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Q9VUQ5 (AGO2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein argonaute-2
Gene names
Name:AGO2
ORF Names:CG7439
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1214 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for RNA interference (RNAi); double-stranded RNA induces potent and specific gene silencing. RNAi is mediated by the RNA-induced silencing complex (RISC), a sequence-specific, multicomponent nuclease that destroys or silences messenger RNAs homologous to the silencing trigger. Ref.6

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Interacts with Fmr1 to form a ribonucleoprotein (RNP) complex involved in translation regulation, other components of the complex are mRpL5, mRpL11, Rm62 and Dcr-1. Interacts with Dcr-1 to form components of the RISC. Interacts with cricket paralysis virus protein 1A; this interaction may block the RISC activity. Ref.6 Ref.7 Ref.8

Domain

PAZ domain provides a major contribution for nucleic acid recognition. PAZ binds oligonucleotides of different lengths and has a strong preference for single-stranded nucleic acids (ssRNA or SSDNA) or RNA duplexes with single-stranded 3' overhangs. Can bind the characteristic two-base 3' overhangs of siRNAs, indicating that it may contribute to the specific and productive incorporation of siRNAs and miRNAs into the RNAi pathway.

Sequence similarities

Belongs to the argonaute family. Ago subfamily.

Contains 1 PAZ domain.

Contains 1 Piwi domain.

Sequence caution

The sequence AAM11104.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processHost-virus interaction
RNA-mediated gene silencing
   Coding sequence diversityAlternative splicing
   LigandMagnesium
Manganese
Metal-binding
RNA-binding
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA interference

Inferred from direct assay PubMed 16271385PubMed 16271386. Source: FlyBase

RNA phosphodiester bond hydrolysis, endonucleolytic

Inferred from direct assay PubMed 16271385. Source: GOC

autophagic cell death

Inferred from expression pattern PubMed 12593804. Source: FlyBase

cellularization

Inferred from mutant phenotype PubMed 16024657. Source: FlyBase

defense response to virus

Inferred from mutant phenotype PubMed 16556799PubMed 20978209PubMed 21957285. Source: FlyBase

dosage compensation by hyperactivation of X chromosome

Inferred from genetic interaction PubMed 22554892. Source: FlyBase

dsRNA transport

Inferred from mutant phenotype PubMed 16862146. Source: FlyBase

heterochromatin organization involved in chromatin silencing

Inferred from mutant phenotype PubMed 19948966. Source: FlyBase

negative regulation of viral genome replication

Inferred from mutant phenotype PubMed 19632183. Source: FlyBase

pole cell formation

Inferred from mutant phenotype PubMed 16024657. Source: FlyBase

production of siRNA involved in RNA interference

Inferred from direct assay Ref.6. Source: UniProtKB

salivary gland cell autophagic cell death

Inferred from expression pattern PubMed 12593804. Source: FlyBase

segment polarity determination

Inferred from genetic interaction PubMed 16934003. Source: FlyBase

siRNA loading onto RISC involved in RNA interference

Inferred from direct assay PubMed 17123955. Source: FlyBase

syncytial nuclear migration

Inferred from mutant phenotype PubMed 16024657. Source: FlyBase

targeting of mRNA for destruction involved in RNA interference

Traceable author statement PubMed 12011447. Source: FlyBase

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentRISC complex

Inferred from direct assay Ref.6PubMed 17123955PubMed 19661431. Source: FlyBase

RISC-loading complex

Inferred from direct assay PubMed 17123955. Source: FlyBase

cytoplasm

Inferred from direct assay PubMed 19252745. Source: FlyBase

   Molecular_functionendoribonuclease activity

Inferred from direct assay PubMed 16271385. Source: FlyBase

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

siRNA binding

Inferred from direct assay Ref.10PubMed 16271385PubMed 18463636. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Fmr1Q9NFU04EBI-442476,EBI-422631

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform B Ref.1 (identifier: Q9VUQ5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform C Ref.1 (identifier: Q9VUQ5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MGKKDK → MHFPITTPE
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12141214Protein argonaute-2
PRO_0000194071

Regions

Domain608 – 717110PAZ
Domain885 – 1186302Piwi
Region681 – 6866Interaction with guide RNA Potential
Region1075 – 10762Interaction with guide RNA Potential
Region1119 – 11279Interaction with guide RNA Potential
Region1156 – 117823Interaction with guide RNA Potential
Compositional bias19 – 391373Gln/Gly-rich

Sites

Metal binding9651Divalent metal cation By similarity
Metal binding10371Divalent metal cation By similarity
Metal binding11731Divalent metal cation By similarity

Natural variations

Alternative sequence1 – 66MGKKDK → MHFPITTPE in isoform C.
VSP_050781
Natural variant7141S → R in strain: 186. Ref.4
Natural variant7401S → P in strain: 130. Ref.4
Natural variant7831S → N in strain: 138, 140 and 196. Ref.4 Ref.5
Natural variant8351T → A in strain: 128, 130, 138, 140, 141, 186, 187 and 196. Ref.4 Ref.5
Natural variant8541S → T in strain: 128, 130, 138, 140, 141, 186, 187 and 196. Ref.4 Ref.5
Natural variant8661D → E in strain: 128, 130, 141, 186 and 187. Ref.4

Experimental info

Sequence conflict2011G → D in AAO39550. Ref.3

Secondary structure

............................... 1214
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform B [UniParc].

Last modified August 16, 2004. Version 3.
Checksum: 0DC73AF09CC33F73

FASTA1,214136,850
        10         20         30         40         50         60 
MGKKDKNKKG GQDSAAAPQP QQQQKQQQQR QQQPQQLQQP QQLQQPQQLQ QPQQQQQQQP 

        70         80         90        100        110        120 
HQQQQQSSRQ QPSTSSGGSR ASGFQQGGQQ QKSQDAEGWT AQKKQGKQQV QGWTKQGQQG 

       130        140        150        160        170        180 
GHQQGRQGQD GGYQQRPPGQ QQGGHQQGRQ GQEGGYQQRP PGQQQGGHQQ GRQGQEGGYQ 

       190        200        210        220        230        240 
QRPSGQQQGG HQQGRQGQEG GYQQRPPGQQ QGGHQQGRQG QEGGYQQRPS GQQQGGHQQG 

       250        260        270        280        290        300 
RQGQEGGYQQ RPPGQQQGGH QQGRQGQEGG YQQRPPGQQQ GGHEQGRQGQ EGGYQQRPSG 

       310        320        330        340        350        360 
QQQGGHQQGR QGQEGGYQQR PSGQQQGGHQ QGRQGQEGGY QQRPSGQQQG GHQQGRQGQE 

       370        380        390        400        410        420 
GGYQQRPPGQ QPNQTQSQGQ YQSRGPPQQQ QAAPLPLPPQ PAGSIKRGTI GKPGQVGINY 

       430        440        450        460        470        480 
LDLDLSKMPS VAYHYDVKIM PERPKKFYRQ AFEQFRVDQL GGAVLAYDGK ASCYSVDKLP 

       490        500        510        520        530        540 
LNSQNPEVTV TDRNGRTLRY TIEIKETGDS TIDLKSLTTY MNDRIFDKPM RAMQCVEVVL 

       550        560        570        580        590        600 
ASPCHNKAIR VGRSFFKMSD PNNRHELDDG YEALVGLYQA FMLGDRPFLN VDISHKSFPI 

       610        620        630        640        650        660 
SMPMIEYLER FSLKAKINNT TNLDYSRRFL EPFLRGINVV YTPPQSFQSA PRVYRVNGLS 

       670        680        690        700        710        720 
RAPASSETFE HDGKKVTIAS YFHSRNYPLK FPQLHCLNVG SSIKSILLPI ELCSIEEGQA 

       730        740        750        760        770        780 
LNRKDGATQV ANMIKYAATS TNVRKRKIMN LLQYFQHNLD PTISRFGIRI ANDFIVVSTR 

       790        800        810        820        830        840 
VLSPPQVEYH SKRFTMVKNG SWRMDGMKFL EPKPKAHKCA VLYCDPRSGR KMNYTQLNDF 

       850        860        870        880        890        900 
GNLIISQGKA VNISLDSDVT YRPFTDDERS LDTIFADLKR SQHDLAIVII PQFRISYDTI 

       910        920        930        940        950        960 
KQKAELQHGI LTQCIKQFTV ERKCNNQTIG NILLKINSKL NGINHKIKDD PRLPMMKNTM 

       970        980        990       1000       1010       1020 
YIGADVTHPS PDQREIPSVV GVAASHDPYG ASYNMQYRLQ RGALEEIEDM FSITLEHLRV 

      1030       1040       1050       1060       1070       1080 
YKEYRNAYPD HIIYYRDGVS DGQFPKIKNE ELRCIKQACD KVGCKPKICC VIVVKRHHTR 

      1090       1100       1110       1120       1130       1140 
FFPSGDVTTS NKFNNVDPGT VVDRTIVHPN EMQFFMVSHQ AIQGTAKPTR YNVIENTGNL 

      1150       1160       1170       1180       1190       1200 
DIDLLQQLTY NLCHMFPRCN RSVSYPAPAY LAHLVAARGR VYLTGTNRFL DLKKEYAKRT 

      1210 
IVPEFMKKNP MYFV 

« Hide

Isoform C [UniParc].

Checksum: 7C794ABF4D993EAF
Show »

FASTA1,217137,216

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[3]Stapleton M., Brokstein P., Hong L., Agbayani A., Booth B., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G. expand/collapse author list , Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
Strain: Berkeley.
Tissue: Embryo.
[4]"Natural selection drives extremely rapid evolution in antiviral RNAi genes."
Obbard D.J., Jiggins F.M., Halligan D.L., Little T.J.
Curr. Biol. 16:580-585(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-1214, VARIANTS ARG-714; PRO-740; ASN-783; ALA-835; THR-854 AND GLU-866.
Strain: 128, 130, 138, 140, 141, 186, 187 and 196.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 449-1214, VARIANTS ASN-783; ALA-835 AND THR-854.
Strain: Berkeley.
Tissue: Ovary.
[6]"Argonaute2, a link between genetic and biochemical analyses of RNAi."
Hammond S.M., Boettcher S., Caudy A.A., Kobayashi R., Hannon G.J.
Science 293:1146-1150(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 506-515; 525-531; 554-557; 617-627; 662-674; 809-815 AND 1181-1188 (ISOFORM B), FUNCTION, INTERACTION WITH DCR-1.
[7]"A Drosophila fragile X protein interacts with components of RNAi and ribosomal proteins."
Ishizuka A., Siomi M.C., Siomi H.
Genes Dev. 16:2497-2508(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FMR1.
[8]"Cricket paralysis virus antagonizes Argonaute 2 to modulate antiviral defense in Drosophila."
Nayak A., Berry B., Tassetto M., Kunitomi M., Acevedo A., Deng C., Krutchinsky A., Gross J., Antoniewski C., Andino R.
Nat. Struct. Mol. Biol. 17:547-554(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRICKET PARALYSIS VIRUS PROTEIN 1A.
[9]"The crystal structure of the Argonaute2 PAZ domain reveals an RNA binding motif in RNAi effector complexes."
Song J.J., Liu J., Tolia N.H., Schneiderman J., Smith S.K., Martienssen R.A., Hannon G.J., Joshua-Tor L.
Nat. Struct. Biol. 10:1026-1032(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 591-726.
[10]"Structure and nucleic-acid binding of the Drosophila Argonaute 2 PAZ domain."
Lingel A., Simon B., Izaurralde E., Sattler M.
Nature 426:465-469(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 602-740.
[11]"Nucleic acid 3'-end recognition by the Argonaute2 PAZ domain."
Lingel A., Simon B., Izaurralde E., Sattler M.
Nat. Struct. Mol. Biol. 11:576-577(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 605-720.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014296 Genomic DNA. Translation: AAF49619.2.
AE014296 Genomic DNA. Translation: AAF49620.2.
BT003546 mRNA. Translation: AAO39550.1.
BT099682 mRNA. Translation: ACV44468.1.
DQ228766 Genomic DNA. Translation: ABB54719.1.
DQ228767 Genomic DNA. Translation: ABB54720.1.
DQ228768 Genomic DNA. Translation: ABB54721.1.
DQ228769 Genomic DNA. Translation: ABB54722.1.
DQ228770 Genomic DNA. Translation: ABB54723.1.
DQ228771 Genomic DNA. Translation: ABB54724.1.
DQ228772 Genomic DNA. Translation: ABB54725.1.
DQ228773 Genomic DNA. Translation: ABB54726.1.
AY094751 mRNA. Translation: AAM11104.1. Different initiation.
RefSeqNP_648775.1. NM_140518.3. [Q9VUQ5-1]
NP_730054.1. NM_168626.3. [Q9VUQ5-2]
UniGeneDm.9677.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R6ZX-ray2.80A/P/Z589-726[»]
1T2RNMR-A602-720[»]
1T2SNMR-A602-720[»]
1VYNNMR-A602-740[»]
3MJ0X-ray2.31A601-723[»]
ProteinModelPortalQ9VUQ5.
SMRQ9VUQ5. Positions 591-719.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid65002. 9 interactions.
DIPDIP-41570N.
IntActQ9VUQ5. 7 interactions.
MINTMINT-248245.

Proteomic databases

PaxDbQ9VUQ5.
PRIDEQ9VUQ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0075559; FBpp0075312; FBgn0087035. [Q9VUQ5-1]
GeneID39683.
KEGGdme:Dmel_CG7439.

Organism-specific databases

CTD27161.
FlyBaseFBgn0087035. AGO2.

Phylogenomic databases

eggNOGNOG279895.
GeneTreeENSGT00640000091312.
InParanoidQ9VUQ5.
KOK11593.
OMAQGQEGGY.
OrthoDBEOG722J7S.
PhylomeDBQ9VUQ5.

Gene expression databases

BgeeQ9VUQ5.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
InterProIPR014811. DUF1785.
IPR003100. PAZ_dom.
IPR003165. Piwi.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamPF08699. DUF1785. 1 hit.
PF02170. PAZ. 1 hit.
PF02171. Piwi. 1 hit.
[Graphical view]
SMARTSM00950. Piwi. 1 hit.
[Graphical view]
SUPFAMSSF101690. SSF101690. 1 hit.
SSF53098. SSF53098. 1 hit.
PROSITEPS50821. PAZ. 1 hit.
PS50822. PIWI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9VUQ5.
GenomeRNAi39683.
NextBio814859.

Entry information

Entry nameAGO2_DROME
AccessionPrimary (citable) accession number: Q9VUQ5
Secondary accession number(s): C7LAD2 expand/collapse secondary AC list , Q2Q3Y0, Q2Q3Y1, Q2Q3Y3, Q2Q3Y4, Q2Q3Y5, Q86P07, Q8T3N2, Q9VUQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase