ID DCL2_ARATH Reviewed; 1388 AA. AC Q3EBC8; Q1KL57; Q1KL58; Q9M9P8; DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 2. DT 24-JAN-2024, entry version 136. DE RecName: Full=Endoribonuclease Dicer homolog 2; DE EC=3.1.26.-; DE AltName: Full=Dicer-like protein 2; DE Short=AtDCL2; GN OrderedLocusNames=At3g03300; ORFNames=T17B22.1; 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] (ISOFORMS 1 AND 2). RX PubMed=16638569; DOI=10.1016/j.febslet.2006.03.072; RA Margis R., Fusaro A.F., Smith N.A., Curtin S.J., Watson J.M., RA Finnegan E.J., Waterhouse P.M.; RT "The evolution and diversification of Dicers in plants."; RL FEBS Lett. 580:2442-2450(2006). 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 SUBCELLULAR LOCATION. RX PubMed=15024409; DOI=10.1371/journal.pbio.0020104; RA Xie Z., Johansen L.K., Gustafson A.M., Kasschau K.D., Lellis A.D., RA Zilberman D., Jacobsen S.E., Carrington J.C.; RT "Genetic and functional diversification of small RNA pathways in plants."; RL PLoS Biol. 2:E104-E104(2004). RN [5] RP FUNCTION. RX PubMed=16040244; DOI=10.1016/j.cub.2005.07.024; RA Gasciolli V., Mallory A.C., Bartel D.P., Vaucheret H.; RT "Partially redundant functions of Arabidopsis DICER-like enzymes and a role RT for DCL4 in producing trans-acting siRNAs."; RL Curr. Biol. 15:1494-1500(2005). RN [6] RP FUNCTION. RX PubMed=16810317; DOI=10.1038/sj.emboj.7601217; RA Bouche N., Lauressergues D., Gasciolli V., Vaucheret H.; RT "An antagonistic function for Arabidopsis DCL2 in development and a new RT function for DCL4 in generating viral siRNAs."; RL EMBO J. 25:3347-3356(2006). RN [7] RP FUNCTION. RX PubMed=17586651; DOI=10.1105/tpc.106.047449; RA Diaz-Pendon J.A., Li F., Li W.X., Ding S.W.; RT "Suppression of antiviral silencing by cucumber mosaic virus 2b protein in RT Arabidopsis is associated with drastically reduced accumulation of three RT classes of viral small interfering RNAs."; RL Plant Cell 19:2053-2063(2007). RN [8] RP FUNCTION. RX PubMed=17592042; DOI=10.1261/rna.541307; RA Moissiard G., Parizotto E.A., Himber C., Voinnet O.; RT "Transitivity in Arabidopsis can be primed, requires the redundant action RT of the antiviral Dicer-like 4 and Dicer-like 2, and is compromised by RT viral-encoded suppressor proteins."; RL RNA 13:1268-1278(2007). RN [9] RP FUNCTION. RX PubMed=18353962; DOI=10.1128/jvi.00272-08; RA Donaire L., Barajas D., Martinez-Garcia B., Martinez-Priego L., Pagan I., RA Llave C.; RT "Structural and genetic requirements for the biogenesis of tobacco rattle RT virus-derived small interfering RNAs."; RL J. Virol. 82:5167-5177(2008). RN [10] RP FUNCTION. RX PubMed=18335032; DOI=10.1371/journal.pone.0001755; RA Mlotshwa S., Pruss G.J., Peragine A., Endres M.W., Li J., Chen X., RA Poethig R.S., Bowman L.H., Vance V.; RT "DICER-LIKE2 plays a primary role in transitive silencing of transgenes in RT Arabidopsis."; RL PLoS ONE 3:E1755-E1755(2008). RN [11] RP GENE FAMILY. RX PubMed=24265739; DOI=10.1371/journal.pone.0078982; RA Xu R., Zhang S., Huang J., Zheng C.; RT "Genome-wide comparative in silico analysis of the RNA helicase gene family RT in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza RT sativa."; RL PLoS ONE 8:E78982-E78982(2013). CC -!- FUNCTION: Ribonuclease (RNase) III involved in RNA-mediated post- CC transcriptional gene silencing (PTGS). Involved in the processing of CC natural small interfering RNAs (nat-siRNAs, derived from cis-natural CC antisense transcripts) by cleaving small dsRNAs into 24 nucleotide nat- CC siRNAs. Plays an essential role in transitive silencing of transgenes CC by processing secondary siRNAs. This pathway, which requires DCL4 and CC RDR6, amplifies silencing by using the target RNA as substrate to CC generate secondary siRNAs, providing an efficient mechanism for long- CC distance silencing. May participate with DCL3 in the production of 24 CC nucleotide repeat-associated siRNAs (ra-siRNAs) which derive from CC heterochromatin and DNA repeats such as transposons. Plays a role in CC antiviral RNA silencing. Involved in the production of viral siRNAs CC derived from the turnip crinkle virus (TCV) and tobacco rattle virus CC (TRV). Targeted by the viral silencing suppressor (VSR) protein 2b of CC the cucumber mosaic virus (CMV) that inactivates DCL2 function in RNA CC silencing. Does not seem to be involved in microRNAs (miRNAs) CC processing. {ECO:0000269|PubMed:16040244, ECO:0000269|PubMed:16810317, CC ECO:0000269|PubMed:17586651, ECO:0000269|PubMed:17592042, CC ECO:0000269|PubMed:18335032, ECO:0000269|PubMed:18353962}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- INTERACTION: CC Q3EBC8; O04492: DRB1; NbExp=2; IntAct=EBI-2464030, EBI-632620; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15024409}. Cytoplasm CC {ECO:0000269|PubMed:15024409}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q3EBC8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q3EBC8-2; Sequence=VSP_040615; CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00657}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF26098.1; Type=Erroneous gene model prediction; Note=The predicted gene At3g03300 has been split into 2 genes: At3g03300 and At3g03305.; Evidence={ECO:0000305}; CC Sequence=ABF19797.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ479970; ABF19797.1; ALT_INIT; mRNA. DR EMBL; DQ479971; ABF19798.1; -; mRNA. DR EMBL; AC012328; AAF26098.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002686; AEE73924.1; -; Genomic_DNA. DR EMBL; CP002686; AEE73925.1; -; Genomic_DNA. DR EMBL; CP002686; AEE73926.1; -; Genomic_DNA. DR RefSeq; NP_001078101.1; NM_001084632.1. [Q3EBC8-2] DR RefSeq; NP_001189798.1; NM_001202869.2. [Q3EBC8-1] DR RefSeq; NP_566199.4; NM_111200.5. [Q3EBC8-1] DR AlphaFoldDB; Q3EBC8; -. DR SMR; Q3EBC8; -. DR IntAct; Q3EBC8; 4. DR STRING; 3702.Q3EBC8; -. DR iPTMnet; Q3EBC8; -. DR PaxDb; 3702-AT3G03300-1; -. DR ProteomicsDB; 224607; -. [Q3EBC8-1] DR EnsemblPlants; AT3G03300.1; AT3G03300.1; AT3G03300. [Q3EBC8-1] DR EnsemblPlants; AT3G03300.2; AT3G03300.2; AT3G03300. [Q3EBC8-2] DR EnsemblPlants; AT3G03300.3; AT3G03300.3; AT3G03300. [Q3EBC8-1] DR GeneID; 821300; -. DR Gramene; AT3G03300.1; AT3G03300.1; AT3G03300. [Q3EBC8-1] DR Gramene; AT3G03300.2; AT3G03300.2; AT3G03300. [Q3EBC8-2] DR Gramene; AT3G03300.3; AT3G03300.3; AT3G03300. [Q3EBC8-1] DR KEGG; ath:AT3G03300; -. DR Araport; AT3G03300; -. DR TAIR; AT3G03300; DCL2. DR eggNOG; KOG0701; Eukaryota. DR HOGENOM; CLU_000907_4_4_1; -. DR InParanoid; Q3EBC8; -. DR OMA; YHVNRMC; -. DR OrthoDB; 342391at2759; -. DR PhylomeDB; Q3EBC8; -. DR PRO; PR:Q3EBC8; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q3EBC8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0051607; P:defense response to virus; IMP:TAIR. DR GO; GO:0051214; P:RNAi-mediated antiviral immunity against RNA virus; IGI:TAIR. DR GO; GO:0010267; P:ta-siRNA processing; IMP:TAIR. DR CDD; cd18034; DEXHc_dicer; 1. DR CDD; cd02844; PAZ_CAF_like; 1. DR CDD; cd00593; RIBOc; 2. DR CDD; cd18802; SF2_C_dicer; 1. DR Gene3D; 3.30.160.20; -; 1. DR Gene3D; 3.30.160.380; Dicer dimerisation domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR Gene3D; 2.170.260.10; paz domain; 1. DR Gene3D; 1.10.1520.10; Ribonuclease III domain; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR038248; Dicer_dimer_sf. DR InterPro; IPR005034; Dicer_dimerisation_dom. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003100; PAZ_dom. DR InterPro; IPR036085; PAZ_dom_sf. DR InterPro; IPR000999; RNase_III_dom. DR InterPro; IPR036389; RNase_III_sf. DR PANTHER; PTHR14950; DICER-RELATED; 1. DR PANTHER; PTHR14950:SF70; ENDORIBONUCLEASE DICER HOMOLOG 2; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF03368; Dicer_dimer; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF02170; PAZ; 1. DR Pfam; PF00636; Ribonuclease_3; 2. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00358; DSRM; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00949; PAZ; 1. DR SMART; SM00535; RIBOc; 2. DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF101690; PAZ domain; 1. DR SUPFAM; SSF69065; RNase III domain-like; 2. DR PROSITE; PS51327; DICER_DSRBF; 1. DR PROSITE; PS50137; DS_RBD; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50821; PAZ; 1. DR PROSITE; PS00517; RNASE_3_1; 1. DR PROSITE; PS50142; RNASE_3_2; 2. DR Genevisible; Q3EBC8; AT. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cytoplasm; Endonuclease; Helicase; KW Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease; KW Nucleotide-binding; Nucleus; Plant defense; Reference proteome; Repeat; KW RNA-binding; RNA-mediated gene silencing. FT CHAIN 1..1388 FT /note="Endoribonuclease Dicer homolog 2" FT /id="PRO_0000404660" FT DOMAIN 31..210 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 380..544 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT DOMAIN 559..645 FT /note="Dicer dsRNA-binding fold" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657" FT DOMAIN 805..935 FT /note="PAZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142" FT DOMAIN 962..1113 FT /note="RNase III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177" FT DOMAIN 1149..1296 FT /note="RNase III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177" FT DOMAIN 1315..1384 FT /note="DRBM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266" FT MOTIF 152..155 FT /note="DECH box" FT BINDING 44..51 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT BINDING 1188 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 1282 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 1285 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT SITE 1278 FT /note="Important for activity" FT /evidence="ECO:0000250" FT VAR_SEQ 1..83 FT /note="MTMDADAMETETTDQVSASPLHFARSYQVEALEKAIKQNTIVFLETGSGKTL FT IAIMLLRSYAYLFRKPSPCFCVFLVPQVVLV -> MLLCLLGSSSGSCHSGIGVRIGVV FT DKGIHQYTDLSFVLQFLHYYTCSFSKFRNFSVTFSIISAFFLVCF (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:16638569" FT /id="VSP_040615" FT CONFLICT 511 FT /note="L -> S (in Ref. 1; ABF19797/ABF19798)" FT /evidence="ECO:0000305" FT CONFLICT 693 FT /note="F -> L (in Ref. 1; ABF19797/ABF19798)" FT /evidence="ECO:0000305" FT CONFLICT 738 FT /note="Q -> R (in Ref. 1; ABF19797/ABF19798)" FT /evidence="ECO:0000305" FT CONFLICT 1130 FT /note="F -> L (in Ref. 1; ABF19797/ABF19798)" FT /evidence="ECO:0000305" SQ SEQUENCE 1388 AA; 156865 MW; 385D5A28E048B10D CRC64; MTMDADAMET ETTDQVSASP LHFARSYQVE ALEKAIKQNT IVFLETGSGK TLIAIMLLRS YAYLFRKPSP CFCVFLVPQV VLVTQQAEAL KMHTDLKVGM YWGDMGVDFW DSSTWKQEVD KYEVLVMTPA ILLDALRHSF LSLSMIKVLI VDECHHAGGK HPYACIMREF YHKELNSGTS NVPRIFGMTA SLVKTKGENL DSYWKKIHEL ETLMNSKVYT CENESVLAGF VPFSTPSFKY YQHIKIPSPK RASLVEKLER LTIKHRLSLG TLDLNSSTVD SVEKRLLRIS STLTYCLDDL GILLAQKAAQ SLSASQNDSF LWGELNMFSV ALVKKFCSDA SQEFLAEIPQ GLNWSVANIN GNAEAGLLTL KTVCLIETLL GYSSLENIRC IIFVDRVITA IVLESLLAEI LPNCNNWKTK YVAGNNSGLQ NQTRKKQNEI VEDFRRGLVN IIVATSILEE GLDVQSCNLV IRFDPASNIC SFIQSRGRAR MQNSDYLMMV ESGDLLTQSR LMKYLSGGKR MREESLDHSL VPCPPLPDDS DEPLFRVEST GATVTLSSSV SLIYHYCSRL PSDEYFKPAP RFDVNKDQGS CTLYLPKSCP VKEVKAEANN KVLKQAVCLK ACIQLHKVGA LSDHLVPDMV VAETVSQKLE KIQYNTEQPC YFPPELVSQF SAQPETTYHF YLIRMKPNSP RNFHLNDVLL GTRVVLEDDI GNTSFRLEDH RGTIAVTLSY VGAFHLTQEE VLFCRRFQIT LFRVLLDHSV ENLMEALNGL HLRDGVALDY LLVPSTHSHE TSLIDWEVIR SVNLTSHEVL EKHENCSTNG ASRILHTKDG LFCTCVVQNA LVYTPHNGYV YCTKGVLNNL NGNSLLTKRN SGDQTYIEYY EERHGIQLNF VDEPLLNGRH IFTLHSYLHM AKKKKEKEHD REFVELPPEL CHVILSPISV DMIYSYTFIP SVMQRIESLL IAYNLKKSIP KVNIPTIKVL EAITTKKCED QFHLESLETL GDSFLKYAVC QQLFQHCHTH HEGLLSTKKD GMISNVMLCQ FGCQQKLQGF IRDECFEPKG WMVPGQSSAA YSLVNDTLPE SRNIYVASRR NLKRKSVADV VESLIGAYLS EGGELAALMF MNWVGIKVDF TTTKIQRDSP IQAEKLVNVG YMESLLNYSF EDKSLLVEAL THGSYMMPEI PRCYQRLEFL GDSVLDYLIT KHLYDKYPCL SPGLLTDMRS ASVNNECYAL VAVKANLHKH ILYASHHLHK HISRTVSEFE QSSLQSTFGW ESDISFPKVL GDVIESLAGA IFVDSGYNKE VVFASIKPLL GCMITPETVK LHPVRELTEL CQKWQFELSK AKDFDSFTVE VKAKEMSFAH TAKASDKKMA KKLAYKEVLN LLKNSLDY //