AGO4_ARATH
ID AGO4_ARATH Reviewed; 924 AA.
AC Q9ZVD5; Q93VG2;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein argonaute 4 {ECO:0000303|PubMed:12522258, ECO:0000303|PubMed:28229965};
DE Short=AtAGO4 {ECO:0000303|PubMed:12522258, ECO:0000303|PubMed:28229965};
DE AltName: Full=Protein OVEREXPRESSOR OF CATIONIC PEROXIDASE 11;
GN Name=AGO4 {ECO:0000303|PubMed:12522258, ECO:0000303|PubMed:28229965};
GN Synonyms=OCP11;
GN OrderedLocusNames=At2g27040 {ECO:0000312|Araport:AT2G27040};
GN ORFNames=T20P8.9 {ECO:0000312|EMBL:AAC77862.2};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12522258; DOI=10.1126/science.1079695;
RA Zilberman D., Cao X., Jacobsen S.E.;
RT "ARGONAUTE4 control of locus-specific siRNA accumulation and DNA and
RT histone methylation.";
RL Science 299:716-719(2003).
RN [5]
RP FUNCTION.
RX PubMed=14988555; DOI=10.1126/science.1095989;
RA Chan S.W., Zilberman D., Xie Z., Johansen L.K., Carrington J.C.,
RA Jacobsen S.E.;
RT "RNA silencing genes control de novo DNA methylation.";
RL Science 303:1336-1336(2004).
RN [6]
RP FUNCTION.
RX PubMed=15242620; DOI=10.1016/j.cub.2004.06.055;
RA Zilberman D., Cao X., Johansen L.K., Xie Z., Carrington J.C.,
RA Jacobsen S.E.;
RT "Role of Arabidopsis ARGONAUTE4 in RNA-directed DNA methylation triggered
RT by inverted repeats.";
RL Curr. Biol. 14:1214-1220(2004).
RN [7]
RP FUNCTION, AND 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., Jacobsen S.E.,
RA 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, SUBCELLULAR LOCATION, AND INTERACTION WITH NRPE1.
RX PubMed=16839879; DOI=10.1016/j.cell.2006.05.032;
RA Li C.F., Pontes O., El-Shami M., Henderson I.R., Bernatavichute Y.V.,
RA Chan S.W.-L., Lagrange T., Pikaard C.S., Jacobsen S.E.;
RT "An ARGONAUTE4-containing nuclear processing center colocalized with Cajal
RT bodies in Arabidopsis thaliana.";
RL Cell 126:93-106(2006).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF ASP-660; ASP-742 AND HIS-874.
RX PubMed=16998468; DOI=10.1038/nature05198;
RA Qi Y., He X., Wang X.J., Kohany O., Jurka J., Hannon G.J.;
RT "Distinct catalytic and non-catalytic roles of ARGONAUTE4 in RNA-directed
RT DNA methylation.";
RL Nature 443:1008-1012(2006).
RN [10]
RP FUNCTION.
RX PubMed=17869110; DOI=10.1016/j.cub.2007.08.039;
RA Baumberger N., Tsai C.-H., Lie M., Havecker E., Baulcombe D.C.;
RT "The Polerovirus silencing suppressor P0 targets ARGONAUTE proteins for
RT degradation.";
RL Curr. Biol. 17:1609-1614(2007).
RN [11]
RP FUNCTION, AND INTERACTION WITH NRPE1.
RX PubMed=17938239; DOI=10.1101/gad.451207;
RA El-Shami M., Pontier D., Lahmy S., Braun L., Picart C., Vega D.,
RA Hakimi M.A., Jacobsen S.E., Cooke R., Lagrange T.;
RT "Reiterated WG/GW motifs form functionally and evolutionarily conserved
RT ARGONAUTE-binding platforms in RNAi-related components.";
RL Genes Dev. 21:2539-2544(2007).
RN [12]
RP FUNCTION, MUTAGENESIS OF GLU-641, AND DISRUPTION PHENOTYPE.
RX PubMed=17993621; DOI=10.1105/tpc.107.054494;
RA Agorio A., Vera P.;
RT "ARGONAUTE4 is required for resistance to Pseudomonas syringae in
RT Arabidopsis.";
RL Plant Cell 19:3778-3790(2007).
RN [13]
RP FUNCTION.
RX PubMed=18342361; DOI=10.1016/j.cell.2008.02.034;
RA Mi S., Cai T., Hu Y., Chen Y., Hodges E., Ni F., Wu L., Li S., Zhou H.,
RA Long C., Chen S., Hannon G.J., Qi Y.;
RT "Sorting of small RNAs into Arabidopsis argonaute complexes is directed by
RT the 5' terminal nucleotide.";
RL Cell 133:116-127(2008).
RN [14]
RP FUNCTION.
RX PubMed=18596098; DOI=10.1128/jvi.00719-08;
RA Raja P., Sanville B.C., Buchmann R.C., Bisaro D.M.;
RT "Viral genome methylation as an epigenetic defense against geminiviruses.";
RL J. Virol. 82:8997-9007(2008).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=18266474; DOI=10.1371/journal.pgen.0040027;
RA Li C.F., Henderson I.R., Song L., Fedoroff N., Lagrange T., Jacobsen S.E.;
RT "Dynamic regulation of ARGONAUTE4 within multiple nuclear bodies in
RT Arabidopsis thaliana.";
RL PLoS Genet. 4:E27-E27(2008).
RN [16]
RP INTERACTION WITH RDM3, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. C24;
RX PubMed=19410546; DOI=10.1016/j.cell.2009.04.028;
RA He X.-J., Hsu Y.-F., Zhu S., Wierzbicki A.T., Pontes O., Pikaard C.S.,
RA Liu H.-L., Wang C.-S., Jin H., Zhu J.-K.;
RT "An effector of RNA-directed DNA methylation in arabidopsis is an ARGONAUTE
RT 4- and RNA-binding protein.";
RL Cell 137:498-508(2009).
RN [17]
RP INTERACTION WITH RDM3.
RC STRAIN=cv. Columbia;
RX PubMed=19343051; DOI=10.1038/embor.2009.31;
RA Bies-Etheve N., Pontier D., Lahmy S., Picart C., Vega D., Cooke R.,
RA Lagrange T.;
RT "RNA-directed DNA methylation requires an AGO4-interacting member of the
RT SPT5 elongation factor family.";
RL EMBO Rep. 10:649-654(2009).
RN [18]
RP FUNCTION, AND INTERACTION WITH NRPE1.
RX PubMed=19377477; DOI=10.1038/ng.365;
RA Wierzbicki A.T., Ream T.S., Haag J.R., Pikaard C.S.;
RT "RNA polymerase V transcription guides ARGONAUTE4 to chromatin.";
RL Nat. Genet. 41:630-634(2009).
RN [19]
RP INTERACTION WITH TURNIP CRINKLE VIRUS CAPSID PROTEIN P38.
RX PubMed=20439431; DOI=10.1101/gad.1908710;
RA Azevedo J., Garcia D., Pontier D., Ohnesorge S., Yu A., Garcia S.,
RA Braun L., Bergdoll M., Hakimi M.A., Lagrange T., Voinnet O.;
RT "Argonaute quenching and global changes in Dicer homeostasis caused by a
RT pathogen-encoded GW repeat protein.";
RL Genes Dev. 24:904-915(2010).
RN [20]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20173091; DOI=10.1105/tpc.109.072199;
RA Havecker E.R., Wallbridge L.M., Hardcastle T.J., Bush M.S., Kelly K.A.,
RA Dunn R.M., Schwach F., Doonan J.H., Baulcombe D.C.;
RT "The Arabidopsis RNA-directed DNA methylation argonautes functionally
RT diverge based on their expression and interaction with target loci.";
RL Plant Cell 22:321-334(2010).
RN [21]
RP FUNCTION, INTERACTION WITH CHROMATIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21738482; DOI=10.1371/journal.pgen.1002120;
RA Rowley M.J., Avrutsky M.I., Sifuentes C.J., Pereira L., Wierzbicki A.T.;
RT "Independent chromatin binding of ARGONAUTE4 and SPT5L/KTF1 mediates
RT transcriptional gene silencing.";
RL PLoS Genet. 7:E1002120-E1002120(2011).
RN [22]
RP INTERACTION WITH SDE3.
RX PubMed=22940249; DOI=10.1016/j.molcel.2012.07.028;
RA Garcia D., Garcia S., Pontier D., Marchais A., Renou J.P., Lagrange T.,
RA Voinnet O.;
RT "Ago hook and RNA helicase motifs underpin dual roles for SDE3 in antiviral
RT defense and silencing of nonconserved intergenic regions.";
RL Mol. Cell 48:109-120(2012).
RN [23]
RP INTERACTION WITH MBD6.
RX PubMed=28229965; DOI=10.1007/s12038-016-9658-1;
RA Parida A.P., Sharma A., Sharma A.K.;
RT "AtMBD6, a methyl CpG binding domain protein, maintains gene silencing in
RT Arabidopsis by interacting with RNA binding proteins.";
RL J. Biosci. 42:57-68(2017).
CC -!- FUNCTION: Together with RDM3, required for transcriptional gene
CC silencing (TGS) by DNA methylation and repressive histone modifications
CC (H3K9me2) of several chromatin loci (PubMed:21738482). Component of the
CC RISC complex that associate with the small interfering RNA (siRNA)
CC pathway involved in direct cytosine methylation at endogenous DNA
CC repeats. Forms a AGO4/NRPE1/siRNA complex in cajal body, facilitating
CC its function in RNA-directed gene silencing of target loci. Required
CC for CpNpG and asymmetric DNA methylation as well as histone H3 'Lys-9'
CC methylation (H3K9me) at SUP and SN1 loci. May be not required for CpG
CC methylation. Required for the production and maintenance of
CC retrotransposon SN1 and Copia and ribosomal 5S 25 nucleotide siRNAs
CC specialized in gene silencing at chromatin level. Involved in de novo
CC methylation of FWA gene and required for the maintenance of RNA-
CC directed DNA methylation (RdDM) triggered by inverted repeat
CC transgenes. Interacts with miRNA miR390 and miR172, targeting
CC respectively TAS3 and AP2 mRNAs, and mediates cleavage of miRNA
CC targets. Associates mainly with small RNAs of 24 nucleotide in length
CC and preferentially recruits small RNAs with a 5' terminal adenosine.
CC Targeted by the turnip yellows virus (TuYV) protein P0 (via F-box-like
CC domain) for probable proteasome degradation and thereby inactivating
CC AGO4 function in RNA silencing. Required for resistance to the
CC bacterial pathogen P.syringae. Works independently of the RdDM pathway
CC in mediating resistance to P.syringae. RdDM is involved in viral genome
CC methylation as an epigenetic defense against geminiviruses
CC (PubMed:12522258, PubMed:14988555, PubMed:15242620, PubMed:16839878,
CC PubMed:16839879, PubMed:16998468, PubMed:17869110, PubMed:17938239,
CC PubMed:17993621, PubMed:18342361, PubMed:18596098, PubMed:19377477,
CC PubMed:20173091). {ECO:0000269|PubMed:12522258,
CC ECO:0000269|PubMed:14988555, ECO:0000269|PubMed:15242620,
CC ECO:0000269|PubMed:16839878, ECO:0000269|PubMed:16839879,
CC ECO:0000269|PubMed:16998468, ECO:0000269|PubMed:17869110,
CC ECO:0000269|PubMed:17938239, ECO:0000269|PubMed:17993621,
CC ECO:0000269|PubMed:18342361, ECO:0000269|PubMed:18596098,
CC ECO:0000269|PubMed:19377477, ECO:0000269|PubMed:20173091,
CC ECO:0000269|PubMed:21738482}.
CC -!- SUBUNIT: Interacts with NRPE1 (via C-terminus). Binding to NRPE1 is
CC required for its function in RdDM. Interacts with turnip crinkle virus
CC (TCV) capsid protein P38; this interaction inhibits probably RNA
CC silencing ability of AGO4. Interacts with SDE3 (PubMed:16839879,
CC PubMed:17938239, PubMed:19377477, PubMed:20439431, PubMed:22940249).
CC Binds to RDM3 (PubMed:19410546, PubMed:19343051). Binds chromatin at
CC loci subject to transcriptional silencing (PubMed:21738482). Interacts
CC with MBD6 (PubMed:28229965). {ECO:0000269|PubMed:16839879,
CC ECO:0000269|PubMed:17938239, ECO:0000269|PubMed:19343051,
CC ECO:0000269|PubMed:19377477, ECO:0000269|PubMed:19410546,
CC ECO:0000269|PubMed:20439431, ECO:0000269|PubMed:21738482,
CC ECO:0000269|PubMed:22940249, ECO:0000269|PubMed:28229965}.
CC -!- INTERACTION:
CC Q9ZVD5; Q9LJF5: DRB3; NbExp=2; IntAct=EBI-2352199, EBI-10815073;
CC Q9ZVD5; Q9M548: DRM2; NbExp=2; IntAct=EBI-2352199, EBI-6923904;
CC Q9ZVD5; Q5D869: NRPE1; NbExp=3; IntAct=EBI-2352199, EBI-2352263;
CC Q9ZVD5; Q9LUJ3: RDM1; NbExp=2; IntAct=EBI-2352199, EBI-15850569;
CC Q9ZVD5; F4JW79: RDM3; NbExp=5; IntAct=EBI-2352199, EBI-2352225;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16839878}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:19410546}. Nucleus, Cajal body
CC {ECO:0000269|PubMed:16839879, ECO:0000269|PubMed:18266474}. Note=Also
CC located in AB-bodies that are distincts from the Cajal bodies and
CC immediately adjacent to the condensed 45S ribosomal DNA (rDNA) loci
CC (PubMed:18266474). Colocalizes with AGO4 and polymerase V in the
CC nucleoplasm (PubMed:19410546). {ECO:0000269|PubMed:18266474,
CC ECO:0000269|PubMed:19410546}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos, mature leaves, vascular
CC tissue of the sepals, stamens and stigma, at the tip of the style and
CC siliques. {ECO:0000269|PubMed:20173091}.
CC -!- DISRUPTION PHENOTYPE: Decreased DNA cytosine methylation at CpNpG and
CC asymmetric positions at different DNA loci corresponding to
CC retroelements, transposons and repetitive DNA sequences
CC (PubMed:12522258, PubMed:17993621, PubMed:21738482). Reduced H3K9me2 at
CC IGN5 and IGN26 loci (PubMed:21738482). {ECO:0000269|PubMed:12522258,
CC ECO:0000269|PubMed:17993621, ECO:0000269|PubMed:21738482}.
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000305}.
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DR EMBL; AC005623; AAC77862.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07928.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07929.1; -; Genomic_DNA.
DR EMBL; AY035081; AAK59586.1; -; mRNA.
DR EMBL; AY051033; AAK93710.1; -; mRNA.
DR PIR; A84668; A84668.
DR RefSeq; NP_001189613.1; NM_001202684.1.
DR RefSeq; NP_565633.1; NM_128262.4.
DR AlphaFoldDB; Q9ZVD5; -.
DR SMR; Q9ZVD5; -.
DR BioGRID; 2598; 4.
DR DIP; DIP-53402N; -.
DR IntAct; Q9ZVD5; 6.
DR MINT; Q9ZVD5; -.
DR STRING; 3702.AT2G27040.2; -.
DR MoonProt; Q9ZVD5; -.
DR iPTMnet; Q9ZVD5; -.
DR PaxDb; Q9ZVD5; -.
DR PRIDE; Q9ZVD5; -.
DR ProteomicsDB; 244704; -.
DR EnsemblPlants; AT2G27040.1; AT2G27040.1; AT2G27040.
DR EnsemblPlants; AT2G27040.2; AT2G27040.2; AT2G27040.
DR GeneID; 817246; -.
DR Gramene; AT2G27040.1; AT2G27040.1; AT2G27040.
DR Gramene; AT2G27040.2; AT2G27040.2; AT2G27040.
DR KEGG; ath:AT2G27040; -.
DR Araport; AT2G27040; -.
DR TAIR; locus:2059258; AT2G27040.
DR eggNOG; KOG1041; Eukaryota.
DR HOGENOM; CLU_004544_2_0_1; -.
DR InParanoid; Q9ZVD5; -.
DR OMA; PTNQEYK; -.
DR OrthoDB; 159407at2759; -.
DR PhylomeDB; Q9ZVD5; -.
DR PRO; PR:Q9ZVD5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVD5; baseline and differential.
DR Genevisible; Q9ZVD5; AT.
DR GO; GO:0015030; C:Cajal body; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000791; C:euchromatin; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IMP:CAFA.
DR GO; GO:0035198; F:miRNA binding; IDA:CAFA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0035197; F:siRNA binding; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0051607; P:defense response to virus; IDA:TAIR.
DR GO; GO:0006306; P:DNA methylation; IMP:TAIR.
DR GO; GO:0080188; P:gene silencing by RNA-directed DNA methylation; IMP:CAFA.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:UniProtKB.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; TAS:TAIR.
DR GO; GO:0051567; P:histone H3-K9 methylation; IMP:TAIR.
DR GO; GO:0019048; P:modulation by virus of host process; IMP:TAIR.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0030422; P:siRNA processing; IMP:CAFA.
DR CDD; cd04657; Piwi_ago-like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR014811; ArgoL1.
DR InterPro; IPR032472; ArgoL2.
DR InterPro; IPR032473; Argonaute_Mid_dom.
DR InterPro; IPR032474; Argonaute_N.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR045246; Piwi_ago-like.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF08699; ArgoL1; 1.
DR Pfam; PF16488; ArgoL2; 1.
DR Pfam; PF16487; ArgoMid; 1.
DR Pfam; PF16486; ArgoN; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM01163; DUF1785; 1.
DR SMART; SM00950; Piwi; 1.
DR SUPFAM; SSF101690; SSF101690; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS50822; PIWI; 1.
PE 1: Evidence at protein level;
KW Host-virus interaction; Nucleus; Plant defense; Reference proteome;
KW Repressor; Ribonucleoprotein; RNA-binding; RNA-mediated gene silencing;
KW Transcription; Transcription regulation; Translation regulation.
FT CHAIN 1..924
FT /note="Protein argonaute 4"
FT /id="PRO_0000404667"
FT DOMAIN 272..408
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 577..885
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 584..591
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 641
FT /note="E->K: In ago4-2; no effect on RNA binding, but loss
FT of slicer activity."
FT /evidence="ECO:0000269|PubMed:17993621"
FT MUTAGEN 660
FT /note="D->A: No effect on RNA binding, but loss of slicer
FT activity."
FT /evidence="ECO:0000269|PubMed:16998468"
FT MUTAGEN 742
FT /note="D->A: No effect on RNA binding, but loss of slicer
FT activity."
FT /evidence="ECO:0000269|PubMed:16998468"
FT MUTAGEN 874
FT /note="H->A: No effect on RNA binding, but loss of slicer
FT activity."
FT /evidence="ECO:0000269|PubMed:16998468"
SQ SEQUENCE 924 AA; 102840 MW; C0323FAE9592B147 CRC64;
MDSTNGNGAD LESANGANGS GVTEALPPPP PVIPPNVEPV RVKTELAEKK GPVRVPMARK
GFGTRGQKIP LLTNHFKVDV ANLQGHFFHY SVALFYDDGR PVEQKGVGRK ILDKVHQTYH
SDLDGKEFAY DGEKTLFTYG ALPSNKMDFS VVLEEVSATR ANGNGSPNGN ESPSDGDRKR
LRRPNRSKNF RVEISYAAKI PLQALANAMR GQESENSQEA IRVLDIILRQ HAARQGCLLV
RQSFFHNDPT NCEPVGGNIL GCRGFHSSFR TTQGGMSLNM DVTTTMIIKP GPVVDFLIAN
QNARDPYSID WSKAKRTLKN LRVKVSPSGQ EFKITGLSDK PCREQTFELK KRNPNENGEF
ETTEVTVADY FRDTRHIDLQ YSADLPCINV GKPKRPTYIP LELCALVPLQ RYTKALTTFQ
RSALVEKSRQ KPQERMTVLS KALKVSNYDA EPLLRSCGIS ISSNFTQVEG RVLPAPKLKM
GCGSETFPRN GRWNFNNKEF VEPTKIQRWV VVNFSARCNV RQVVDDLIKI GGSKGIEIAS
PFQVFEEGNQ FRRAPPMIRV ENMFKDIQSK LPGVPQFILC VLPDKKNSDL YGPWKKKNLT
EFGIVTQCMA PTRQPNDQYL TNLLLKINAK LGGLNSMLSV ERTPAFTVIS KVPTIILGMD
VSHGSPGQSD VPSIAAVVSS REWPLISKYR ASVRTQPSKA EMIESLVKKN GTEDDGIIKE
LLVDFYTSSN KRKPEHIIIF RDGVSESQFN QVLNIELDQI IEACKLLDAN WNPKFLLLVA
QKNHHTKFFQ PTSPENVPPG TIIDNKICHP KNNDFYLCAH AGMIGTTRPT HYHVLYDEIG
FSADELQELV HSLSYVYQRS TSAISVVAPI CYAHLAAAQL GTFMKFEDQS ETSSSHGGIT
APGPISVAQL PRLKDNVANS MFFC
