O04379 (AGO1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein argonaute 1

Gene names

Name:	AGO1
Ordered Locus Names:	At1g48410
ORF Names:	F11A17.3, T1N15.2

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	1048 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in RNA-mediated post-transcriptional gene silencing (PTGS). Main component of the RNA-induced silencing complex (RISC) that binds to a short guide RNA such as microRNA (miRNA) or small interfering RNA (siRNA). RISC uses the mature miRNA or siRNA as a guide for slicer-directed cleavage of homologous mRNAs to repress gene expression. Requires DRB1 for directional loading of the small RNA duplex (guide stand and passenger strand) onto RISC for passenger strand degradation. Unlike animal RISC that associates in high molecular weight complex, Arabidopsis RISC is probably composed only of the AGO1 protein and associated RNA without any other proteins. Associates mainly with miRNAs of 21 nucleotide in length and preferentially recruits small RNAs with a 5' terminal uridine. Associates with 22 nucleotide miRNAs to trigger RDR6-dependent secondary siRNAs biogenesis. This pathway amplifies silencing by using the target RNA as substrate to generate secondary siRNAs. Binds to miR168 which targets its own mRNA for repression, establishing a homeostatic regulatory loop. Involved in antiviral RNA silencing by contributing to viral RNA clearance. Is capable of targeting viral RNAs with more compact structures than AGO7 which favors less structured RNA targets. May not associate with 24 nucleotide siRNAs involved in chromatin silencing. Essential for multiple processes in development. Essential for proper development of leaves and floral organs, and formation of axillary meristems. Like AGO10, required for stem cell function and organ polarity. Ref.1 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18
Subunit structure	Interacts with turnip yellows virus (TuYV) protein P0 (via F-box-like domain); this interaction targets AGO1 for degradation, and thereby suppresses its function in silencing. Interacts with turnip crinkle virus (TCV) capsid protein P38 (via GW motifs); these interactions inhibit RNA silencing ability of AGO1. Interacts (via PAZ domain) with cucumber mosaic virus (CMV) protein 2b; these interactions inhibit AGO1 function in RNA silencing. Interacts with SDE3. Ref.8 Ref.9 Ref.19 Ref.20
Subcellular location	Cytoplasm Potential.
Tissue specificity	Widely expressed at low levels.
Developmental stage	Expressed throughout all developmental stages.
Disruption phenotype	Narrow rosette leaves. Single shoot bearing a terminal inflorescence. Abnormal inflorescence with infertile flowers and filamentous organs. Ref.1 Ref.7
Sequence similarities	Belongs to the argonaute family. Ago subfamily. Contains 1 PAZ domain. Contains 1 Piwi domain.
Sequence caution	The sequence AAF79718.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Host-virus interaction Plant defense RNA-mediated gene silencing Transcription Transcription regulation Translation regulation
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
Molecular function	Developmental protein Repressor Ribonucleoprotein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA interference Inferred from mutant phenotype PubMed 17558406. Source: TAIR adaxial/abaxial pattern specification Inferred from mutant phenotype PubMed 22623415. Source: TAIR adventitious root development Inferred from mutant phenotype PubMed 15829601. Source: TAIR auxin metabolic process Inferred from genetic interaction PubMed 15829601. Source: TAIR defense response Inferred from electronic annotation. Source: UniProtKB-KW embryo development ending in seed dormancy Inferred from genetic interaction PubMed 9876176. Source: TAIR gene silencing by RNA Inferred from electronic annotation. Source: UniProtKB-KW gene silencing by miRNA Inferred from expression pattern PubMed 15131082. Source: TAIR leaf morphogenesis Inferred from mutant phenotype Ref.1. Source: TAIR leaf proximal/distal pattern formation Inferred from mutant phenotype PubMed 22623415. Source: TAIR leaf vascular tissue pattern formation Inferred from mutant phenotype PubMed 22623415. Source: TAIR multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW response to auxin stimulus Inferred from genetic interaction PubMed 15829601. Source: TAIR response to far red light Inferred from genetic interaction PubMed 15829601. Source: TAIR stem cell development Inferred from genetic interaction PubMed 18653559. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus induced gene silencing Inferred from direct assay Ref.8. Source: TAIR virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay Ref.12. Source: TAIR extrinsic to membrane Inferred from direct assay PubMed 22247288. Source: TAIR nucleus Inferred from direct assay PubMed 17442570. Source: TAIR ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW endoribonuclease activity Inferred from direct assay Ref.7. Source: TAIR miRNA binding Inferred from physical interaction Ref.7. Source: TAIR siRNA binding Inferred from physical interaction Ref.7. Source: TAIR
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O04379-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O04379-2)

The sequence of this isoform differs from the canonical sequence as follows:
     332-332: R → RIR

Note: May be due to a competing acceptor splice site. No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1048

1048

Protein argonaute 1

PRO_0000194068

Regions

Domain

391 – 501

111

PAZ

Domain

676 – 997

322

Piwi

Compositional bias

13 – 104

92

Gly-rich

Amino acid modifications

Modified residue

1001

1

Phosphoserine Ref.12 Ref.15

Natural variations

Alternative sequence

332

1

R → RIR in isoform 2.

VSP_040612

Secondary structure

1

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1048

Helix Strand Turn

Details...

Beta strand

596 – 598

3

Beta strand

604 – 609

6

Helix

616 – 632

17

Helix

650 – 652

3

Helix

653 – 666

14

Beta strand

676 – 681

6

Helix

688 – 698

11

Beta strand

704 – 708

5

Helix

709 – 714

6

Helix

717 – 730

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 3E5146343A09C541	FASTA	1,048	116,191
	10 20 30 40 50 60 MVRKRRTDAP SEGGEGSGSR EAGPVSGGGR GSQRGGFQQG GGQHQGGRGY TPQPQQGGRG 70 80 90 100 110 120 GRGYGQPPQQ QQQYGGPQEY QGRGRGGPPH QGGRGGYGGG RGGGPSSGPP QRQSVPELHQ 130 140 150 160 170 180 ATSPTYQAVS SQPTLSEVSP TQVPEPTVLA QQFEQLSVEQ GAPSQAIQPI PSSSKAFKFP 190 200 210 220 230 240 MRPGKGQSGK RCIVKANHFF AELPDKDLHH YDVTITPEVT SRGVNRAVMK QLVDNYRDSH 250 260 270 280 290 300 LGSRLPAYDG RKSLYTAGPL PFNSKEFRIN LLDEEVGAGG QRREREFKVV IKLVARADLH 310 320 330 340 350 360 HLGMFLEGKQ SDAPQEALQV LDIVLRELPT SRYIPVGRSF YSPDIGKKQS LGDGLESWRG 370 380 390 400 410 420 FYQSIRPTQM GLSLNIDMSS TAFIEANPVI QFVCDLLNRD ISSRPLSDAD RVKIKKALRG 430 440 450 460 470 480 VKVEVTHRGN MRRKYRISGL TAVATRELTF PVDERNTQKS VVEYFHETYG FRIQHTQLPC 490 500 510 520 530 540 LQVGNSNRPN YLPMEVCKIV EGQRYSKRLN ERQITALLKV TCQRPIDREK DILQTVQLND 550 560 570 580 590 600 YAKDNYAQEF GIKISTSLAS VEARILPPPW LKYHESGREG TCLPQVGQWN MMNKKMINGG 610 620 630 640 650 660 TVNNWICINF SRQVQDNLAR TFCQELAQMC YVSGMAFNPE PVLPPVSARP EQVEKVLKTR 670 680 690 700 710 720 YHDATSKLSQ GKEIDLLIVI LPDNNGSLYG DLKRICETEL GIVSQCCLTK HVFKMSKQYM 730 740 750 760 770 780 ANVALKINVK VGGRNTVLVD ALSRRIPLVS DRPTIIFGAD VTHPHPGEDS SPSIAAVVAS 790 800 810 820 830 840 QDWPEITKYA GLVCAQAHRQ ELIQDLFKEW KDPQKGVVTG GMIKELLIAF RRSTGHKPLR 850 860 870 880 890 900 IIFYRDGVSE GQFYQVLLYE LDAIRKACAS LEAGYQPPVT FVVVQKRHHT RLFAQNHNDR 910 920 930 940 950 960 HSVDRSGNIL PGTVVDSKIC HPTEFDFYLC SHAGIQGTSR PAHYHVLWDE NNFTADGLQS 970 980 990 1000 1010 1020 LTNNLCYTYA RCTRSVSIVP PAYYAHLAAF RARFYMEPET SDSGSMASGS MARGGGMAGR 1030 1040 STRGPNVNAA VRPLPALKEN VKRVMFYC
	Isoform 2 [UniParc]. Checksum: 233B89E5E4D9E1EC	FASTA	1,050	116,460
	10 20 30 40 50 60 MVRKRRTDAP SEGGEGSGSR EAGPVSGGGR GSQRGGFQQG GGQHQGGRGY TPQPQQGGRG 70 80 90 100 110 120 GRGYGQPPQQ QQQYGGPQEY QGRGRGGPPH QGGRGGYGGG RGGGPSSGPP QRQSVPELHQ 130 140 150 160 170 180 ATSPTYQAVS SQPTLSEVSP TQVPEPTVLA QQFEQLSVEQ GAPSQAIQPI PSSSKAFKFP 190 200 210 220 230 240 MRPGKGQSGK RCIVKANHFF AELPDKDLHH YDVTITPEVT SRGVNRAVMK QLVDNYRDSH 250 260 270 280 290 300 LGSRLPAYDG RKSLYTAGPL PFNSKEFRIN LLDEEVGAGG QRREREFKVV IKLVARADLH 310 320 330 340 350 360 HLGMFLEGKQ SDAPQEALQV LDIVLRELPT SRIRYIPVGR SFYSPDIGKK QSLGDGLESW 370 380 390 400 410 420 RGFYQSIRPT QMGLSLNIDM SSTAFIEANP VIQFVCDLLN RDISSRPLSD ADRVKIKKAL 430 440 450 460 470 480 RGVKVEVTHR GNMRRKYRIS GLTAVATREL TFPVDERNTQ KSVVEYFHET YGFRIQHTQL 490 500 510 520 530 540 PCLQVGNSNR PNYLPMEVCK IVEGQRYSKR LNERQITALL KVTCQRPIDR EKDILQTVQL 550 560 570 580 590 600 NDYAKDNYAQ EFGIKISTSL ASVEARILPP PWLKYHESGR EGTCLPQVGQ WNMMNKKMIN 610 620 630 640 650 660 GGTVNNWICI NFSRQVQDNL ARTFCQELAQ MCYVSGMAFN PEPVLPPVSA RPEQVEKVLK 670 680 690 700 710 720 TRYHDATSKL SQGKEIDLLI VILPDNNGSL YGDLKRICET ELGIVSQCCL TKHVFKMSKQ 730 740 750 760 770 780 YMANVALKIN VKVGGRNTVL VDALSRRIPL VSDRPTIIFG ADVTHPHPGE DSSPSIAAVV 790 800 810 820 830 840 ASQDWPEITK YAGLVCAQAH RQELIQDLFK EWKDPQKGVV TGGMIKELLI AFRRSTGHKP 850 860 870 880 890 900 LRIIFYRDGV SEGQFYQVLL YELDAIRKAC ASLEAGYQPP VTFVVVQKRH HTRLFAQNHN 910 920 930 940 950 960 DRHSVDRSGN ILPGTVVDSK ICHPTEFDFY LCSHAGIQGT SRPAHYHVLW DENNFTADGL 970 980 990 1000 1010 1020 QSLTNNLCYT YARCTRSVSI VPPAYYAHLA AFRARFYMEP ETSDSGSMAS GSMARGGGMA 1030 1040 1050 GRSTRGPNVN AAVRPLPALK ENVKRVMFYC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"AGO1 defines a novel locus of Arabidopsis controlling leaf development." Bohmert K., Camus I., Bellini C., Bouchez D., Caboche M., Benning C. EMBO J. 17:170-180(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE. Strain: cv. Columbia. Tissue: Leaf.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: cv. Columbia.
[5]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-346 (ISOFORM 2). Strain: cv. Columbia.
[6]	"The role of ARGONAUTE1 (AGO1) in meristem formation and identity." Kidner C.A., Martienssen R.A. Dev. Biol. 280:504-517(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Arabidopsis ARGONAUTE1 is an RNA Slicer that selectively recruits microRNAs and short interfering RNAs." Baumberger N., Baulcombe D.C. Proc. Natl. Acad. Sci. U.S.A. 102:11928-11933(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[8]	"Cucumber mosaic virus-encoded 2b suppressor inhibits Arabidopsis Argonaute1 cleavage activity to counter plant defense." Zhang X., Yuan Y.R., Pei Y., Lin S.S., Tuschl T., Patel D.J., Chua N.H. Genes Dev. 20:3255-3268(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CUCUMBER MOSAIC VIRUS PROTEIN 2B.
[9]	"The Polerovirus silencing suppressor P0 targets ARGONAUTE proteins for degradation." Baumberger N., Tsai C.-H., Lie M., Havecker E., Baulcombe D.C. Curr. Biol. 17:1609-1614(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TURNIP YELLOWS VIRUS PROTEIN P0.
[10]	"Sorting of small RNAs into Arabidopsis argonaute complexes is directed by the 5' terminal nucleotide." Mi S., Cai T., Hu Y., Chen Y., Hodges E., Ni F., Wu L., Li S., Zhou H., Long C., Chen S., Hannon G.J., Qi Y. Cell 133:116-127(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Specificity of ARGONAUTE7-miR390 interaction and dual functionality in TAS3 trans-acting siRNA formation." Montgomery T.A., Howell M.D., Cuperus J.T., Li D., Hansen J.E., Alexander A.L., Chapman E.J., Fahlgren N., Allen E., Carrington J.C. Cell 133:128-141(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis." de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H. J. Proteome Res. 7:2458-2470(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1001, MASS SPECTROMETRY. Tissue: Root.
[13]	"The mechanism selecting the guide strand from small RNA duplexes is different among argonaute proteins." Takeda A., Iwasaki S., Watanabe T., Utsumi M., Watanabe Y. Plant Cell Physiol. 49:493-500(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Arabidopsis DRB4, AGO1, AGO7, and RDR6 participate in a DCL4-initiated antiviral RNA silencing pathway negatively regulated by DCL1." Qu F., Ye X., Morris T.J. Proc. Natl. Acad. Sci. U.S.A. 105:14732-14737(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana." Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C. J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1001, MASS SPECTROMETRY. Strain: cv. Columbia.
[16]	"Unique functionality of 22-nt miRNAs in triggering RDR6-dependent siRNA biogenesis from target transcripts in Arabidopsis." Cuperus J.T., Carbonell A., Fahlgren N., Garcia-Ruiz H., Burke R.T., Takeda A., Sullivan C.M., Gilbert S.D., Montgomery T.A., Carrington J.C. Nat. Struct. Mol. Biol. 17:997-1003(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[17]	"Redundant and specific roles of the ARGONAUTE proteins AGO1 and ZLL in development and small RNA-directed gene silencing." Mallory A.C., Hinze A., Tucker M.R., Bouche N., Gasciolli V., Elmayan T., Lauressergues D., Jauvion V., Vaucheret H., Laux T. PLoS Genet. 5:E1000646-E1000646(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"The Arabidopsis thaliana double-stranded RNA binding protein DRB1 directs guide strand selection from microRNA duplexes." Eamens A.L., Smith N.A., Curtin S.J., Wang M.B., Waterhouse P.M. RNA 15:2219-2235(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"Argonaute quenching and global changes in Dicer homeostasis caused by a pathogen-encoded GW repeat protein." Azevedo J., Garcia D., Pontier D., Ohnesorge S., Yu A., Garcia S., Braun L., Bergdoll M., Hakimi M.A., Lagrange T., Voinnet O. Genes Dev. 24:904-915(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TURNIP CRINKLE VIRUS CAPSID PROTEIN P38.
[20]	"Ago hook and RNA helicase motifs underpin dual roles for SDE3 in antiviral defense and silencing of nonconserved intergenic regions." Garcia D., Garcia S., Pontier D., Marchais A., Renou J.P., Lagrange T., Voinnet O. Mol. Cell 48:109-120(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SDE3.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U91995 mRNA. Translation: AAC18440.1.
AC007932 Genomic DNA. Translation: AAD49755.1.
AC020889 Genomic DNA. Translation: AAF79718.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE32287.1.
CP002684 Genomic DNA. Translation: AEE32288.1.
CP002684 Genomic DNA. Translation: AEE32289.1.
BT000941 mRNA. Translation: AAN41341.1.
AK227868 mRNA. Translation: BAE99844.1.

IPI

IPI00522985.
IPI00523962.

RefSeq

NP_001185169.1. NM_001198240.1.
NP_175274.1. NM_103737.3.
NP_849784.1. NM_179453.2.

UniGene

At.21124.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3VNA	X-ray	2.00	A	592-739	[»]
3VNB	X-ray	1.50	A	592-739	[»]
4G0P	X-ray	1.80	A	593-738	[»]
4G0Q	X-ray	1.80	A	593-738	[»]
4G0X	X-ray	1.35	A	593-738	[»]
4G0Y	X-ray	1.65	A	593-738	[»]
4G0Z	X-ray	1.75	A	593-738	[»]

ProteinModelPortal

O04379.

SMR

O04379. Positions 177-996.

ModBase

Search...

Proteomic databases

PaxDb

O04379.

PRIDE

O04379.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT1G48410.1; AT1G48410.1; AT1G48410.

GeneID

841262.

KEGG

ath:AT1G48410.

Organism-specific databases

TAIR

At1g48410.

Phylogenomic databases

eggNOG

NOG279895.

HOGENOM

HOG000116043.

InParanoid

O04379.

KO

K11593.

OMA

KDLHHYD.

PhylomeDB

O04379.

ProtClustDB

CLSN2693050.

Gene expression databases

ArrayExpress

O04379.

Genevestigator

O04379.

Family and domain databases

InterPro

IPR024357. Argonaut_Gly-rich.
IPR014811. DUF1785.
IPR003100. PAZ.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view]

Pfam

PF08699. DUF1785. 1 hit.
PF12764. Gly-rich_Ago1. 1 hit.
PF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view]

SMART

SM00949. PAZ. 1 hit.
SM00950. Piwi. 1 hit.
[Graphical view]

SUPFAM

SSF101690. PAZ. 1 hit.
SSF53098. RNaseH_fold. 1 hit.

PROSITE

PS50821. PAZ. 1 hit.
PS50822. PIWI. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AGO1_ARATH

Accession

Primary (citable) accession number: O04379
Secondary accession number(s): Q0WSQ4, Q3ECU7, Q9LP83

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program