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 24-JAN-2024, entry version 98.
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.ENSBTAP00000063841; -.
DR PaxDb; 9913-ENSBTAP00000024385; -.
DR eggNOG; KOG1041; Eukaryota.
DR InParanoid; Q6T5B7; -.
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: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:0004521; F:RNA endonuclease activity; ISS:UniProtKB.
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; cd02846; PAZ_argonaute_like; 1.
DR CDD; cd04657; Piwi_ago-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.170.260.10; paz domain; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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 PANTHER; PTHR22891; EUKARYOTIC TRANSLATION INITIATION FACTOR 2C; 1.
DR PANTHER; PTHR22891:SF3; PROTEIN ARGONAUTE-3; 1.
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; PAZ domain; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 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 230..349
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
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
//
