GenomeNet

Database: UniProt
Entry: Q9SHF3
LinkDB: Q9SHF3
Original site: Q9SHF3 
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   16-OCT-2019, entry version 111.
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;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.,
RA   Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
RA   Shibata K., 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
RT   for 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.,
RA   Zhou H., Long C., Chen S., Hannon G.J., Qi Y.;
RT   "Sorting of small RNAs into Arabidopsis argonaute complexes is
RT   directed by 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
RT   in 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-
RT   dependent 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
RT   loop to sort small RNAs.";
RL   EMBO J. 31:3588-3595(2012).
CC   -!- FUNCTION: Involved in RNA-mediated post-transcriptional gene
CC       silencing (PTGS). Main component of the RNA-induced silencing
CC       complex (RISC) that binds to a short guide RNA such as microRNA
CC       (miRNA) or small interfering RNA (siRNA). RISC uses the mature
CC       miRNA or siRNA as a guide for slicer-directed cleavage of
CC       homologous mRNAs to repress gene expression. Associates mainly
CC       with siRNAs of 21 nucleotide in length and preferentially recruits
CC       small RNAs with a 5' terminal adenosine. Probably involved in
CC       antiviral RNA silencing. Associates with siRNA derived from
CC       cucumber mosaic virus (CMV). Targeted by turnip yellows virus
CC       (TuYV) protein P0 (via F-box-like domain) for probable proteasome
CC       degradation and thereby inactivating AGO2 function in RNA
CC       silencing. Required to direct NERD-dependent DNA methylation and
CC       silencing. {ECO:0000269|PubMed:17869110,
CC       ECO:0000269|PubMed:18342361, ECO:0000269|PubMed:18342362,
CC       ECO:0000269|PubMed:18344228, 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};
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   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   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   eggNOG; ENOG410XP07; LUCA.
DR   HOGENOM; HOG000116043; -.
DR   InParanoid; Q9SHF3; -.
DR   KO; K11593; -.
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:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
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:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0019048; P:modulation by virus of host morphology or physiology; IMP:TAIR.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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; 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; Complete proteome; Plant defense; Reference proteome;
KW   Repressor; Ribonucleoprotein; RNA-binding;
KW   RNA-mediated gene silencing; Transcription; Transcription regulation;
KW   Translation regulation.
FT   CHAIN         1   1014       Protein argonaute 2.
FT                                /FTId=PRO_0000404665.
FT   DOMAIN      366    482       PAZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00142}.
FT   DOMAIN      666    965       Piwi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00150}.
FT   REGION      857    858       Interaction with guide RNA.
FT                                {ECO:0000255}.
FT   REGION      900    908       Interaction with guide RNA.
FT                                {ECO:0000255}.
FT   REGION      937    959       Interaction with guide RNA.
FT                                {ECO:0000255}.
FT   COMPBIAS      8     28       Poly-Gly.
FT   CONFLICT    658    658       K -> R (in Ref. 3; AAO64849 and 4;
FT                                BAC43071). {ECO:0000305}.
FT   STRAND      590    595       {ECO:0000244|PDB:4G0M}.
FT   TURN        596    600       {ECO:0000244|PDB:4G0M}.
FT   HELIX       609    619       {ECO:0000244|PDB:4G0M}.
FT   STRAND      628    632       {ECO:0000244|PDB:4G0M}.
FT   HELIX       635    639       {ECO:0000244|PDB:4G0M}.
FT   HELIX       641    658       {ECO:0000244|PDB:4G0M}.
FT   TURN        659    661       {ECO:0000244|PDB:4G0M}.
FT   STRAND      666    673       {ECO:0000244|PDB:4G0M}.
FT   HELIX       677    687       {ECO:0000244|PDB:4G0M}.
FT   STRAND      692    697       {ECO:0000244|PDB:4G0M}.
FT   HELIX       698    701       {ECO:0000244|PDB:4G0M}.
FT   STRAND      702    704       {ECO:0000244|PDB:4G0M}.
FT   HELIX       706    719       {ECO:0000244|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
//
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