AGO2_XENLA
ID AGO2_XENLA Reviewed; 862 AA.
AC Q6DCX2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-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; BC077863; AAH77863.1; -; mRNA.
DR RefSeq; NP_001086988.1; NM_001093519.1.
DR AlphaFoldDB; Q6DCX2; -.
DR SMR; Q6DCX2; -.
DR DNASU; 446823; -.
DR GeneID; 446823; -.
DR KEGG; xla:446823; -.
DR CTD; 446823; -.
DR Xenbase; XB-GENE-1001922; ago2.L.
DR OrthoDB; 159407at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 446823; Expressed in neurula embryo and 17 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: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; IEA:UniProtKB-UniRule.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB.
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 GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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..862
FT /note="Protein argonaute-2"
FT /id="PRO_0000371220"
FT DOMAIN 238..351
FT /note="PAZ"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT DOMAIN 520..821
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 527..569
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 590..593
FT /note="Interaction with GW182 family members"
FT /evidence="ECO:0000255"
FT REGION 653..663
FT /note="Interaction with GW182 family members"
FT /evidence="ECO:0000255"
FT REGION 712..713
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 756..764
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 793..815
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000250"
FT REGION 825..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 600
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT BINDING 672
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
FT BINDING 810
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03031"
SQ SEQUENCE 862 AA; 97645 MW; 781AB283CABDDAC1 CRC64;
MYSGAGPVLV PPTTTPPLPM PAYTFKPPPR PDFGTSGRTI KLQANVFEMD IPKIEIYHYD
IDIKPEKCPR RVNREIVEHM VQHFKAQIFG DRKPVFDGRK NLYTAMPLPI ARDKQVELEV
TLPGEGKDRI FKVAIKWMAC VSLQALHDAL SGRLPNVPFE TVQALDVVMR 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
ILYGGRSKAI ATPVQGVWDM RNKQFHTGIE IKVWAIACFA PQRQCTEVHL KTFTEQLRKI
SRDAGMPIQG QPCFCKYAQG ADSVEPMFRH LKNTYTGLQL VVVILPGKTP VYAEVKRVGD
TVLGMATQCV QMKNVQRTTP QTLSNLCLKI NVKLGGVNNI LLPQGRPPVF QQPVIFLGAD
VTHPPAGDGK KPSIAAVVGS MDAHPNRYCA TVRVQQHRQE IIQDLSAMVR ELLIQFYKST
RFKPTRIIFY RDGVSEGQFQ QVLHHELLAI REACIKLEKD YQPGITFIVV QKRHHTRLFC
TDRNERVGKS GNIPAGTTVD TKITHPSEFD FYLCSHAGIQ GTSRPSHYHV LWDDNRFSSD
ELQILTYQLC HTYVRCTRSV SIPAPAYYAH LVAFRARYHL VDKEHDSAEG SHTSGQSNGR
DQQALAKAVQ VHQDTLRTMY FA
