AGO6_ARATH
ID AGO6_ARATH Reviewed; 878 AA.
AC O48771;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein argonaute 6;
GN Name=AGO6; OrderedLocusNames=At2g32940; ORFNames=T21L14.12;
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 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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17332757; DOI=10.1038/sj.emboj.7601603;
RA Zheng X., Zhu J., Kapoor A., Zhu J.K.;
RT "Role of Arabidopsis AGO6 in siRNA accumulation, DNA methylation and
RT transcriptional gene silencing.";
RL EMBO J. 26:1691-1701(2007).
RN [5]
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).
CC -!- FUNCTION: Involved in transcriptional gene silencing (TGS). Component
CC of the RISC complex that associate with the small interfering RNA
CC (siRNA) pathway involved in direct cytosine methylation at endogenous
CC DNA repeats. Required for the accumulation of specific siRNAs derived
CC from transgene and heterochromatin-related endogenous loci. Involved in
CC RNA-directed DNA methylation (RdDM) at specific endogenous loci.
CC Probably not required for the accumulation of siRNAs derived from
CC transgene inverted repeats that induce post-transcriptional gene
CC silencing (PTGS). Associates mainly with small RNAs of 24 nucleotide in
CC length and preferentially recruits small RNAs with a 5' terminal
CC adenosine. Targeted by turnip yellows virus (TuYV) protein P0 (via F-
CC box-like domain) for probable proteasome degradation and thereby
CC inactivating AGO6 function in RNA silencing.
CC {ECO:0000269|PubMed:17332757, ECO:0000269|PubMed:17869110,
CC ECO:0000269|PubMed:20173091}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17332757}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons and shoot
CC meristematic region. {ECO:0000269|PubMed:17332757,
CC ECO:0000269|PubMed:20173091}.
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB91987.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003033; AAB91987.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08765.1; -; Genomic_DNA.
DR PIR; T01113; T01113.
DR RefSeq; NP_180853.2; NM_128854.4.
DR AlphaFoldDB; O48771; -.
DR SMR; O48771; -.
DR STRING; 3702.AT2G32940.1; -.
DR PaxDb; O48771; -.
DR PRIDE; O48771; -.
DR ProteomicsDB; 244721; -.
DR EnsemblPlants; AT2G32940.1; AT2G32940.1; AT2G32940.
DR GeneID; 817856; -.
DR Gramene; AT2G32940.1; AT2G32940.1; AT2G32940.
DR KEGG; ath:AT2G32940; -.
DR Araport; AT2G32940; -.
DR TAIR; locus:2059370; AT2G32940.
DR eggNOG; KOG1041; Eukaryota.
DR HOGENOM; CLU_004544_2_0_1; -.
DR InParanoid; O48771; -.
DR OMA; MNDQYYT; -.
DR OrthoDB; 220258at2759; -.
DR PhylomeDB; O48771; -.
DR PRO; PR:O48771; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48771; baseline and differential.
DR Genevisible; O48771; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0035197; F:siRNA binding; IDA:TAIR.
DR GO; GO:0051607; P:defense response to virus; IDA:TAIR.
DR GO; GO:0006306; P:DNA methylation; 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: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; 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; SM00950; Piwi; 1.
DR SUPFAM; SSF101690; SSF101690; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS50822; PIWI; 1.
PE 2: Evidence at transcript level;
KW Nucleus; Plant defense; Reference proteome; Repressor; Ribonucleoprotein;
KW RNA-binding; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Translation regulation.
FT CHAIN 1..878
FT /note="Protein argonaute 6"
FT /id="PRO_0000404668"
FT DOMAIN 256..372
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 541..851
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 98681 MW; 6EF8E441BD65D5E5 CRC64;
METSSSLPLS PISIEPEQPS HRDYDITTRR GVGTTGNPIE LCTNHFNVSV RQPDVVFYQY
TVSITTENGD AVDGTGISRK LMDQLFKTYS SDLDGKRLAY DGEKTLYTVG PLPQNEFDFL
VIVEGSFSKR DCGVSDGGSS SGTCKRSKRS FLPRSYKVQI HYAAEIPLKT VLGTQRGAYT
PDKSAQDALR VLDIVLRQQA AERGCLLVRQ AFFHSDGHPM KVGGGVIGIR GLHSSFRPTH
GGLSLNIDVS TTMILEPGPV IEFLKANQSV ETPRQIDWIK AAKMLKHMRV KATHRNMEFK
IIGLSSKPCN QQLFSMKIKD GEREVPIREI TVYDYFKQTY TEPISSAYFP CLDVGKPDRP
NYLPLEFCNL VSLQRYTKPL SGRQRVLLVE SSRQKPLERI KTLNDAMHTY CYDKDPFLAG
CGISIEKEMT QVEGRVLKPP MLKFGKNEDF QPCNGRWNFN NKMLLEPRAI KSWAIVNFSF
PCDSSHISRE LISCGMRKGI EIDRPFALVE EDPQYKKAGP VERVEKMIAT MKLKFPDPPH
FILCILPERK TSDIYGPWKK ICLTEEGIHT QCICPIKISD QYLTNVLLKI NSKLGGINSL
LGIEYSYNIP LINKIPTLIL GMDVSHGPPG RADVPSVAAV VGSKCWPLIS RYRAAVRTQS
PRLEMIDSLF QPIENTEKGD NGIMNELFVE FYRTSRARKP KQIIIFRDGV SESQFEQVLK
IEVDQIIKAY QRLGESDVPK FTVIVAQKNH HTKLFQAKGP ENVPAGTVVD TKIVHPTNYD
FYMCAHAGKI GTSRPAHYHV LLDEIGFSPD DLQNLIHSLS YVNQRSTTAT SIVAPVRYAH
LAAAQVAQFT KFEGISEDGK VPELPRLHEN VEGNMFFC