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Protein

Protein argonaute-2

Gene

AGO2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.1 Publication

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi965Divalent metal cationBy similarity1
Metal bindingi1037Divalent metal cationBy similarity1
Metal bindingi1173Divalent metal cationBy similarity1

GO - Molecular functioni

  • endoribonuclease activity Source: FlyBase
  • metal ion binding Source: UniProtKB-KW
  • siRNA binding Source: FlyBase

GO - Biological processi

  • cellularization Source: FlyBase
  • cellular response to virus Source: FlyBase
  • defense response to virus Source: FlyBase
  • dosage compensation by hyperactivation of X chromosome Source: FlyBase
  • dsRNA transport Source: FlyBase
  • gene silencing by miRNA Source: FlyBase
  • heterochromatin organization involved in chromatin silencing Source: FlyBase
  • negative regulation of transposition, RNA-mediated Source: FlyBase
  • negative regulation of viral genome replication Source: FlyBase
  • pole cell formation Source: FlyBase
  • production of siRNA involved in RNA interference Source: UniProtKB
  • RNA interference Source: FlyBase
  • segment polarity determination Source: FlyBase
  • siRNA loading onto RISC involved in RNA interference Source: FlyBase
  • syncytial nuclear migration Source: FlyBase
  • targeting of mRNA for destruction involved in RNA interference Source: FlyBase
  • viral process Source: UniProtKB-KW

Keywordsi

Molecular functionRNA-binding
Biological processHost-virus interaction, RNA-mediated gene silencing
LigandMagnesium, Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein argonaute-2
Gene namesi
Name:AGO2Imported
ORF Names:CG7439
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0087035 AGO2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001940711 – 1214Protein argonaute-2Add BLAST1214

Proteomic databases

PaxDbiQ9VUQ5
PRIDEiQ9VUQ5

Expressioni

Gene expression databases

BgeeiFBgn0087035
ExpressionAtlasiQ9VUQ5 baseline and differential
GenevisibleiQ9VUQ5 DM

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi65002, 49 interactors
DIPiDIP-41570N
IntActiQ9VUQ5, 32 interactors
MINTiQ9VUQ5
STRINGi7227.FBpp0075313

Structurei

Secondary structure

11214
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi601 – 603Combined sources3
Helixi604 – 611Combined sources8
Beta strandi618 – 621Combined sources4
Helixi623 – 625Combined sources3
Helixi627 – 634Combined sources8
Beta strandi638 – 641Combined sources4
Helixi645 – 647Combined sources3
Beta strandi652 – 655Combined sources4
Beta strandi658 – 663Combined sources6
Turni664 – 666Combined sources3
Beta strandi668 – 677Combined sources10
Helixi678 – 683Combined sources6
Turni684 – 686Combined sources3
Beta strandi692 – 698Combined sources7
Beta strandi705 – 708Combined sources4
Helixi710 – 712Combined sources3
Beta strandi713 – 716Combined sources4
Turni717 – 719Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R6ZX-ray2.80A/P/Z589-726[»]
1T2RNMR-A602-720[»]
1T2SNMR-A602-720[»]
1VYNNMR-A602-740[»]
3MJ0X-ray2.31A601-723[»]
ProteinModelPortaliQ9VUQ5
SMRiQ9VUQ5
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9VUQ5

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini608 – 717PAZPROSITE-ProRule annotationAdd BLAST110
Domaini885 – 1186PiwiPROSITE-ProRule annotationAdd BLAST302

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni681 – 686Interaction with guide RNASequence analysis6
Regioni1075 – 1076Interaction with guide RNASequence analysis2
Regioni1119 – 1127Interaction with guide RNASequence analysis9
Regioni1156 – 1178Interaction with guide RNASequence analysisAdd BLAST23

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi19 – 391Gln/Gly-richAdd BLAST373

Domaini

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 similaritiesi

Belongs to the argonaute family. Ago subfamily.Curated

Phylogenomic databases

eggNOGiKOG1041 Eukaryota
ENOG410XP07 LUCA
GeneTreeiENSGT00760000119148
InParanoidiQ9VUQ5
KOiK11593
OrthoDBiEOG091G020J
PhylomeDBiQ9VUQ5

Family and domain databases

Gene3Di3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR014811 ArgoL1
IPR032472 ArgoL2
IPR032473 Argonaute_Mid_dom
IPR032474 Argonaute_N
IPR003100 PAZ_dom
IPR036085 PAZ_dom_sf
IPR003165 Piwi
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
PfamiView protein in Pfam
PF08699 ArgoL1, 1 hit
PF16488 ArgoL2, 1 hit
PF16487 ArgoMid, 1 hit
PF16486 ArgoN, 1 hit
PF02170 PAZ, 1 hit
PF02171 Piwi, 1 hit
SMARTiView protein in SMART
SM01163 DUF1785, 1 hit
SM00950 Piwi, 1 hit
SUPFAMiSSF101690 SSF101690, 1 hit
SSF53098 SSF53098, 1 hit
PROSITEiView protein in PROSITE
PS50821 PAZ, 1 hit
PS50822 PIWI, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform B (identifier: Q9VUQ5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGKKDKNKKG GQDSAAAPQP QQQQKQQQQR QQQPQQLQQP QQLQQPQQLQ
60 70 80 90 100
QPQQQQQQQP HQQQQQSSRQ QPSTSSGGSR ASGFQQGGQQ QKSQDAEGWT
110 120 130 140 150
AQKKQGKQQV QGWTKQGQQG GHQQGRQGQD GGYQQRPPGQ QQGGHQQGRQ
160 170 180 190 200
GQEGGYQQRP PGQQQGGHQQ GRQGQEGGYQ QRPSGQQQGG HQQGRQGQEG
210 220 230 240 250
GYQQRPPGQQ QGGHQQGRQG QEGGYQQRPS GQQQGGHQQG RQGQEGGYQQ
260 270 280 290 300
RPPGQQQGGH QQGRQGQEGG YQQRPPGQQQ GGHEQGRQGQ EGGYQQRPSG
310 320 330 340 350
QQQGGHQQGR QGQEGGYQQR PSGQQQGGHQ QGRQGQEGGY QQRPSGQQQG
360 370 380 390 400
GHQQGRQGQE GGYQQRPPGQ QPNQTQSQGQ YQSRGPPQQQ QAAPLPLPPQ
410 420 430 440 450
PAGSIKRGTI GKPGQVGINY LDLDLSKMPS VAYHYDVKIM PERPKKFYRQ
460 470 480 490 500
AFEQFRVDQL GGAVLAYDGK ASCYSVDKLP LNSQNPEVTV TDRNGRTLRY
510 520 530 540 550
TIEIKETGDS TIDLKSLTTY MNDRIFDKPM RAMQCVEVVL ASPCHNKAIR
560 570 580 590 600
VGRSFFKMSD PNNRHELDDG YEALVGLYQA FMLGDRPFLN VDISHKSFPI
610 620 630 640 650
SMPMIEYLER FSLKAKINNT TNLDYSRRFL EPFLRGINVV YTPPQSFQSA
660 670 680 690 700
PRVYRVNGLS RAPASSETFE HDGKKVTIAS YFHSRNYPLK FPQLHCLNVG
710 720 730 740 750
SSIKSILLPI ELCSIEEGQA LNRKDGATQV ANMIKYAATS TNVRKRKIMN
760 770 780 790 800
LLQYFQHNLD PTISRFGIRI ANDFIVVSTR VLSPPQVEYH SKRFTMVKNG
810 820 830 840 850
SWRMDGMKFL EPKPKAHKCA VLYCDPRSGR KMNYTQLNDF GNLIISQGKA
860 870 880 890 900
VNISLDSDVT YRPFTDDERS LDTIFADLKR SQHDLAIVII PQFRISYDTI
910 920 930 940 950
KQKAELQHGI LTQCIKQFTV ERKCNNQTIG NILLKINSKL NGINHKIKDD
960 970 980 990 1000
PRLPMMKNTM YIGADVTHPS PDQREIPSVV GVAASHDPYG ASYNMQYRLQ
1010 1020 1030 1040 1050
RGALEEIEDM FSITLEHLRV YKEYRNAYPD HIIYYRDGVS DGQFPKIKNE
1060 1070 1080 1090 1100
ELRCIKQACD KVGCKPKICC VIVVKRHHTR FFPSGDVTTS NKFNNVDPGT
1110 1120 1130 1140 1150
VVDRTIVHPN EMQFFMVSHQ AIQGTAKPTR YNVIENTGNL DIDLLQQLTY
1160 1170 1180 1190 1200
NLCHMFPRCN RSVSYPAPAY LAHLVAARGR VYLTGTNRFL DLKKEYAKRT
1210
IVPEFMKKNP MYFV
Length:1,214
Mass (Da):136,850
Last modified:August 16, 2004 - v3
Checksum:i0DC73AF09CC33F73
GO
Isoform C (identifier: Q9VUQ5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MGKKDK → MHFPITTPE

Note: No experimental confirmation available.
Show »
Length:1,217
Mass (Da):137,216
Checksum:i7C794ABF4D993EAF
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti201G → D in AAO39550 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti714S → R in strain: 186. 1 Publication1
Natural varianti740S → P in strain: 130. 1 Publication1
Natural varianti783S → N in strain: 138, 140 and 196. 2 Publications1
Natural varianti835T → A in strain: 128, 130, 138, 140, 141, 186, 187 and 196. 2 Publications1
Natural varianti854S → T in strain: 128, 130, 138, 140, 141, 186, 187 and 196. 2 Publications1
Natural varianti866D → E in strain: 128, 130, 141, 186 and 187. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0507811 – 6MGKKDK → MHFPITTPE in isoform C. 1 Publication6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_648775.1, NM_140518.3 [Q9VUQ5-1]
NP_730054.1, NM_168626.3 [Q9VUQ5-2]
UniGeneiDm.9677

Genome annotation databases

EnsemblMetazoaiFBtr0075559; FBpp0075312; FBgn0087035 [Q9VUQ5-1]
FBtr0075560; FBpp0075313; FBgn0087035 [Q9VUQ5-2]
GeneIDi39683
KEGGidme:Dmel_CG7439

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiAGO2_DROME
AccessioniPrimary (citable) accession number: Q9VUQ5
Secondary accession number(s): C7LAD2
, Q2Q3Y0, Q2Q3Y1, Q2Q3Y3, Q2Q3Y4, Q2Q3Y5, Q86P07, Q8T3N2, Q9VUQ6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: May 23, 2018
This is version 139 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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