AGO7_ARATH
ID AGO7_ARATH Reviewed; 990 AA.
AC Q9C793;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protein argonaute 7;
DE AltName: Full=Protein ZIPPY;
GN Name=AGO7; Synonyms=ZIP; OrderedLocusNames=At1g69440; ORFNames=F10D13.11;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=14521841; DOI=10.1016/j.cub.2003.09.004;
RA Hunter C., Sun H., Poethig R.S.;
RT "The Arabidopsis heterochronic gene ZIPPY is an ARGONAUTE family member.";
RL Curr. Biol. 13:1734-1739(2003).
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 FUNCTION.
RX PubMed=16682354; DOI=10.1016/j.cub.2006.03.035;
RA Adenot X., Elmayan T., Lauressergues D., Boutet S., Bouche N.,
RA Gasciolli V., Vaucheret H.;
RT "DRB4-dependent TAS3 trans-acting siRNAs control leaf morphology through
RT AGO7.";
RL Curr. Biol. 16:927-932(2006).
RN [5]
RP FUNCTION.
RX PubMed=16682355; DOI=10.1016/j.cub.2006.03.064;
RA Garcia D., Collier S.A., Byrne M.E., Martienssen R.A.;
RT "Specification of leaf polarity in Arabidopsis via the trans-acting siRNA
RT pathway.";
RL Curr. Biol. 16:933-938(2006).
RN [6]
RP FUNCTION.
RX PubMed=16818444; DOI=10.1242/dev.02491;
RA Hunter C., Willmann M.R., Wu G., Yoshikawa M., de la Luz Gutierrez-Nava M.,
RA Poethig S.R.;
RT "Trans-acting siRNA-mediated repression of ETTIN and ARF4 regulates
RT heteroblasty in Arabidopsis.";
RL Development 133:2973-2981(2006).
RN [7]
RP FUNCTION.
RX PubMed=16699177; DOI=10.1093/pcp/pcj057;
RA Xu L., Yang L., Pi L., Liu Q., Ling Q., Wang H., Poethig R.S., Huang H.;
RT "Genetic interaction between the AS1-AS2 and RDR6-SGS3-AGO7 pathways for
RT leaf morphogenesis.";
RL Plant Cell Physiol. 47:853-863(2006).
RN [8]
RP FUNCTION.
RX PubMed=18003861; DOI=10.1101/gad.1595107;
RA Katiyar-Agarwal S., Gao S., Vivian-Smith A., Jin H.;
RT "A novel class of bacteria-induced small RNAs in Arabidopsis.";
RL Genes Dev. 21:3123-3134(2007).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [10]
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).
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 a 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. Required for the processing of 21 nucleotide trans-acting
CC siRNAs (ta-siRNAs) derived from TAS3a transcripts. Associates
CC preferentially with the microRNA (miRNA) miR390 which guides the
CC cleavage of TAS3 precursor RNA. Seems to act as miR390 specific slicer.
CC Associates mainly with small RNAs of 21 nucleotide in length and with a
CC 5' terminal adenosine. Acts in the RDR6/SGS3/DCL4/AGO7 trans-acting
CC siRNA pathway involved in leaf developmental timing. Does not seems to
CC act on leaf polarity. Required for the production of the 30-40nt
CC bacterial-induced long siRNAs (lsiRNA). Involved in antiviral RNA
CC silencing by contributing to efficient viral RNAs clearance. Targets
CC less structured viral RNAs than AGO1 which is capable of targeting RNAs
CC with more compact structures. {ECO:0000269|PubMed:14521841,
CC ECO:0000269|PubMed:16682354, ECO:0000269|PubMed:16682355,
CC ECO:0000269|PubMed:16699177, ECO:0000269|PubMed:16818444,
CC ECO:0000269|PubMed:18003861, ECO:0000269|PubMed:18342362,
CC ECO:0000269|PubMed:18799732}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and floral buds, and at low
CC levels in roots. {ECO:0000269|PubMed:18342362}.
CC -!- DISRUPTION PHENOTYPE: First leaves are elongated and curl downward.
CC Increased number of hydathodes per leaf. Accelerated appearance of
CC abaxial trichomes. Presence of stigmatic tissue in the middle of the
CC septum at the apical end of the carpels. {ECO:0000269|PubMed:14521841}.
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000305}.
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DR EMBL; AC073178; AAG60096.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34925.1; -; Genomic_DNA.
DR EMBL; AY394564; AAQ92355.1; -; mRNA.
DR RefSeq; NP_177103.1; NM_105611.5.
DR AlphaFoldDB; Q9C793; -.
DR SMR; Q9C793; -.
DR STRING; 3702.AT1G69440.1; -.
DR iPTMnet; Q9C793; -.
DR PaxDb; Q9C793; -.
DR PRIDE; Q9C793; -.
DR ProteomicsDB; 244836; -.
DR EnsemblPlants; AT1G69440.1; AT1G69440.1; AT1G69440.
DR GeneID; 843276; -.
DR Gramene; AT1G69440.1; AT1G69440.1; AT1G69440.
DR KEGG; ath:AT1G69440; -.
DR Araport; AT1G69440; -.
DR TAIR; locus:2007111; AT1G69440.
DR eggNOG; KOG1041; Eukaryota.
DR HOGENOM; CLU_004544_0_1_1; -.
DR InParanoid; Q9C793; -.
DR OMA; MNWPSAN; -.
DR OrthoDB; 220258at2759; -.
DR PhylomeDB; Q9C793; -.
DR PRO; PR:Q9C793; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C793; baseline and differential.
DR Genevisible; Q9C793; AT.
DR GO; GO:0005737; C:cytoplasm; 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:0051607; P:defense response to virus; IDA:TAIR.
DR GO; GO:0010599; P:lsiRNA processing; IMP:TAIR.
DR GO; GO:0010492; P:maintenance of shoot apical meristem identity; IEA:EnsemblPlants.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; TAS:TAIR.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IBA:GO_Central.
DR GO; GO:0040034; P:regulation of development, heterochronic; IMP:TAIR.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0010267; P:ta-siRNA processing; IMP:TAIR.
DR GO; GO:0010050; P:vegetative phase change; IMP:TAIR.
DR CDD; cd04657; Piwi_ago-like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR014811; ArgoL1.
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; 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 2: Evidence at transcript level;
KW Plant defense; Reference proteome; Repressor; Ribonucleoprotein;
KW RNA-binding; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Translation regulation.
FT CHAIN 1..990
FT /note="Protein argonaute 7"
FT /id="PRO_0000404669"
FT DOMAIN 375..484
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 649..950
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 990 AA; 113397 MW; 8C3A270FA7E51D9D CRC64;
MEEKTHHHHH STNKHIPSSK SRTPLLHKPY HHHVQTNPPP FLLHPSSHQN LNLVASNLPS
SYYYYYYCYF YSQFHNSLPP PPPPHLLPLS PPLPPLLPLP PPHSMTRFHK SLPVSQVVER
KQQHQQKKKI QVSNNKVSGS IAIEEAALVV AKRPDFGGQD GSVIYLLANH FLVKFDSSQR
IYHYNVEISP QPSKEIARMI KQKLVETDRN SFSGVVPAFD GRQNIYSPVE FQGDRLEFFV
NLPIPSCKAV MNYGDLREKQ PQKKIEKLFR VNMKLVSKFD GKEQRKEGED WAPLPPEYIH
ALDVILRENP MEKCTSIGRS FYSSSMGGSK EIGGGAVGLR GFFQSLRHTQ QGLALNMDLS
ITAFHESIGV IAYLQKRLEF LTDLPRNKGR ELSLEEKREV EKALKNIRVF VCHRETVQRY
RVYGLTEEIT ENIWFPDREG KYLRLMSYFK DHYGYEIQFK NLPCLQISRA RPCYLPMELC
MICEGQKFLG KLSDDQAAKI MKMGCQKPNE RKAIIDKVMT GSVGPSSGNQ TREFNLEVSR
EMTLLKGRIL QPPKLKLDRP RNLKESKVFK GTRIERWALM SIGGSSDQKS TIPKFINELT
QKCEHLGVFL SKNTLSSTFF EPSHILNNIS LLESKLKEIQ RAASNNLQLI ICVMEKKHKG
YGDLKRISET RIGVVTQCCL YPNITKLSSQ FVSNLALKIN AKIGGSMTEL YNSIPSHIPR
LLRPDEPVIF MGADVTHPHP FDDCSPSVAA VVGSINWPEA NRYVSRMRSQ THRQEIIQDL
DLMVKELLDD FYKAVKKLPN RIIFFRDGVS ETQFKKVLQE ELQSIKTACS KFQDYNPSIT
FAVVQKRHHT RLFRCDPDHE NIPPGTVVDT VITHPKEFDF YLCSHLGVKG TSRPTHYHIL
WDENEFTSDE LQRLVYNLCY TFVRCTKPIS IVPPAYYAHL AAYRGRLYIE RSSESNGGSM
NPSSVSRVGP PKTIPLPKLS DNVKNLMFYC
