AGO2_ARATH
ID AGO2_ARATH Reviewed; 1014 AA.
AC Q9SHF3; Q8GX33;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein argonaute 2;
GN Name=AGO2; OrderedLocusNames=At1g31280; ORFNames=T19E23.7;
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=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 [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] OF 444-1014.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 475-1014.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [7]
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 [8]
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 [9]
RP FUNCTION, AND INTERACTION WITH NERD.
RC STRAIN=cv. Columbia;
RX PubMed=22940247; DOI=10.1016/j.molcel.2012.07.027;
RA Pontier D., Picart C., Roudier F., Garcia D., Lahmy S., Azevedo J.,
RA Alart E., Laudie M., Karlowski W.M., Cooke R., Colot V., Voinnet O.,
RA Lagrange T.;
RT "NERD, a plant-specific GW protein, defines an additional RNAi-dependent
RT chromatin-based pathway in Arabidopsis.";
RL Mol. Cell 48:121-132(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 579-727.
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).
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. Associates mainly with siRNAs of 21 nucleotide in length
CC and preferentially recruits small RNAs with a 5' terminal adenosine.
CC Probably involved in antiviral RNA silencing. Associates with siRNA
CC derived from cucumber mosaic virus (CMV). Targeted by turnip yellows
CC virus (TuYV) protein P0 (via F-box-like domain) for probable proteasome
CC degradation and thereby inactivating AGO2 function in RNA silencing.
CC Required to direct NERD-dependent DNA methylation and silencing.
CC {ECO:0000269|PubMed:17869110, ECO:0000269|PubMed:18342361,
CC ECO:0000269|PubMed:18342362, ECO:0000269|PubMed:18344228,
CC ECO:0000269|PubMed:22940247}.
CC -!- SUBUNIT: Interacts with NERD. {ECO:0000269|PubMed:22940247}.
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO64849.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC007654; AAF24585.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31335.1; -; Genomic_DNA.
DR EMBL; BT005914; AAO64849.1; ALT_INIT; mRNA.
DR EMBL; AK118463; BAC43071.1; -; mRNA.
DR PIR; H86438; H86438.
DR RefSeq; NP_174413.2; NM_102866.3.
DR PDB; 4G0M; X-ray; 2.31 A; A/B=579-727.
DR PDBsum; 4G0M; -.
DR AlphaFoldDB; Q9SHF3; -.
DR SMR; Q9SHF3; -.
DR BioGRID; 25251; 2.
DR IntAct; Q9SHF3; 1.
DR STRING; 3702.AT1G31280.1; -.
DR iPTMnet; Q9SHF3; -.
DR PaxDb; Q9SHF3; -.
DR PRIDE; Q9SHF3; -.
DR ProteomicsDB; 244718; -.
DR EnsemblPlants; AT1G31280.1; AT1G31280.1; AT1G31280.
DR GeneID; 840016; -.
DR Gramene; AT1G31280.1; AT1G31280.1; AT1G31280.
DR KEGG; ath:AT1G31280; -.
DR Araport; AT1G31280; -.
DR TAIR; locus:2197545; AT1G31280.
DR eggNOG; KOG1041; Eukaryota.
DR HOGENOM; CLU_004544_3_0_1; -.
DR InParanoid; Q9SHF3; -.
DR OMA; YLCSYYG; -.
DR OrthoDB; 159407at2759; -.
DR PhylomeDB; Q9SHF3; -.
DR PRO; PR:Q9SHF3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SHF3; baseline and differential.
DR Genevisible; Q9SHF3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
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:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0051607; P:defense response to virus; IDA: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 CDD; cd04657; Piwi_ago-like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR014811; ArgoL1.
DR InterPro; IPR032472; ArgoL2.
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; PF16486; ArgoN; 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; Plant defense; Reference proteome; Repressor;
KW Ribonucleoprotein; RNA-binding; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Translation regulation.
FT CHAIN 1..1014
FT /note="Protein argonaute 2"
FT /id="PRO_0000404665"
FT DOMAIN 366..482
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 666..965
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..858
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000255"
FT REGION 900..908
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000255"
FT REGION 937..959
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000255"
FT COMPBIAS 79..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 658
FT /note="K -> R (in Ref. 3; AAO64849 and 4; BAC43071)"
FT /evidence="ECO:0000305"
FT STRAND 590..595
FT /evidence="ECO:0007829|PDB:4G0M"
FT TURN 596..600
FT /evidence="ECO:0007829|PDB:4G0M"
FT HELIX 609..619
FT /evidence="ECO:0007829|PDB:4G0M"
FT STRAND 628..632
FT /evidence="ECO:0007829|PDB:4G0M"
FT HELIX 635..639
FT /evidence="ECO:0007829|PDB:4G0M"
FT HELIX 641..658
FT /evidence="ECO:0007829|PDB:4G0M"
FT TURN 659..661
FT /evidence="ECO:0007829|PDB:4G0M"
FT STRAND 666..673
FT /evidence="ECO:0007829|PDB:4G0M"
FT HELIX 677..687
FT /evidence="ECO:0007829|PDB:4G0M"
FT STRAND 692..697
FT /evidence="ECO:0007829|PDB:4G0M"
FT HELIX 698..701
FT /evidence="ECO:0007829|PDB:4G0M"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:4G0M"
FT HELIX 706..719
FT /evidence="ECO:0007829|PDB:4G0M"
SQ SEQUENCE 1014 AA; 113423 MW; 0B6E36C922069DD2 CRC64;
MERGGYRGGR GDGRGRGGRG YGGGGGGGEQ GRDRGYGGGE QGRGRGSERG GGNRGQGRGE
QQDFRSQSQR GPPPGHGGRG TTQFQQPRPQ VAPQPSQAPA SYAGSVGGVA GRGAWGRKPQ
VPSDSASPST STTVVSEPVR VAEVMNLKPS VQVATSDRKE PMKRPDRGGV VAVRRVNLYV
NHYKVNFNPE SVIRHYDVEI KGEIPTKKVS RFELAMVRDK VFTDNPDEFP LAMTAYDGQK
NIFSAVELPT GSYKVEYPKT EEMRGRSYTF TIKQVNVLKL GDLKEYMTGR SSFNPRDVLQ
GMDVVMKEHP SKCMITVGKS FFTRETEPDE DFRFGVIAAK GYRHTLKPTA QGLSLCLDYS
VLAFRKAMSV IEYLKLYFNW SDMRQFRRRD VEEELIGLKV TVNHRKNKQK LTIVGLSMQN
TKDIKFDLID QEGNEPPRKT SIVEYFRIKY GRHIVHKDIP CLDLGKNGRQ NFVPMEFCDL
VEGQIYPKDN LDKDSALWLK KLSLVNPQQR QRNIDKMIKA RNGPSGGEII GNFGLKVDTN
MTPVEGRVLK APSLKLAERG RVVREEPNPR QNNQWNLMKK GVTRGSIVKH WAVLDFTASE
RFNKMPNDFV DNLIDRCWRL GMQMEAPIVY KTSRMETLSN GNAIEELLRS VIDEASRKHG
GARPTLVLCA MSRKDDGYKT LKWIAETKLG LVTQCFLTGP ATKGGDQYRA NLALKMNAKV
GGSNVELMDT FSFFKKEDEV MFIGADVNHP AARDKMSPSI VAVVGTLNWP EANRYAARVI
AQPHRKEEIQ GFGDACLELV KAHVQATGKR PNKIVIFRDG VSDAQFDMVL NVELLDVKLT
FEKNGYNPKI TVIVAQKRHQ TRFFPATNND GSDKGNVPSG TVVDTKVIHP YEYDFYLCSH
HGGIGTSKPT HYYTLWDELG FTSDQVQKLI FEMCFTFTRC TKPVSLVPPV YYADMVAFRG
RMYHEASSRE KNFKQPRGAS TSAASLASSL SSLTIEDKAI FKLHAELENV MFFV
