ID   AGO3_BOVIN              Reviewed;         861 AA.
AC   Q6T5B7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 91.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Golding M.C., Westhusin M.E.;
RT   "Bovine epigenetics.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SEQUENCE REVISION.
RA   Golding M.C., Long C.R., Westhusin M.E.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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. Proposed to be involved in
CC       stabilization of small RNA derivates (siRNA) derived from processed RNA
CC       polymerase III-transcribed Alu repeats containing a DR2 retinoic acid
CC       response element (RARE) in stem cells and in the subsequent siRNA-
CC       dependent degradation of a subset of RNA polymerase II-transcribed
CC       coding mRNAs by recruiting a mRNA decapping complex involving EDC4.
CC       Possesses RNA slicer activity but only on select RNAs bearing 5'- and
CC       3'-flanking sequences to the region of guide-target complementarity (By
CC       similarity). {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   -!- SUBUNIT: Interacts with EIF4B, IMP8, PRMT5 and TNRC6B (By similarity).
CC       Interacts with APOBEC3F, APOBEC3G and APOBEC3H. Interacts with EDC4 (By
CC       similarity). {ECO:0000255|HAMAP-Rule:MF_03032}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
CC       Rule:MF_03032}.
CC   -!- PTM: Ubiquitinated on surface-exposed lysines by a SCF-like E3
CC       ubiquitin-protein ligase complex containing ZSWIM8 during target-
CC       directed microRNA degradation (TDMD), a process that mediates
CC       degradation of microRNAs (miRNAs). Ubiquitination by the SCF-like E3
CC       ubiquitin-protein ligase complex containing ZSWIM8 leads to its
CC       subsequent degradation, thereby exposing miRNAs for degradation. ZSWIM8
CC       recognizes and binds AGO3 when it is engaged with a TDMD target.
CC       {ECO:0000250|UniProtKB:Q9UKV8}.
CC   -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03032}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAR12162.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY436348; AAR12162.2; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q6T5B7; -.
DR   SMR; Q6T5B7; -.
DR   STRING; 9913.ENSBTAP00000024385; -.
DR   PaxDb; Q6T5B7; -.
DR   PRIDE; Q6T5B7; -.
DR   eggNOG; KOG1041; Eukaryota.
DR   InParanoid; Q6T5B7; -.
DR   OrthoDB; 159407at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW   Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding;
KW   RNA-mediated gene silencing; Translation regulation; Ubl conjugation.
FT   CHAIN           1..861
FT                   /note="Protein argonaute-3"
FT                   /id="PRO_0000371222"
FT   DOMAIN          236..349
FT                   /note="PAZ"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03032"
FT   DOMAIN          518..820
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..806
FT                   /note="Interaction with guide RNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9G7"
FT   REGION          824..847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         809
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9G7"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9G7"
FT   MOD_RES         826
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9G7"
SQ   SEQUENCE   861 AA;  97300 MW;  1A28CDACD5070697 CRC64;
     MEIGSAGPVG AQPLLMVPRR PGYGTMGKPT KLLANCFQVE IPKIDVYLYE VDIKPDKCPR
     RVNREVVDSM VQHFKVTIFG DRRPVYDGKR SLYTANPLPV ATTGVDLDAT LPGEGGKDRP
     FKVSIKFVSR VSWHLLHEVL TGRTLPEPLE LDKPISTNPV HAVDVVLRHL PSMKYTPVGR
     SFFSAPEGYD HPLGGGREVW FGFHQSVRPA MWKMMLNIDV SATAFYKAQP VIQFMCEVLD
     IHNIDEQPRP LTDSHRVKST KEIKGLKVEV THCGTMRRKY RVCNVTRRPA SHQTFPLQLE
     NGQTVERTVA QYFREKYTLQ LKYPHLPCLQ VGQEQKHTYL PLEVCNIVAG QRCIKKLTDN
     QTSTMIKATA RSAPDRQEEI SRLVRSANYE TDPFVQEFQF KVRDEMAHVT GRVLPAPMLQ
     YGGRNRTVAT PSHGVWDMRG KQFHTGVEIE MWAIACFATQ RQCREEILKG FTDQLRKISK
     DAGMPIQGQP CFCKYAQGAD SVEPMFRHLK NTYSGLQLII VILPGKTPVY AEVKRVGDTL
     LGMATQCVQV KNVIKTSPQT LSNLCLKINV KLGGINNILV PHQRPSVFQQ PVIFLGADVT
     HPPAGDGKKP SIAAVVGSMD AHPSRYCATV RVQRPRQEII QDLASMVREL LIQFYKSTRF
     KPTRIIFYRD GVSEGQFRQV LYYELLAIRE ACISLEKDYQ PGITYIVVQK RHHTRLFCAD
     RTERVGRSGN IPAGTTVDTD ITHPYEFDFY LCSHAGIQGT SRPSHYHVLW DDNCFTADEL
     QLLTYQPSAH TYVHCTRSVS IPAPAYYAHL VAFRARYHLV DKERDSAEGS HVSGQSNGRD
     PQALAKAAQI HQDTLRTMYF A