AGO1_ARATH
ID AGO1_ARATH Reviewed; 1048 AA.
AC O04379; Q0WSQ4; Q3ECU7; Q9LP83;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein argonaute 1 {ECO:0000303|PubMed:9427751};
GN Name=AGO1 {ECO:0000303|PubMed:9427751};
GN OrderedLocusNames=At1g48410 {ECO:0000312|Araport:AT1G48410};
GN ORFNames=F11A17.3 {ECO:0000312|EMBL:AAD49755.1},
GN T1N15.2 {ECO:0000312|EMBL:AAF79718.1};
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] (ISOFORM 1), FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=9427751; DOI=10.1093/emboj/17.1.170;
RA Bohmert K., Camus I., Bellini C., Bouchez D., Caboche M., Benning C.;
RT "AGO1 defines a novel locus of Arabidopsis controlling leaf development.";
RL EMBO J. 17:170-180(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-346 (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=15882589; DOI=10.1016/j.ydbio.2005.01.031;
RA Kidner C.A., Martienssen R.A.;
RT "The role of ARGONAUTE1 (AGO1) in meristem formation and identity.";
RL Dev. Biol. 280:504-517(2005).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16081530; DOI=10.1073/pnas.0505461102;
RA Baumberger N., Baulcombe D.C.;
RT "Arabidopsis ARGONAUTE1 is an RNA Slicer that selectively recruits
RT microRNAs and short interfering RNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11928-11933(2005).
RN [8]
RP FUNCTION, AND INTERACTION WITH CUCUMBER MOSAIC VIRUS PROTEIN 2B.
RX PubMed=17158744; DOI=10.1101/gad.1495506;
RA Zhang X., Yuan Y.R., Pei Y., Lin S.S., Tuschl T., Patel D.J., Chua N.H.;
RT "Cucumber mosaic virus-encoded 2b suppressor inhibits Arabidopsis
RT Argonaute1 cleavage activity to counter plant defense.";
RL Genes Dev. 20:3255-3268(2006).
RN [9]
RP INTERACTION WITH TURNIP YELLOWS VIRUS PROTEIN P0.
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 [10]
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 [11]
RP FUNCTION.
RX PubMed=18342362; DOI=10.1016/j.cell.2008.02.033;
RA Montgomery T.A., Howell M.D., Cuperus J.T., Li D., Hansen J.E.,
RA Alexander A.L., Chapman E.J., Fahlgren N., Allen E., Carrington J.C.;
RT "Specificity of ARGONAUTE7-miR390 interaction and dual functionality in
RT TAS3 trans-acting siRNA formation.";
RL Cell 133:128-141(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1001, 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 [13]
RP FUNCTION.
RX PubMed=18344228; DOI=10.1093/pcp/pcn043;
RA Takeda A., Iwasaki S., Watanabe T., Utsumi M., Watanabe Y.;
RT "The mechanism selecting the guide strand from small RNA duplexes is
RT different among argonaute proteins.";
RL Plant Cell Physiol. 49:493-500(2008).
RN [14]
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 [15]
RP IDENTIFICATION BY 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 [16]
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).
RN [17]
RP FUNCTION.
RX PubMed=20562854; DOI=10.1038/nsmb.1866;
RA Cuperus J.T., Carbonell A., Fahlgren N., Garcia-Ruiz H., Burke R.T.,
RA Takeda A., Sullivan C.M., Gilbert S.D., Montgomery T.A., Carrington J.C.;
RT "Unique functionality of 22-nt miRNAs in triggering RDR6-dependent siRNA
RT biogenesis from target transcripts in Arabidopsis.";
RL Nat. Struct. Mol. Biol. 17:997-1003(2010).
RN [18]
RP FUNCTION.
RX PubMed=19763164; DOI=10.1371/journal.pgen.1000646;
RA Mallory A.C., Hinze A., Tucker M.R., Bouche N., Gasciolli V., Elmayan T.,
RA Lauressergues D., Jauvion V., Vaucheret H., Laux T.;
RT "Redundant and specific roles of the ARGONAUTE proteins AGO1 and ZLL in
RT development and small RNA-directed gene silencing.";
RL PLoS Genet. 5:E1000646-E1000646(2009).
RN [19]
RP FUNCTION.
RX PubMed=19861421; DOI=10.1261/rna.1646909;
RA Eamens A.L., Smith N.A., Curtin S.J., Wang M.B., Waterhouse P.M.;
RT "The Arabidopsis thaliana double-stranded RNA binding protein DRB1 directs
RT guide strand selection from microRNA duplexes.";
RL RNA 15:2219-2235(2009).
RN [20]
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 [21]
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 [22]
RP INTERACTION WITH HESO1.
RX PubMed=24733911; DOI=10.1073/pnas.1405083111;
RA Ren G., Xie M., Zhang S., Vinovskis C., Chen X., Yu B.;
RT "Methylation protects microRNAs from an AGO1-associated activity that
RT uridylates 5' RNA fragments generated by AGO1 cleavage.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:6365-6370(2014).
RN [23]
RP INTERACTION WITH URT1.
RX PubMed=25928341; DOI=10.1371/journal.pgen.1005091;
RA Wang X., Zhang S., Dou Y., Zhang C., Chen X., Yu B., Ren G.;
RT "Synergistic and independent actions of multiple terminal nucleotidyl
RT transferases in the 3' tailing of small RNAs in Arabidopsis.";
RL PLoS Genet. 11:E1005091-E1005091(2015).
RN [24]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RICE1 AND RICE2.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=28463111; DOI=10.7554/elife.24466;
RA Zhang Z., Hu F., Sung M.W., Shu C., Castillo-Gonzalez C., Koiwa H.,
RA Tang G., Dickman M., Li P., Zhang X.;
RT "RISC-interacting clearing 3'- 5' exoribonucleases (RICEs) degrade
RT uridylated cleavage fragments to maintain functional RISC in Arabidopsis
RT thaliana.";
RL Elife 6:E24466-E24466(2017).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 593-738 IN COMPLEX WITH AMP; CMP;
RP GMP AND UMP.
RX PubMed=22850669; DOI=10.1038/emboj.2012.204;
RA Frank F., Hauver J., Sonenberg N., Nagar B.;
RT "Arabidopsis Argonaute MID domains use their nucleotide specificity loop to
RT sort small RNAs.";
RL EMBO J. 31:3588-3595(2012).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 592-739, AND RNA-BINDING.
RX PubMed=22771475; DOI=10.1016/j.febslet.2012.06.038;
RA Zha X., Xia Q., Yuan Y.A.;
RT "Structural insights into small RNA sorting and mRNA target binding by
RT Arabidopsis Argonaute Mid domains.";
RL FEBS Lett. 586:3200-3207(2012).
CC -!- FUNCTION: Involved in RNA-mediated post-transcriptional gene silencing
CC (PTGS). Main component of the RNA-induced silencing complex (RISC) that
CC binds to a short guide RNA such as microRNA (miRNA) or small
CC interfering RNA (siRNA). RISC uses the mature miRNA or siRNA as a guide
CC for slicer-directed cleavage of homologous mRNAs to repress gene
CC expression. Requires DRB1 for directional loading of the small RNA
CC duplex (guide stand and passenger strand) onto RISC for passenger
CC strand degradation. Unlike animal RISC that associates in high
CC molecular weight complex, Arabidopsis RISC is probably composed only of
CC the AGO1 protein and associated RNA without any other proteins.
CC Associates mainly with miRNAs of 21 nucleotide in length and
CC preferentially recruits small RNAs with a 5' terminal uridine.
CC Associates with 22 nucleotide miRNAs to trigger RDR6-dependent
CC secondary siRNAs biogenesis. This pathway amplifies silencing by using
CC the target RNA as substrate to generate secondary siRNAs. Binds to
CC miR168 which targets its own mRNA for repression, establishing a
CC homeostatic regulatory loop. Involved in antiviral RNA silencing by
CC contributing to viral RNA clearance. Is capable of targeting viral RNAs
CC with more compact structures than AGO7 which favors less structured RNA
CC targets. May not associate with 24 nucleotide siRNAs involved in
CC chromatin silencing. Essential for multiple processes in development.
CC Essential for proper development of leaves and floral organs, and
CC formation of axillary meristems. Like AGO10, required for stem cell
CC function and organ polarity. {ECO:0000269|PubMed:15882589,
CC ECO:0000269|PubMed:16081530, ECO:0000269|PubMed:17158744,
CC ECO:0000269|PubMed:18342361, ECO:0000269|PubMed:18342362,
CC ECO:0000269|PubMed:18344228, ECO:0000269|PubMed:18799732,
CC ECO:0000269|PubMed:19763164, ECO:0000269|PubMed:19861421,
CC ECO:0000269|PubMed:20562854, ECO:0000269|PubMed:9427751}.
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 turnip yellows virus (TuYV) protein P0 (via F-
CC box-like domain); this interaction targets AGO1 for degradation, and
CC thereby suppresses its function in silencing. Interacts with turnip
CC crinkle virus (TCV) capsid protein P38 (via GW motifs); these
CC interactions inhibit RNA silencing ability of AGO1. Interacts (via PAZ
CC domain) with cucumber mosaic virus (CMV) protein 2b; these interactions
CC inhibit AGO1 function in RNA silencing. Interacts with SDE3
CC (PubMed:17158744, PubMed:17869110, PubMed:20439431, PubMed:22850669,
CC PubMed:22940249). Interacts with HESO1 (PubMed:24733911). Interacts
CC with URT1 (PubMed:25928341). Interacts with RICE1 and RICE2 that act as
CC cofactors (PubMed:28463111). {ECO:0000269|PubMed:17158744,
CC ECO:0000269|PubMed:17869110, ECO:0000269|PubMed:20439431,
CC ECO:0000269|PubMed:22850669, ECO:0000269|PubMed:22940249,
CC ECO:0000269|PubMed:24733911, ECO:0000269|PubMed:25928341,
CC ECO:0000269|PubMed:28463111}.
CC -!- INTERACTION:
CC O04379; Q9M1S8: AMP1; NbExp=2; IntAct=EBI-6912745, EBI-6912802;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28463111}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O04379-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O04379-2; Sequence=VSP_040612;
CC -!- TISSUE SPECIFICITY: Widely expressed at low levels.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout all developmental stages.
CC -!- DISRUPTION PHENOTYPE: Narrow rosette leaves. Single shoot bearing a
CC terminal inflorescence. Abnormal inflorescence with infertile flowers
CC and filamentous organs. {ECO:0000269|PubMed:16081530,
CC ECO:0000269|PubMed:9427751}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79718.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U91995; AAC18440.1; -; mRNA.
DR EMBL; AC007932; AAD49755.1; -; Genomic_DNA.
DR EMBL; AC020889; AAF79718.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32287.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32288.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32289.1; -; Genomic_DNA.
DR EMBL; BT000941; AAN41341.1; -; mRNA.
DR EMBL; AK227868; BAE99844.1; -; mRNA.
DR RefSeq; NP_001185169.1; NM_001198240.1. [O04379-2]
DR RefSeq; NP_175274.1; NM_103737.4. [O04379-1]
DR RefSeq; NP_849784.1; NM_179453.3. [O04379-2]
DR PDB; 3VNA; X-ray; 2.00 A; A=592-739.
DR PDB; 3VNB; X-ray; 1.50 A; A=592-739.
DR PDB; 4G0P; X-ray; 1.80 A; A=593-738.
DR PDB; 4G0Q; X-ray; 1.80 A; A=593-738.
DR PDB; 4G0X; X-ray; 1.35 A; A=593-738.
DR PDB; 4G0Y; X-ray; 1.65 A; A=593-738.
DR PDB; 4G0Z; X-ray; 1.75 A; A=593-738.
DR PDBsum; 3VNA; -.
DR PDBsum; 3VNB; -.
DR PDBsum; 4G0P; -.
DR PDBsum; 4G0Q; -.
DR PDBsum; 4G0X; -.
DR PDBsum; 4G0Y; -.
DR PDBsum; 4G0Z; -.
DR AlphaFoldDB; O04379; -.
DR SMR; O04379; -.
DR BioGRID; 26487; 11.
DR IntAct; O04379; 1.
DR STRING; 3702.AT1G48410.2; -.
DR iPTMnet; O04379; -.
DR PaxDb; O04379; -.
DR PRIDE; O04379; -.
DR ProteomicsDB; 244928; -. [O04379-1]
DR EnsemblPlants; AT1G48410.1; AT1G48410.1; AT1G48410. [O04379-1]
DR EnsemblPlants; AT1G48410.2; AT1G48410.2; AT1G48410. [O04379-2]
DR EnsemblPlants; AT1G48410.3; AT1G48410.3; AT1G48410. [O04379-2]
DR GeneID; 841262; -.
DR Gramene; AT1G48410.1; AT1G48410.1; AT1G48410. [O04379-1]
DR Gramene; AT1G48410.2; AT1G48410.2; AT1G48410. [O04379-2]
DR Gramene; AT1G48410.3; AT1G48410.3; AT1G48410. [O04379-2]
DR KEGG; ath:AT1G48410; -.
DR Araport; AT1G48410; -.
DR TAIR; locus:2007760; AT1G48410.
DR eggNOG; KOG1041; Eukaryota.
DR HOGENOM; CLU_004544_0_0_1; -.
DR InParanoid; O04379; -.
DR OMA; VGANRHY; -.
DR PhylomeDB; O04379; -.
DR PRO; PR:O04379; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04379; baseline and differential.
DR Genevisible; O04379; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; IDA:CAFA.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0035197; F:siRNA binding; IDA:TAIR.
DR GO; GO:0009955; P:adaxial/abaxial pattern specification; IMP:TAIR.
DR GO; GO:0048830; P:adventitious root development; IMP:TAIR.
DR GO; GO:0009850; P:auxin metabolic process; IGI:TAIR.
DR GO; GO:0030154; P:cell differentiation; IGI:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IDA:TAIR.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR GO; GO:0010589; P:leaf proximal/distal pattern formation; IMP:TAIR.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IMP:TAIR.
DR GO; GO:0016441; P:post-transcriptional gene silencing; IEP: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:0009733; P:response to auxin; IGI:TAIR.
DR GO; GO:0010218; P:response to far red light; IGI:TAIR.
DR GO; GO:0009616; P:RNAi-mediated antiviral immune response; IDA:TAIR.
DR CDD; cd04657; Piwi_ago-like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR014811; ArgoL1.
DR InterPro; IPR032472; ArgoL2.
DR InterPro; IPR024357; Argonaut_Gly-rich.
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; PF12764; Gly-rich_Ago1; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF02171; Piwi; 1.
DR SMART; SM01163; DUF1785; 1.
DR SMART; SM00949; PAZ; 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 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Host-virus interaction; Magnesium; Manganese; Metal-binding;
KW Phosphoprotein; Plant defense; Reference proteome; Repressor;
KW Ribonucleoprotein; RNA-binding; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Translation regulation.
FT CHAIN 1..1048
FT /note="Protein argonaute 1"
FT /id="PRO_0000194068"
FT DOMAIN 391..501
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 676..997
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..887
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000255"
FT REGION 932..940
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000255"
FT REGION 969..991
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000255"
FT REGION 1005..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 760
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 846
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 986
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT VAR_SEQ 332
FT /note="R -> RIR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_040612"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:4G0X"
FT STRAND 604..609
FT /evidence="ECO:0007829|PDB:4G0X"
FT HELIX 616..632
FT /evidence="ECO:0007829|PDB:4G0X"
FT HELIX 650..652
FT /evidence="ECO:0007829|PDB:4G0X"
FT HELIX 653..666
FT /evidence="ECO:0007829|PDB:4G0X"
FT STRAND 676..681
FT /evidence="ECO:0007829|PDB:4G0X"
FT HELIX 688..698
FT /evidence="ECO:0007829|PDB:4G0X"
FT STRAND 704..708
FT /evidence="ECO:0007829|PDB:4G0X"
FT HELIX 709..714
FT /evidence="ECO:0007829|PDB:4G0X"
FT HELIX 717..730
FT /evidence="ECO:0007829|PDB:4G0X"
SQ SEQUENCE 1048 AA; 116191 MW; 3E5146343A09C541 CRC64;
MVRKRRTDAP SEGGEGSGSR EAGPVSGGGR GSQRGGFQQG GGQHQGGRGY TPQPQQGGRG
GRGYGQPPQQ QQQYGGPQEY QGRGRGGPPH QGGRGGYGGG RGGGPSSGPP QRQSVPELHQ
ATSPTYQAVS SQPTLSEVSP TQVPEPTVLA QQFEQLSVEQ GAPSQAIQPI PSSSKAFKFP
MRPGKGQSGK RCIVKANHFF AELPDKDLHH YDVTITPEVT SRGVNRAVMK QLVDNYRDSH
LGSRLPAYDG RKSLYTAGPL PFNSKEFRIN LLDEEVGAGG QRREREFKVV IKLVARADLH
HLGMFLEGKQ SDAPQEALQV LDIVLRELPT SRYIPVGRSF YSPDIGKKQS LGDGLESWRG
FYQSIRPTQM GLSLNIDMSS TAFIEANPVI QFVCDLLNRD ISSRPLSDAD RVKIKKALRG
VKVEVTHRGN MRRKYRISGL TAVATRELTF PVDERNTQKS VVEYFHETYG FRIQHTQLPC
LQVGNSNRPN YLPMEVCKIV EGQRYSKRLN ERQITALLKV TCQRPIDREK DILQTVQLND
YAKDNYAQEF GIKISTSLAS VEARILPPPW LKYHESGREG TCLPQVGQWN MMNKKMINGG
TVNNWICINF SRQVQDNLAR TFCQELAQMC YVSGMAFNPE PVLPPVSARP EQVEKVLKTR
YHDATSKLSQ GKEIDLLIVI LPDNNGSLYG DLKRICETEL GIVSQCCLTK HVFKMSKQYM
ANVALKINVK VGGRNTVLVD ALSRRIPLVS DRPTIIFGAD VTHPHPGEDS SPSIAAVVAS
QDWPEITKYA GLVCAQAHRQ ELIQDLFKEW KDPQKGVVTG GMIKELLIAF RRSTGHKPLR
IIFYRDGVSE GQFYQVLLYE LDAIRKACAS LEAGYQPPVT FVVVQKRHHT RLFAQNHNDR
HSVDRSGNIL PGTVVDSKIC HPTEFDFYLC SHAGIQGTSR PAHYHVLWDE NNFTADGLQS
LTNNLCYTYA RCTRSVSIVP PAYYAHLAAF RARFYMEPET SDSGSMASGS MARGGGMAGR
STRGPNVNAA VRPLPALKEN VKRVMFYC
