB83130.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80393.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80394.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80395.1; -; Genomic_DNA.
DR EMBL; AY074363; AAL67059.1; -; mRNA.
DR EMBL; AY150509; AAN13025.1; -; mRNA.
DR PIR; T48069; T48069.
DR RefSeq; NP_001154686.1; NM_001161214.2. [Q8H1D4-2]
DR RefSeq; NP_191839.2; NM_116145.4. [Q8H1D4-1]
DR RefSeq; NP_974480.1; NM_202751.1. [Q8H1D4-1]
DR PDB; 2N3F; NMR; -; A=1-153.
DR PDB; 2N3G; NMR; -; A=1-153.
DR PDB; 2N3H; NMR; -; A=1-153.
DR PDBsum; 2N3F; -.
DR PDBsum; 2N3G; -.
DR PDBsum; 2N3H; -.
DR AlphaFoldDB; Q8H1D4; -.
DR BMRB; Q8H1D4; -.
DR SMR; Q8H1D4; -.
DR BioGRID; 10769; 6.
DR IntAct; Q8H1D4; 2.
DR MINT; Q8H1D4; -.
DR STRING; 3702.AT3G62800.1; -.
DR iPTMnet; Q8H1D4; -.
DR PaxDb; Q8H1D4; -.
DR PRIDE; Q8H1D4; -.
DR ProteomicsDB; 241260; -. [Q8H1D4-1]
DR EnsemblPlants; AT3G62800.1; AT3G62800.1; AT3G62800. [Q8H1D4-1]
DR EnsemblPlants; AT3G62800.2; AT3G62800.2; AT3G62800. [Q8H1D4-1]
DR EnsemblPlants; AT3G62800.3; AT3G62800.3; AT3G62800. [Q8H1D4-2]
DR GeneID; 825455; -.
DR Gramene; AT3G62800.1; AT3G62800.1; AT3G62800. [Q8H1D4-1]
DR Gramene; AT3G62800.2; AT3G62800.2; AT3G62800. [Q8H1D4-1]
DR Gramene; AT3G62800.3; AT3G62800.3; AT3G62800. [Q8H1D4-2]
DR KEGG; ath:AT3G62800; -.
DR Araport; AT3G62800; -.
DR TAIR; locus:2081620; AT3G62800.
DR eggNOG; ENOG502QTBA; Eukaryota.
DR InParanoid; Q8H1D4; -.
DR OMA; HPTNDAT; -.
DR OrthoDB; 1311940at2759; -.
DR PhylomeDB; Q8H1D4; -.
DR PRO; PR:Q8H1D4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8H1D4; baseline and differential.
DR Genevisible; Q8H1D4; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:TAIR.
DR GO; GO:0051607; P:defense response to virus; IMP:CACAO.
DR GO; GO:0035196; P:miRNA processing; IMP:TAIR.
DR GO; GO:0009616; P:RNAi-mediated antiviral immune response; IMP:UniProtKB.
DR GO; GO:0010267; P:ta-siRNA processing; IMP:TAIR.
DR CDD; cd19907; DSRM_AtDRB-like_rpt1; 1.
DR CDD; cd19908; DSRM_AtDRB-like_rpt2; 1.
DR InterPro; IPR044450; AtDRB-like_DSRM_1.
DR InterPro; IPR044451; AtDRB-like_DSRM_2.
DR InterPro; IPR014720; dsRBD_dom.
DR Pfam; PF00035; dsrm; 2.
DR SMART; SM00358; DSRM; 2.
DR PROSITE; PS50137; DS_RBD; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Host-virus interaction; Nucleus;
KW Plant defense; Reference proteome; Repeat; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..355
FT /note="Double-stranded RNA-binding protein 4"
FT /id="PRO_0000404655"
FT DOMAIN 4..73
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 82..150
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 149..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 243..268
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040614"
FT CONFLICT 190
FT /note="M -> V (in Ref. 4; AAL67059)"
FT /evidence="ECO:0000305"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:2N3F"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2N3F"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2N3F"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2N3F"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2N3F"
FT HELIX 56..71
FT /evidence="ECO:0007829|PDB:2N3F"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2N3F"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2N3F"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:2N3F"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:2N3F"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2N3F"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:2N3F"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:2N3F"
FT HELIX 133..149
FT /evidence="ECO:0007829|PDB:2N3F"
SQ SEQUENCE 355 AA; 38416 MW; B97C224D28466772 CRC64;
MDHVYKGQLQ AYALQHNLEL PVYANEREGP PHAPRFRCNV TFCGQTFQSS EFFPTLKSAE
HAAAKIAVAS LTPQSPEGID VAYKNLLQEI AQKESSLLPF YATATSGPSH APTFTSTVEF
AGKVFSGEEA KTKKLAEMSA AKVAFMSIKN GNSNQTGSPT LPSERQEDVN SNVKSSPQEI
HSQPSSKVVM TPDTPSKGIK VNEDEFPDLH DAPASNAKEI NVALNEPENP TNDGTLSALT
TDGMKMNIAS SSLPIPHNPT NVITLNAPAA NGIKRNIAAC SSWMPQNPTN DGSETSSCVV
DESEKKKLIM GTGHLSIPTG QHVVCRPWNP EITLPQDAEM LFRDDKFIAY RLVKP
