AGO2_XENTR
ID AGO2_XENTR Reviewed; 871 AA.
AC Q6DJB9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Protein argonaute-2 {ECO:0000255|HAMAP-Rule:MF_03031};
DE Short=Argonaute2 {ECO:0000255|HAMAP-Rule:MF_03031};
DE EC=3.1.26.n2 {ECO:0000255|HAMAP-Rule:MF_03031};
DE AltName: Full=Argonaute RISC catalytic component 2;
DE AltName: Full=Eukaryotic translation initiation factor 2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
DE Short=eIF-2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
DE Short=eIF2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
DE AltName: Full=Protein slicer {ECO:0000255|HAMAP-Rule:MF_03031};
GN Name=ago2; Synonyms=eif2c2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for RNA-mediated gene silencing (RNAi) by the RNA-
CC induced silencing complex (RISC). The 'minimal RISC' appears to include
CC ago2 bound to a short guide RNA such as a microRNA (miRNA) or short
CC interfering RNA (siRNA). These guide RNAs direct RISC to complementary
CC mRNAs that are targets for RISC-mediated gene silencing. The precise
CC mechanism of gene silencing depends on the degree of complementarity
CC between the miRNA or siRNA and its target. Binding of RISC to a
CC perfectly complementary mRNA generally results in silencing due to
CC endonucleolytic cleavage of the mRNA specifically by ago2. Binding of
CC RISC to a partially complementary mRNA results in silencing through
CC inhibition of translation, and this is independent of endonuclease
CC activity. The inhibition of translational initiation leads to the
CC accumulation of the affected mRNA in cytoplasmic processing bodies (P-
CC bodies), where mRNA degradation may subsequently occur.
CC {ECO:0000255|HAMAP-Rule:MF_03031}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=endonucleolytic cleavage to 5'-phosphomonoester.;
CC EC=3.1.26.n2; Evidence={ECO:0000255|HAMAP-Rule:MF_03031};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of the RISC loading complex (RLC), or micro-RNA
CC (miRNA) loading complex (miRLC), which is composed of dicer1, ago2 and
CC tarbp2. Note that the trimeric RLC/miRLC is also referred to as RISC.
CC {ECO:0000255|HAMAP-Rule:MF_03031}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
CC Rule:MF_03031}.
CC -!- DOMAIN: The Piwi domain may perform RNA cleavage by a mechanism similar
CC to that of RNase H. However, while RNase H utilizes a triad of Asp-Asp-
CC Glu (DDE) for metal ion coordination, this protein appears to utilize a
CC triad of Asp-Asp-His (DDH). {ECO:0000255|HAMAP-Rule:MF_03031}.
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03031}.
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DR EMBL; BC075263; AAH75263.1; -; mRNA.
DR RefSeq; NP_001004877.1; NM_001004877.1.
DR AlphaFoldDB; Q6DJB9; -.
DR SMR; Q6DJB9; -.
DR STRING; 8364.ENSXETP00000051244; -.
DR PaxDb; Q6DJB9; -.
DR PRIDE; Q6DJB9; -.
DR Ensembl; ENSXETT00000051244; ENSXETP00000051244; ENSXETG00000023755.
DR GeneID; 448205; -.
DR KEGG; xtr:448205; -.
DR CTD; 27161; -.
DR Xenbase; XB-GENE-1001916; ago2.
DR eggNOG; KOG1041; Eukaryota.
DR HOGENOM; CLU_004544_4_3_1; -.
DR InParanoid; Q6DJB9; -.
DR OrthoDB; 159407at2759; -.
DR Reactome; R-XTR-203927; MicroRNA (miRNA) biogenesis.
DR Reactome; R-XTR-426486; Small interfering RNA (siRNA) biogenesis.
DR Reactome; R-XTR-426496; Post-transcriptional silencing by small RNAs.
DR Reactome; R-XTR-5578749; Transcriptional regulation by small RNAs.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000023755; Expressed in neurula embryo and 16 other tissues.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0016442; C:RISC complex; ISS:UniProtKB.
DR GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0070551; F:endoribonuclease activity, cleaving siRNA-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:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB.
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:0035197; F:siRNA binding; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:0035279; P:miRNA-mediated gene silencing by mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:0031054; P:pre-miRNA processing; ISS:UniProtKB.
DR CDD; cd04657; Piwi_ago-like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_03031; AGO2; 1.
DR InterPro; IPR028602; AGO2.
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; Magnesium; Manganese; Metal-binding;
KW Nuclease; Reference proteome; Ribonucleoprotein; RNA-binding;
KW RNA-mediated gene silencing; Translation regulation.
FT CHAIN 1..871
FT /note="Protein argonaute-2"
FT /id="PRO_0000371221"
FT DOMAIN 238..351
FT /note="PAZ"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT DOMAIN 529..830
FT /note="Piwi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT REGION 314..319
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 536..578
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 599..602
FT /note="Interaction with GW182 family members"
FT /evidence="ECO:0000255"
FT REGION 662..672
FT /note="Interaction with GW182 family members"
FT /evidence="ECO:0000255"
FT REGION 721..722
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 765..773
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 802..824
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 834..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 609
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT BINDING 681
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT BINDING 819
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
SQ SEQUENCE 871 AA; 98737 MW; A9AF0FCB56EF17B5 CRC64;
MYAGAGPVLV PPTPTPPLPM PAYTFKPPPR PDFGTSGRTI KLQANFFEMD IPKIEIYHYE
IDIKPEKCPR RVNREIVEHM VQHFKAQIFG DRKPVFDGRK NLYTAMPLPI ARDKQVELEV
TLPGEGKDRI FKVAIKWMAC VSLQALHDAL SGRLPSVPFE TIQALDVVMR HLPSMRYTPV
GRSFFTASEG CANPLGGGRE VWFGFHQSVR PSLWKMMLNI DVSATAFYKA QPVIEFMCEV
LDFKSIEEQQ KPLTDSQRVK FTKEIKGLKV EITHCGQMKR KYRVCNVTRR PASHQTFPLQ
QESGQTVECT VAQYFKDRHK LVLRYPHLPC LQVGQEQKHT YLPLEVCNIV AGQRCIKKLT
DNQTSTMIRA TARSAPDRQE EISKLMRSAS FNTDPFVREF GIMVKDDMTD VTGRVLQPPS
ILYGGRVWEE PNAPLNKAIA TPVQGVWDMR NKQFHTGIEI KVWAIACFAP QRQCTEVHLK
TFTEQLRKIS RDAGMPIQGQ PCFCKYAQGA DSVEPMFRHL KNTYTGLQLV VVILPGKTPV
YAEVKRVGDT VLGMATQCVQ MKNVQRTTPQ TLSNLCLKIN VKLGGVNNIL LPQGRPPVFQ
QPVIFLGADV THPPAGDGKK PSIAAVVGSM DAHPNRYCAT VRVQQHRQEI IQDLSAMVRE
LLIQFYKSTR FKPTRIIFYR DGVSEGQFQQ VLHHELLAIR EACIKLEKDY QPGITFIVVQ
KRHHTRLFCT DRNERVGKSG NIPAGTTVDT KITHPSEFDF YLCSHAGIQG TSRPSHYHVL
WDDNRFSSDE LQILTYQLCH TYVRCTRSVS IPAPAYYAHL VAFRARYHLV DKEHDSAEGS
HTSGQSNGRD QQALAKAVQV HQDTLRTMYF A
