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Database: UniProt
Entry: A3KPK0
LinkDB: A3KPK0
Original site: A3KPK0 
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   16-OCT-2019, entry version 95.
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   Cyprinidae; 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.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   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., Eliott D., Threadgold G.,
RA   Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
RA   Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
RA   Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
RA   Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
RA   Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
RA   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.,
RA   Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
RA   Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
RA   Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
RA   Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
RA   Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
RA   Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
RA   Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds
CC       to short RNAs such as microRNAs (miRNAs) and represses the
CC       translation of mRNAs which are complementary to them. Possesses
CC       RNA slicer activity but only on select RNAs bearing 5'- and 3'-
CC       flanking sequences to the region of guide-target complementarity.
CC       {ECO:0000255|HAMAP-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}.
DR   EMBL; BX005424; CAM47011.1; -; Genomic_DNA.
DR   RefSeq; NP_001153500.1; NM_001160028.1.
DR   SMR; A3KPK0; -.
DR   STRING; 7955.ENSDARP00000086246; -.
DR   PaxDb; A3KPK0; -.
DR   PeptideAtlas; 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   eggNOG; ENOG410XP07; LUCA.
DR   GeneTree; ENSGT00940000155256; -.
DR   HOGENOM; HOG000116043; -.
DR   InParanoid; A3KPK0; -.
DR   KO; K11593; -.
DR   OMA; DSVKNVM; -.
DR   OrthoDB; 159407at2759; -.
DR   PhylomeDB; A3KPK0; -.
DR   TreeFam; TF101510; -.
DR   PRO; PR:A3KPK0; -.
DR   Proteomes; UP000000437; Chromosome 19.
DR   Bgee; ENSDARG00000063079; Expressed in 19 organ(s), highest expression level in multi-cellular organism.
DR   ExpressionAtlas; A3KPK0; baseline.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0035278; P:miRNA mediated 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   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; 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   Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Metal-binding;
KW   Nuclease; Reference proteome; Ribonucleoprotein; RNA-binding;
KW   RNA-mediated gene silencing; Translation regulation.
FT   CHAIN         1    860       Protein argonaute-3.
FT                                /FTId=PRO_0000371224.
FT   DOMAIN      236    349       PAZ. {ECO:0000255|HAMAP-Rule:MF_03032}.
FT   DOMAIN      518    819       Piwi. {ECO:0000255|HAMAP-Rule:MF_03032}.
FT   REGION      530    567       Interaction with guide RNA.
FT                                {ECO:0000250|UniProtKB:Q9H9G7}.
FT   REGION      758    805       Interaction with guide RNA.
FT                                {ECO:0000250|UniProtKB:Q9H9G7}.
FT   METAL       598    598       Divalent metal cation.
FT                                {ECO:0000250|UniProtKB:Q9H9G7}.
FT   METAL       638    638       Divalent metal cation.
FT                                {ECO:0000250|UniProtKB:Q9H9G7}.
FT   METAL       670    670       Divalent metal cation.
FT                                {ECO:0000250|UniProtKB:Q9H9G7}.
FT   METAL       808    808       Divalent metal cation.
FT                                {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
//
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