AGO3_CHICK
ID AGO3_CHICK Reviewed; 860 AA.
AC Q5ZLG4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=RCJMB04_6f12;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719770; CAG31429.1; -; mRNA.
DR RefSeq; NP_001026071.1; NM_001030900.1.
DR AlphaFoldDB; Q5ZLG4; -.
DR SMR; Q5ZLG4; -.
DR STRING; 9031.ENSGALP00000003521; -.
DR PaxDb; Q5ZLG4; -.
DR GeneID; 419628; -.
DR KEGG; gga:419628; -.
DR CTD; 192669; -.
DR VEuPathDB; HostDB:geneid_419628; -.
DR eggNOG; KOG1041; Eukaryota.
DR InParanoid; Q5ZLG4; -.
DR OrthoDB; 159407at2759; -.
DR PhylomeDB; Q5ZLG4; -.
DR PRO; PR:Q5ZLG4; -.
DR Proteomes; UP000000539; 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 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_0000371223"
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; 97271 MW; E6BFBCA2686C7156 CRC64;
MEISSAGPVG AQPLLMVPRR PGYGTMGKPI KLLANCFQVE IPKIDVYLYE VDIKPDKCPR
RVNREVVDSM VQHFKVTIFG DRRPVYDGKR SLYTANPLPV ATTGVDLDVT LPGEGGKDRP
FKVSIKFVSR VSWHLLHEVL TGRTLPEPLE PDKPISTNPV HAVDVVLRHL PSMKYTPVGR
SFFSAPEGYD HPLGGGREVW FGFHQSVRPA MWKMMLNIDV SATAFYKAQP VIQFMCEVLD
IHNIDEQPRP LTDSHRVKFT KEIKGLKVEV THCGTMRRKY RVCNVTRRPA SHQTFPLQLE
NGQTVERTVA QYFREKYNLQ LKYPHLPCLQ VGQEQKHTYL PLEVCNIVAG QRCIKKLTDN
QTSTMIKATA RSAPDRQEEI SRLVRSANYD ADPFVQEFQF KVRDEMAHVT GRVLPAPMLQ
YGGRNRTVAT PSHGVWDMRG KQFHTGVEIK MWAIACFATQ RQCREEILKG FTDQLRKISK
DAGMPIQGQP CFCKYAQGAD SVGPMFRHLK NTYSGLQLII VILPGKTPVY AEVKRAGDTL
LGMATQCVQV KNVIKTSPQT LSNLCLKINV KLGGINNILV PHQRPSVFQQ PVIFLGADVT
HPPAGDGKKP SIAAVVGSMD AHPSRYCATV RVQRPRQEII QDLASMVREL LIQFYKSTRF
KPTRIIFYRD GVSEGQFRQV LYYELLAIRE ACISLEKDYQ PGITYIVVQK RHHTRLFCAD
RTERVGRSGN IPAGTTVDTD ITHPYEFDFY LCSHAGIQGT SRPSHYHVLW DDNCFTADEL
QLLTYQLCHT YVRCTRSVSI PAPAYYAHLV AFRARYHLVD KEHDSAEGSH VSGQSNGRDP
QALAKAVQIH QDTLRTMYFA
