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Database: UniProt
Entry: Q9LXW7
LinkDB: Q9LXW7
Original site: Q9LXW7 
ID   DCL3_ARATH              Reviewed;        1580 AA.
AC   Q9LXW7;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   16-OCT-2019, entry version 125.
DE   RecName: Full=Endoribonuclease Dicer homolog 3;
DE            EC=3.1.26.-;
DE   AltName: Full=Dicer-like protein 3;
DE            Short=AtDCL3;
GN   Name=DCL3; OrderedLocusNames=At3g43920; ORFNames=T15B3.60;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 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.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   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.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   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
RT   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
RT   reference 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
RT   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
RT   role for DCL4 in producing trans-acting siRNAs.";
RL   Curr. Biol. 15:1494-1500(2005).
RN   [6]
RP   INTERACTION WITH DRB2 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.,
RA   Koiwa H., 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   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16839878; DOI=10.1016/j.cell.2006.05.031;
RA   Pontes O., Li C.F., Nunes P.C., Haag J., Ream T., Vitins A.,
RA   Jacobsen S.E., Pikaard C.S.;
RT   "The Arabidopsis chromatin-modifying nuclear siRNA pathway involves a
RT   nucleolar RNA processing center.";
RL   Cell 126:79-92(2006).
RN   [8]
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
RT   new function for DCL4 in generating viral siRNAs.";
RL   EMBO J. 25:3347-3356(2006).
RN   [9]
RP   FUNCTION.
RX   PubMed=17579240; DOI=10.1534/genetics.107.070649;
RA   Schmitz R.J., Hong L., Fitzpatrick K.E., Amasino R.M.;
RT   "DICER-LIKE 1 and DICER-LIKE 3 redundantly act to promote flowering
RT   via repression of FLOWERING LOCUS C in Arabidopsis thaliana.";
RL   Genetics 176:1359-1362(2007).
RN   [10]
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
RT   protein in Arabidopsis is associated with drastically reduced
RT   accumulation of three classes of viral small interfering RNAs.";
RL   Plant Cell 19:2053-2063(2007).
RN   [11]
RP   FUNCTION.
RX   PubMed=18353962; DOI=10.1128/jvi.00272-08;
RA   Donaire L., Barajas D., Martinez-Garcia B., Martinez-Priego L.,
RA   Pagan I., Llave C.;
RT   "Structural and genetic requirements for the biogenesis of tobacco
RT   rattle virus-derived small interfering RNAs.";
RL   J. Virol. 82:5167-5177(2008).
RN   [12]
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
RT   family in Zea mays and Glycine max: a comparison with Arabidopsis and
RT   Oryza 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
CC       of repeat-associated small interfering RNAs (ra-siRNAs, derived
CC       from heterochromatin and DNA repeats such as transposons) by
CC       cleaving small dsRNAs into 24 nucleotide ra-siRNAs. Plays a role
CC       in antiviral RNA silencing. Involved in the production of viral
CC       siRNAs derived from the cabbage leaf curl virus (CaLCuV) and
CC       tobacco rattle virus (TRV). Targeted by the viral silencing
CC       suppressor (VSR) protein 2b of the cucumber mosaic virus (CMV)
CC       that inactivates DCL3 function in RNA silencing. Acts redundantly
CC       with DICER-LIKE 1 (DCL1) to promote flowering via repression of
CC       FLOWERING LOCUS C (FLC). Does not seem to be involved in microRNAs
CC       (miRNAs) processing. {ECO:0000269|PubMed:16040244,
CC       ECO:0000269|PubMed:16810317, ECO:0000269|PubMed:17579240,
CC       ECO:0000269|PubMed:17586651, 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   -!- SUBUNIT: Interacts with DRB2 and DRB5.
CC       {ECO:0000269|PubMed:15821876}.
CC   -!- INTERACTION:
CC       Q9LJF5:DRB3; NbExp=2; IntAct=EBI-632737, EBI-10815073;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000269|PubMed:15024409, ECO:0000269|PubMed:16839878}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9LXW7-1; Sequence=Displayed;
CC         Note=Derived from EST data. No experimental confirmation
CC         available.;
CC       Name=2;
CC         IsoId=Q9LXW7-2; Sequence=VSP_040616, VSP_040617;
CC   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC       {ECO:0000305}.
DR   EMBL; DQ479972; ABF19799.1; -; mRNA.
DR   EMBL; AL163975; CAB88120.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77842.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77843.1; -; Genomic_DNA.
DR   PIR; T48946; T48946.
DR   RefSeq; NP_001154662.2; NM_001161190.2. [Q9LXW7-1]
DR   RefSeq; NP_189978.1; NM_114260.1. [Q9LXW7-2]
DR   BioGrid; 8828; 5.
DR   IntAct; Q9LXW7; 3.
DR   MINT; Q9LXW7; -.
DR   STRING; 3702.AT3G43920.2; -.
DR   PaxDb; Q9LXW7; -.
DR   PRIDE; Q9LXW7; -.
DR   EnsemblPlants; AT3G43920.1; AT3G43920.1; AT3G43920. [Q9LXW7-2]
DR   EnsemblPlants; AT3G43920.2; AT3G43920.2; AT3G43920. [Q9LXW7-1]
DR   GeneID; 823508; -.
DR   Gramene; AT3G43920.1; AT3G43920.1; AT3G43920. [Q9LXW7-2]
DR   Gramene; AT3G43920.2; AT3G43920.2; AT3G43920. [Q9LXW7-1]
DR   KEGG; ath:AT3G43920; -.
DR   Araport; AT3G43920; -.
DR   TAIR; locus:2097139; AT3G43920.
DR   eggNOG; KOG0701; Eukaryota.
DR   eggNOG; COG0571; LUCA.
DR   eggNOG; COG1111; LUCA.
DR   HOGENOM; HOG000030250; -.
DR   InParanoid; Q9LXW7; -.
DR   KO; K11592; -.
DR   OrthoDB; 1337630at2759; -.
DR   PhylomeDB; Q9LXW7; -.
DR   PRO; PR:Q9LXW7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LXW7; baseline and differential.
DR   Genevisible; Q9LXW7; AT.
DR   GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:TAIR.
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:0010216; P:maintenance of DNA methylation; IMP:TAIR.
DR   GO; GO:0030422; P:production of siRNA involved in RNA interference; IMP:TAIR.
DR   GO; GO:0010267; P:production of ta-siRNAs involved in RNA interference; IMP:TAIR.
DR   GO; GO:0051214; P:RNA virus induced gene silencing; IGI:TAIR.
DR   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 1.10.1520.10; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_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   Pfam; PF00270; DEAD; 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; SM00949; PAZ; 1.
DR   SMART; SM00535; RIBOc; 2.
DR   SUPFAM; SSF101690; SSF101690; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF69065; SSF69065; 2.
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.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Complete proteome; Endonuclease;
KW   Helicase; Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease;
KW   Nucleotide-binding; Nucleus; Plant defense; Reference proteome;
KW   Repeat; RNA-binding; RNA-mediated gene silencing.
FT   CHAIN         1   1580       Endoribonuclease Dicer homolog 3.
FT                                /FTId=PRO_0000404661.
FT   DOMAIN       51    223       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      394    562       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      821    934       PAZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00142}.
FT   DOMAIN      985   1157       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1198   1340       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   NP_BIND      64     71       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       170    173       DECH box.
FT   COMPBIAS    622    630       Poly-Ser.
FT   METAL      1234   1234       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1326   1326       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1329   1329       Magnesium or manganese. {ECO:0000250}.
FT   SITE       1322   1322       Important for activity. {ECO:0000250}.
FT   VAR_SEQ     101    103       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16638569}.
FT                                /FTId=VSP_040616.
FT   VAR_SEQ     186    231       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16638569}.
FT                                /FTId=VSP_040617.
SQ   SEQUENCE   1580 AA;  177425 MW;  EA71D47BF3C29FA5 CRC64;
     MHSSLEPEKM EEGGGSNSLK RKFSEIDGDQ NLDSVSSPMM TDSNGSYELK VYEVAKNRNI
     IAVLGTGIDK SEITKRLIKA MGSSDTDKRL IIFLAPTVNL VKQQCCEIRA LVNLKVEEYF
     GAKGVDKWTS QRWDEEFSKH DVLVMTPQIL LDVLRSAFLK LEMVCLLIID ECHHTTGNHP
     YAKLMKEFYH ESTSKPKIFG LTASAVIRKG IVSSPSNYAA QVSELERLMD SKIFNPEERE
     GVEKFATTVK EGPILYNPSP SCSLELKEKL ETSHLKFDAS LRRLQELGKD SFLNMDNKFE
     TYQKRLSIDY REILHCLDNL GLICAHLAAE VCLEKISDTK EESETYKECS MVCKEFLEDI
     LSTIGVYLPQ DDKSLVDLQQ NHLSAVISGH VSPKLKELFH LLDSFRGDKQ KQCLILVERI
     ITAKVIERFV KKEASLAYLN VLYLTENNPS TNVSAQKMQI EIPDLFQHGK VNLLFITDVV
     EEGFQVPDCS CMVCFDLPKT MCSYSQSQKH AKQSNSKSIM FLERGNPKQR DHLHDLMRRE
     VLIQDPEAPN LKSCPPPVKN GHGVKEIGSM VIPDSNITVS EEAASTQTMS DPPSRNEQLP
     PCKKLRLDNN LLQSNGKEKV ASSKSKSSSS AAGSKKRKEL HGTTCANALS GTWGENIDGA
     TFQAYKFDFC CNISGEVYSS FSLLLESTLA EDVGKVEMDL YLVRKLVKAS VSPCGQIRLS
     QEELVKAKYF QQFFFNGMFG KLFVGSKSQG TKREFLLQTD TSSLWHPAFM FLLLPVETND
     LASSATIDWS AINSCASIVE FLKKNSLLDL RDSDGNQCNT SSGQEVLLDD KMEETNLIHF
     ANASSDKNSL EELVVIAIHT GRIYSIVEAV SDSSAMSPFE VDASSGYATY AEYFNKKYGI
     VLAHPNQPLM KLKQSHHAHN LLVDFNEEMV VKTEPKAGNV RKRKPNIHAH LPPELLARID
     VPRAVLKSIY LLPSVMHRLE SLMLASQLRE EIDCSIDNFS ISSTSILEAV TTLTCPESFS
     MERLELLGDS VLKYVASCHL FLKYPDKDEG QLSRQRQSII SNSNLHRLTT SRKLQGYIRN
     GAFEPRRWTA PGQFSLFPVP CKCGIDTREV PLDPKFFTEN MTIKIGKSCD MGHRWVVSKS
     VSDCAEALIG AYYVSGGLSA SLHMMKWLGI DVDFDPNLVV EAINRVSLRC YIPKEDELIE
     LERKIQHEFS AKFLLKEAIT HSSLRESYSY ERLEFLGDSV LDFLITRHLF NTYEQTGPGE
     MTDLRSACVN NENFAQVAVK NNLHTHLQRC ATVLETQIND YLMSFQKPDE TGRSIPSIQG
     PKALGDVVES IAGALLIDTR LDLDQVWRVF EPLLSPLVTP DKLQLPPYRE LNELCDSLGY
     FFRVKCSNDG VKAQATIQLQ LDDVLLTGDG SEQTNKLALG KAASHLLTQL EKRNISRKTS
     LGDNQSSMDV NLACNHSDRE TLTSETTEIQ SIVIPFIGPI NMKKGGPRGT LHEFCKKHLW
     PMPTFDTSEE KSRTPFEFID GGEKRTSFSS FTSTITLRIP NREAVMYAGE ARPDKKSSFD
     SAVVELLYEL ERRKIVIIQK
//
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