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AGO3_ARATH
ID   AGO3_ARATH              Reviewed;        1194 AA.
AC   Q9SHF2;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Protein argonaute 3;
GN   Name=AGO3; OrderedLocusNames=At1g31290; ORFNames=T19E23.8;
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).
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AC007654; AAF24586.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31336.1; -; Genomic_DNA.
DR   RefSeq; NP_174414.1; NM_102867.2.
DR   AlphaFoldDB; Q9SHF2; -.
DR   SMR; Q9SHF2; -.
DR   STRING; 3702.AT1G31290.1; -.
DR   PaxDb; Q9SHF2; -.
DR   PRIDE; Q9SHF2; -.
DR   ProteomicsDB; 244773; -.
DR   EnsemblPlants; AT1G31290.1; AT1G31290.1; AT1G31290.
DR   GeneID; 840017; -.
DR   Gramene; AT1G31290.1; AT1G31290.1; AT1G31290.
DR   KEGG; ath:AT1G31290; -.
DR   Araport; AT1G31290; -.
DR   TAIR; locus:2197550; AT1G31290.
DR   eggNOG; KOG1041; Eukaryota.
DR   HOGENOM; CLU_004544_3_0_1; -.
DR   InParanoid; Q9SHF2; -.
DR   OrthoDB; 220258at2759; -.
DR   PhylomeDB; Q9SHF2; -.
DR   PRO; PR:Q9SHF2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SHF2; baseline and differential.
DR   Genevisible; Q9SHF2; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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   3: Inferred from homology;
KW   Plant defense; Reference proteome; Repressor; Ribonucleoprotein;
KW   RNA-binding; RNA-mediated gene silencing; Transcription;
KW   Transcription regulation; Translation regulation.
FT   CHAIN           1..1194
FT                   /note="Protein argonaute 3"
FT                   /id="PRO_0000404666"
FT   DOMAIN          540..656
FT                   /note="PAZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT   DOMAIN          841..1145
FT                   /note="Piwi"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT   REGION          1..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1194 AA;  129185 MW;  930E52C6CDBE2AB2 CRC64;
     MDRGGYRGGR GDGRGRGGGG DRGRGYSGRG DGRGRGGDGD RGYSGRGDGH GRGGGGDRGR
     GYSGRGDGRG RGGGGDRGRG YSGRGDGHGR GGGGDRGRGY SGRGRGFVQD RDGGWVNPGQ
     SSGGHVRGRG TQLQQPPPQE VPPSSSQAQV SQGVAPGDVG QGGVGDVGRD GVGDVGRDGV
     GDVGQGGVGD VGQVGVGDVG QGGVGDVGQG GVGDVGRDGV GDVGRDGVGD VGRGGVGDRG
     QSQSGLSSGH FGRGTQLQQP QPQAVSQSSS QGQVSQSFAT GGVGLGAWAR KPQLFSDSTV
     LPSSSSSNVV ASHTASGSQV MTPKPSSSDK KEPVKRPDKG GNIKVKGVIN LSVNHFRVSF
     STESVIRHYD VDIKGENSSK KISRFELAMV KEKLFKDNND FPNAMTAYDG QKNIFSAVEL
     PTGSFKVDFS ETEEIMRGRS YTFIIKQVKE LKLLDLQAYI DGRSTFIPRD VLQGMDVVMK
     EHPSKRMITV GKRFFSTRLE IDFGYGVGAA KGFHHTLKPT VQGLSLCLNS SLLAFRKAIS
     VIEYLKLYFG WRNIRQFKNC RPDDVVQELI GLKVTVDHRK TKQKFIIMGL SKDDTKDIKF
     DFIDHAGNQP PRKISIVEYF KEKYGRDIDH KDIPCLNLGK KGRENFVPME FCNLVEGQIF
     PKEKLYRDSA AWLKELSLVT PQQRLENINK MIKSSDGPRG GDIIGNFGLR VDPNMTTVEG
     RVLEAPTLKL TDRRGNPIHE KLMSESNQWN LTTKGVTKGS IIKHWAVLDF TASESLKKKM
     PGYFVNKLIE RCKGLGMQME APIVCKTSSM ETLYDGNALE ELLRSVIDEA SHNHGGACPT
     LVLCAMTGKH DGYKTLKWIA ETKLGLVTQC FLTISAIKGE TVSDQYLANL ALKINAKVGG
     TNVELVDNIF SFFKKEDKVM FIGADVNHPA AHDNMSPSIV AVVGTLNWPE ANRYAARVKA
     QSHRKEEIQG FGETCWELIE AHSQAPEKRP NKIVIFRDGV SDGQFDMVLN VELQNVKDVF
     AKVGYNPQIT VIVAQKRHQT RFFPATTSKD GRAKGNVPSG TVVDTTIIHP FEYDFYLCSQ
     HGAIGTSKPT HYYVLSDEIG FNSNQIQKLI FDLCFTFTRC TKPVALVPPV SYADKAASRG
     RVYYEASLMK KNSKQSRGAS SSSASVASSS SSVTMEDKEI FKVHAGIENF MFFV
 
 
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