AGO3_DANRE
ID AGO3_DANRE Reviewed; 860 AA.
AC A3KPK0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein argonaute-3 {ECO:0000255|HAMAP-Rule:MF_03032};
DE Short=Argonaute3 {ECO:0000255|HAMAP-Rule:MF_03032};
DE EC=3.1.26.n2 {ECO:0000250|UniProtKB:Q9H9G7};
DE AltName: Full=Argonaute RISC catalytic component 3;
DE AltName: Full=Eukaryotic translation initiation factor 2C 3 {ECO:0000255|HAMAP-Rule:MF_03032};
DE Short=eIF-2C 3 {ECO:0000255|HAMAP-Rule:MF_03032};
DE Short=eIF2C 3 {ECO:0000255|HAMAP-Rule:MF_03032};
GN Name=ago3; Synonyms=eif2c3; ORFNames=si:dkey-3n22.3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds to
CC short RNAs such as microRNAs (miRNAs) and represses the translation of
CC mRNAs which are complementary to them. Possesses RNA slicer activity
CC but only on select RNAs bearing 5'- and 3'-flanking sequences to the
CC region of guide-target complementarity. {ECO:0000255|HAMAP-
CC Rule:MF_03032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=endonucleolytic cleavage to 5'-phosphomonoester.;
CC EC=3.1.26.n2; Evidence={ECO:0000250|UniProtKB:Q9H9G7};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
CC Rule:MF_03032}.
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03032}.
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DR EMBL; BX005424; CAM47011.1; -; Genomic_DNA.
DR RefSeq; NP_001153500.1; NM_001160028.1.
DR AlphaFoldDB; A3KPK0; -.
DR SMR; A3KPK0; -.
DR STRING; 7955.ENSDARP00000086246; -.
DR PaxDb; A3KPK0; -.
DR PeptideAtlas; A3KPK0; -.
DR PRIDE; A3KPK0; -.
DR Ensembl; ENSDART00000091813; ENSDARP00000086246; ENSDARG00000063079.
DR GeneID; 568159; -.
DR KEGG; dre:568159; -.
DR CTD; 568159; -.
DR ZFIN; ZDB-GENE-060503-452; ago3b.
DR eggNOG; KOG1041; Eukaryota.
DR GeneTree; ENSGT00940000155256; -.
DR HOGENOM; CLU_004544_0_0_1; -.
DR InParanoid; A3KPK0; -.
DR OMA; KPRQAQP; -.
DR PhylomeDB; A3KPK0; -.
DR TreeFam; TF101510; -.
DR PRO; PR:A3KPK0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000063079; Expressed in early embryo and 21 other tissues.
DR ExpressionAtlas; A3KPK0; baseline and differential.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0016442; C:RISC complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0090624; F:endoribonuclease activity, cleaving miRNA-paired mRNA; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0072091; P:regulation of stem cell proliferation; IEA:InterPro.
DR CDD; cd04657; Piwi_ago-like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_03032; AGO3; 1.
DR InterPro; IPR028603; AGO3.
DR InterPro; IPR014811; ArgoL1.
DR InterPro; IPR032472; ArgoL2.
DR InterPro; IPR032473; Argonaute_Mid_dom.
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; PF16487; ArgoMid; 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 Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Reference proteome; Ribonucleoprotein; RNA-binding;
KW RNA-mediated gene silencing; Translation regulation.
FT CHAIN 1..860
FT /note="Protein argonaute-3"
FT /id="PRO_0000371224"
FT DOMAIN 236..349
FT /note="PAZ"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03032"
FT DOMAIN 518..819
FT /note="Piwi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03032"
FT REGION 530..567
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250|UniProtKB:Q9H9G7"
FT REGION 758..805
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250|UniProtKB:Q9H9G7"
FT BINDING 598
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q9H9G7"
FT BINDING 638
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q9H9G7"
FT BINDING 670
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q9H9G7"
FT BINDING 808
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q9H9G7"
SQ SEQUENCE 860 AA; 97332 MW; E77D0FE15165D536 CRC64;
MEIGTTGAVG AAPQFSVPRR PGYGTMGKPI KLLANCFQVD IPKMDVYLYD VDIKPEKCPR
RVNREVVDSM VQHFKVTIFG DRRPVYDGKK SLYTAQPLPV ASAGVDLDVT LPGEGGKDRI
FKVTIKFVSL VSWHMLHEVL TGRSTPDPLE LDKPISTNPV HAVDVVLRHL PSMRYTPVGR
SFFSSPEGYD HPLGGGREVW FGFHQSVRPA MWKMMLNIDV SATAFYKAQP VIQFMCEVLD
IHNIDEQPRP LTDSHRVKFT KEIKGLKVEV THCGTMRRKY RVCNVTRRPA SHQTFPLQLE
NGQTVERTVA QYFREKYNLQ LKYPHLPCLQ VGQEQKHTYL PLEVCNIVAG QRCIKKLTDN
QTSTMIKATA RSAPDRQEEI SRLVRSANYN SDPFVQEFQF RVRDEMAEVT GRVLPAPMLQ
YGGRNRTVAT PSHGVWDMRG KQFHTGVEIK MWAIACFATQ RQCREEVLKG FTDQLRKISK
DAGMPIQGQP CFCKYAQGAD NVEPMFRHLK NTYAGLQLII VILPGKTPVY AEVKRVGDTL
LGMATQCVQV KNVVKTSPQT LSNLCLKINV KLGGINNILV PHQRPSVFQQ PVIFLGADVT
HPPAGDGKKP SIAAVVGSMD AHPSRYCATV RVQRPRQEVI QDLASMVREL LIQFYKSTHY
KPTRIIFYRD GVSEGQFRQV LYYELLAIRE ACISLEKEYQ PGITYIVVQK RHHTRLFCAD
RAERVGRSGN IPAGTTVDTD ITHPYEFDFY LCSHAGIQGT SRPSHYYVLW DDNCFTADEF
QLLTYQLCHT YVRCTRSVSI PAPAYYAHLV AFRARYHLVD KEHDSAEGSH VSGQSNGRDP
QALAKAVQIH HDTLRTMYFA
