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AGO9_ARATH
ID   AGO9_ARATH              Reviewed;         896 AA.
AC   Q84VQ0; Q56X15; Q84YI4;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Protein argonaute 9;
GN   Name=AGO9; OrderedLocusNames=At5g21150; ORFNames=T10F18.180;
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].
RC   STRAIN=cv. Landsberg erecta; TISSUE=Anther, and Ovule;
RX   PubMed=12805595; DOI=10.1104/pp.102.017798;
RA   Scutt C.P., Vinauger-Douard M., Fourquin C., Ailhas J., Kuno N., Uchida K.,
RA   Gaude T., Furuya M., Dumas C.;
RT   "The identification of candidate genes for a reverse genetic analysis of
RT   development and function in the Arabidopsis gynoecium.";
RL   Plant Physiol. 132:653-665(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-896.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=20208518; DOI=10.1038/nature08828;
RA   Olmedo-Monfil V., Duran-Figueroa N., Arteaga-Vazquez M., Demesa-Arevalo E.,
RA   Autran D., Grimanelli D., Slotkin R.K., Martienssen R.A.,
RA   Vielle-Calzada J.P.;
RT   "Control of female gamete formation by a small RNA pathway in
RT   Arabidopsis.";
RL   Nature 464:628-632(2010).
RN   [7]
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).
RN   [8]
RP   FUNCTION.
RX   PubMed=21057207; DOI=10.4161/psb.5.11.13548;
RA   Duran-Figueroa N., Vielle-Calzada J.P.;
RT   "ARGONAUTE9-dependent silencing of transposable elements in pericentromeric
RT   regions of Arabidopsis.";
RL   Plant Signal. Behav. 5:1476-1479(2010).
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. Associates preferentially with small RNAs of 24 nucleotide
CC       in length with a 5' terminal adenosine. Interacts with 24 nucleotide
CC       sRNAs derived from transposable elements (TEs). Required to silence
CC       pericentrometric-located TEs in female gametes and their accessory
CC       cells. Necessary to inactivate a significant proportion of long
CC       terminal repeat retrotransposons (LTRs) in the ovule. Required to
CC       specify cell fate in ovule. Involved in the control of female gamete
CC       formation by restricting the specification of gametophyte precursors in
CC       a dosage-dependent, non-cell-autonomous manner. Targeted by turnip
CC       yellows virus (TuYV) protein P0 (via F-box-like domain) for probable
CC       proteasome degradation and thereby inactivating AGO9 function in RNA
CC       silencing. {ECO:0000269|PubMed:17869110, ECO:0000269|PubMed:20173091,
CC       ECO:0000269|PubMed:20208518, ECO:0000269|PubMed:21057207}.
CC   -!- TISSUE SPECIFICITY: Expressed in embryonic shoot apex region, pollen
CC       and developing ovules. {ECO:0000269|PubMed:20173091}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in all cells of the young ovule
CC       primordium at pre-meiotic stages, including the L1 layer. At early
CC       stages of female gametogenesis, expression is restricted to the distal
CC       (micropylar) portion of the developing ovule, but is absent from the 1-
CC       nuclear female gametophyte. In fully differentiated ovules, expressed
CC       at the proximal and distal poles but not in the female gametophyte.
CC       {ECO:0000269|PubMed:20208518}.
CC   -!- DISRUPTION PHENOTYPE: Differentiation of multiple gametic cells able to
CC       initiate gametogenesis. Abnormally enlarged sub-epidermal cells in
CC       developing ovules. {ECO:0000269|PubMed:20208518}.
CC   -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO73892.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ544236; CAD66636.1; -; mRNA.
DR   EMBL; AC140977; AAO73892.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED92940.1; -; Genomic_DNA.
DR   EMBL; AK221864; BAD94152.1; -; mRNA.
DR   RefSeq; NP_197613.2; NM_122122.3.
DR   AlphaFoldDB; Q84VQ0; -.
DR   SMR; Q84VQ0; -.
DR   IntAct; Q84VQ0; 1.
DR   STRING; 3702.AT5G21150.1; -.
DR   PaxDb; Q84VQ0; -.
DR   PRIDE; Q84VQ0; -.
DR   ProteomicsDB; 244664; -.
DR   EnsemblPlants; AT5G21150.1; AT5G21150.1; AT5G21150.
DR   GeneID; 832241; -.
DR   Gramene; AT5G21150.1; AT5G21150.1; AT5G21150.
DR   KEGG; ath:AT5G21150; -.
DR   Araport; AT5G21150; -.
DR   TAIR; locus:2179008; AT5G21150.
DR   eggNOG; KOG1041; Eukaryota.
DR   HOGENOM; CLU_004544_2_0_1; -.
DR   InParanoid; Q84VQ0; -.
DR   OMA; FTHVEGR; -.
DR   OrthoDB; 159407at2759; -.
DR   PhylomeDB; Q84VQ0; -.
DR   PRO; PR:Q84VQ0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q84VQ0; baseline and differential.
DR   Genevisible; Q84VQ0; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
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:1904159; P:megasporocyte differentiation; IMP:TAIR.
DR   GO; GO:0009554; P:megasporogenesis; IMP:TAIR.
DR   GO; GO:0010529; P:negative regulation of transposition; IMP:TAIR.
DR   GO; GO:0048481; P:plant ovule development; 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   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..896
FT                   /note="Protein argonaute 9"
FT                   /id="PRO_0000404671"
FT   DOMAIN          264..380
FT                   /note="PAZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT   DOMAIN          550..857
FT                   /note="Piwi"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT   CONFLICT        268
FT                   /note="V -> I (in Ref. 1; CAD66636)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        443
FT                   /note="R -> C (in Ref. 4; BAD94152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        571
FT                   /note="N -> D (in Ref. 1; CAD66636)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        616
FT                   /note="P -> T (in Ref. 4; BAD94152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        827
FT                   /note="Y -> H (in Ref. 1; CAD66636)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        871
FT                   /note="I -> M (in Ref. 4; BAD94152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        876
FT                   /note="A -> T (in Ref. 1; CAD66636)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   896 AA;  100524 MW;  F2043904C1293300 CRC64;
     MDSDEPNGSG LPPPPPFVPA NLVPEVEPVK KNILLPMARP RGSGSKGQKI PLLTNHFGVK
     FNKPSGYFFH YSVAINYEDG RPVEAKGIGR KILDKVQETY QSDLGAKYFA YDGEKTLFTV
     GALPSNKLDF SVVLEEIPSS RNHAGNDTND ADRKRSRRPN QTKKFMVEIS YAAKIPMQAI
     ASALQGKETE NLQDALRVLD IILRQSAARQ GCLLVRQSFF HNDVKNFVPI GGGVSGCRGF
     HSSFRTTQGG LSLNIDTSTT MIVQPGPVVD FLLANQNKKD PYGMDWNKAR RVLKNLRVQI
     TLSNREYKIS GLSEHSCKDQ LFTWRKPNDK GEFEEVEITV LNYYKERNIE VRYSGDFPCI
     NVGKPKRPTY FPIEFCNLVS LQRYTKSLTN FQRAALVEKS RQKPPERMAS LTKGLKDSNY
     NADPVLQDSG VSIITNFTQV EGRILPTPML KVGKGENLSP IKGKWNFMRK TLAEPTTVTR
     WAVVNFSARC DTNTLIRDLI KCGREKGINV EPPFKDVINE NPQFRNAPAT VRVENMFEQI
     KSKLPKPPLF LLCILAERKN SDVYGPWKKK NLVDLGIVTQ CIAPTRLNDQ YLTNVLLKIN
     AKLGGLNSLL AMERSPAMPK VTQVPTIIVG MDVSHGSPGQ SDIPSIAAVV SSRQWPLISK
     YKACVRTQSR KMEMIDNLFK PVNGKDEGMF RELLLDFYYS SENRKPEHII IFRDGVSESQ
     FNQVLNIELD QMMQACKFLD DTWHPKFTVI VAQKNHHTKF FQSRGPDNVP PGTIIDSQIC
     HPRNFDFYLC AHAGMIGTTR PTHYHVLYDE IGFATDDLQE LVHSLSYVYQ RSTTAISVVA
     PVCYAHLAAA QMGTVMKYEE LSETSSSHGG ITTPGAVPVP PMPQLHNNVS TSMFFC
 
 
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