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Protein argonaute-2 (Argonaute2) (EC 3.1.26.n2) (Argonaute RISC catalytic component 2) (Eukaryotic translation initiation factor 2C 2) (eIF-2C 2) (eIF2C 2) (Golgi ER protein 95 kDa) (GERp95) (Protein slicer)

 AGO2_RAT                Reviewed;         860 AA.
Q9QZ81;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
14-NOV-2003, sequence version 2.
20-JUN-2018, entry version 120.
RecName: Full=Protein argonaute-2 {ECO:0000255|HAMAP-Rule:MF_03031};
Short=Argonaute2 {ECO:0000255|HAMAP-Rule:MF_03031};
EC=3.1.26.n2 {ECO:0000255|HAMAP-Rule:MF_03031};
AltName: Full=Argonaute RISC catalytic component 2;
AltName: Full=Eukaryotic translation initiation factor 2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
Short=eIF-2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
Short=eIF2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
AltName: Full=Golgi ER protein 95 kDa;
Short=GERp95;
AltName: Full=Protein slicer {ECO:0000255|HAMAP-Rule:MF_03031};
Name=Ago2; Synonyms=Eif2c2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Hepatoma;
PubMed=10512872; DOI=10.1091/mbc.10.10.3357;
Cikaluk D.E., Tahbaz N., Hendricks L.C., DiMattia G.E., Hansen D.,
Pilgrim D., Hobman T.C.;
"GERp95, a membrane-associated protein that belongs to a family of
proteins involved in stem cell differentiation.";
Mol. Biol. Cell 10:3357-3372(1999).
-!- FUNCTION: Required for RNA-mediated gene silencing (RNAi) by the
RNA-induced silencing complex (RISC). The 'minimal RISC' appears
to include AGO2 bound to a short guide RNA such as a microRNA
(miRNA) or short interfering RNA (siRNA). These guide RNAs direct
RISC to complementary mRNAs that are targets for RISC-mediated
gene silencing. The precise mechanism of gene silencing depends on
the degree of complementarity between the miRNA or siRNA and its
target. Binding of RISC to a perfectly complementary mRNA
generally results in silencing due to endonucleolytic cleavage of
the mRNA specifically by AGO2. Binding of RISC to a partially
complementary mRNA results in silencing through inhibition of
translation, and this is independent of endonuclease activity. May
inhibit translation initiation by binding to the 7-methylguanosine
cap, thereby preventing the recruitment of the translation
initiation factor eIF4-E. May also inhibit translation initiation
via interaction with EIF6, which itself binds to the 60S ribosomal
subunit and prevents its association with the 40S ribosomal
subunit. The inhibition of translational initiation leads to the
accumulation of the affected mRNA in cytoplasmic processing bodies
(P-bodies), where mRNA degradation may subsequently occur. In some
cases RISC-mediated translational repression is also observed for
miRNAs that perfectly match the 3' untranslated region (3'-UTR).
Can also up-regulate the translation of specific mRNAs under
certain growth conditions. Binds to the AU element of the 3'-UTR
of the TNF (TNF-alpha) mRNA and up-regulates translation under
conditions of serum starvation. Also required for transcriptional
gene silencing (TGS), in which short RNAs known as antigene RNAs
or agRNAs direct the transcriptional repression of complementary
promoter regions. {ECO:0000255|HAMAP-Rule:MF_03031}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_03031}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts with DICER1 through its Piwi domain and with
TARBP2 during assembly of the RNA-induced silencing complex
(RISC). Together, DICER1, AGO2 and TARBP2 constitute the trimeric
RISC loading complex (RLC), or micro-RNA (miRNA) loading complex
(miRLC). Within the RLC/miRLC, DICER1 and TARBP2 are required to
process precursor miRNAs (pre-miRNAs) to mature miRNAs and then
load them onto AGO2. AGO2 bound to the mature miRNA constitutes
the minimal RISC and may subsequently dissociate from DICER1 and
TARBP2. Note however that the term RISC has also been used to
describe the trimeric RLC/miRLC. The formation of RISC complexes
containing siRNAs rather than miRNAs appears to occur
independently of DICER1. Interacts with AGO1. Also interacts with
DDB1, DDX5, DDX6, DDX20, DHX30, DHX36, DDX47, DHX9, ELAVL, FXR1,
GEMIN4, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3, PABPC1, PRMT5, P4HA1,
P4HB, RBM4, SART3, TNRC6A, TNRC6B, UPF1 and YBX1. Interacts with
the P-body components DCP1A and XRN1. Associates with polysomes
and messenger ribonucleoproteins (mNRPs). Interacts with RBM4; the
interaction is modulated under stress-induced conditions, occurs
under both cell proliferation and differentiation conditions and
in an RNA- and phosphorylation-independent manner. Interacts with
LIMD1, WTIP and AJUBA. Interacts with TRIM71; the interaction
increases in presence of RNA. Interacts with APOBEC3G in an RNA-
dependent manner. Interacts with APOBEC3A, APOBEC3C, APOBEC3F and
APOBEC3H. Interacts with DICER1, TARBP2, EIF6, MOV10 and RPL7A
(60S ribosome subunit); they form a large RNA-induced silencing
complex (RISC). Interacts with FMR1. Interacts with ZFP36.
Interacts with RC3H1; the interaction is RNA independent (By
similarity). {ECO:0000250|UniProtKB:Q8CJG0, ECO:0000255|HAMAP-
Rule:MF_03031}.
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
Rule:MF_03031}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03031}.
Note=Translational repression of mRNAs results in their
recruitment to P-bodies. Translocation to the nucleus requires
IMP8. {ECO:0000255|HAMAP-Rule:MF_03031}.
-!- DOMAIN: The Piwi domain may perform RNA cleavage by a mechanism
similar to that of RNase H. However, while RNase H utilizes a
triad of Asp-Asp-Glu (DDE) for metal ion coordination, this
protein appears to utilize a triad of Asp-Asp-His (DDH).
{ECO:0000255|HAMAP-Rule:MF_03031}.
-!- PTM: Hydroxylated. 4-hydroxylation appears to enhance protein
stability but is not required for miRNA-binding or endonuclease
activity. {ECO:0000255|HAMAP-Rule:MF_03031}.
-!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
{ECO:0000255|HAMAP-Rule:MF_03031}.
-!- CAUTION: Was originally thought to be membrane-associated.
{ECO:0000305|PubMed:10512872}.
-!- SEQUENCE CAUTION:
Sequence=AAF12800.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AF195534; AAF12800.1; ALT_INIT; mRNA.
RefSeq; NP_067608.1; NM_021597.1.
UniGene; Rn.234328; -.
ProteinModelPortal; Q9QZ81; -.
SMR; Q9QZ81; -.
BioGrid; 248738; 1.
IntAct; Q9QZ81; 6.
MINT; Q9QZ81; -.
STRING; 10116.ENSRNOP00000011898; -.
iPTMnet; Q9QZ81; -.
PhosphoSitePlus; Q9QZ81; -.
PaxDb; Q9QZ81; -.
PeptideAtlas; Q9QZ81; -.
PRIDE; Q9QZ81; -.
GeneID; 59117; -.
KEGG; rno:59117; -.
UCSC; RGD:621255; rat.
CTD; 27161; -.
RGD; 621255; Ago2.
eggNOG; KOG1041; Eukaryota.
eggNOG; ENOG410XP07; LUCA.
HOGENOM; HOG000116043; -.
InParanoid; Q9QZ81; -.
KO; K11593; -.
PhylomeDB; Q9QZ81; -.
PRO; PR:Q9QZ81; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0035068; C:micro-ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0005844; C:polysome; ISS:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0016442; C:RISC complex; IEA:InterPro.
GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB.
GO; GO:0070551; F:endoribonuclease activity, cleaving siRNA-paired mRNA; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB.
GO; GO:0035197; F:siRNA binding; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; NAS:RGD.
GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
GO; GO:0035278; P:miRNA mediated inhibition of translation; ISS:UniProtKB.
GO; GO:0035279; P:mRNA cleavage involved in gene silencing by miRNA; ISS:UniProtKB.
GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
GO; GO:0031054; P:pre-miRNA processing; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.420.10; -; 1.
HAMAP; MF_03031; AGO2; 1.
InterPro; IPR028602; AGO2.
InterPro; IPR014811; ArgoL1.
InterPro; IPR032472; ArgoL2.
InterPro; IPR032473; Argonaute_Mid_dom.
InterPro; IPR032474; Argonaute_N.
InterPro; IPR003100; PAZ_dom.
InterPro; IPR036085; PAZ_dom_sf.
InterPro; IPR003165; Piwi.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF08699; ArgoL1; 1.
Pfam; PF16488; ArgoL2; 1.
Pfam; PF16487; ArgoMid; 1.
Pfam; PF16486; ArgoN; 1.
Pfam; PF02170; PAZ; 1.
Pfam; PF02171; Piwi; 1.
SMART; SM01163; DUF1785; 1.
SMART; SM00949; PAZ; 1.
SMART; SM00950; Piwi; 1.
SUPFAM; SSF101690; SSF101690; 1.
SUPFAM; SSF53098; SSF53098; 1.
PROSITE; PS50821; PAZ; 1.
PROSITE; PS50822; PIWI; 1.
2: Evidence at transcript level;
Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Hydroxylation;
Magnesium; Manganese; Metal-binding; Nitration; Nuclease; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Ribonucleoprotein;
RNA-binding; RNA-mediated gene silencing; Transcription;
Transcription regulation; Translation regulation.
CHAIN 1 860 Protein argonaute-2.
/FTId=PRO_0000194060.
DOMAIN 236 349 PAZ. {ECO:0000255|HAMAP-Rule:MF_03031}.
DOMAIN 518 819 Piwi. {ECO:0000255|HAMAP-Rule:MF_03031}.
REGION 312 317 Interaction with guide RNA.
{ECO:0000250}.
REGION 525 567 Interaction with guide RNA.
{ECO:0000250}.
REGION 588 591 Interaction with GW182 family members.
{ECO:0000255}.
REGION 651 661 Interaction with GW182 family members.
{ECO:0000255}.
REGION 710 711 Interaction with guide RNA.
{ECO:0000250}.
REGION 754 762 Interaction with guide RNA.
{ECO:0000250}.
REGION 791 813 Interaction with guide RNA.
{ECO:0000250}.
METAL 598 598 Divalent metal cation.
{ECO:0000255|HAMAP-Rule:MF_03031}.
METAL 670 670 Divalent metal cation.
{ECO:0000255|HAMAP-Rule:MF_03031}.
METAL 808 808 Divalent metal cation.
{ECO:0000255|HAMAP-Rule:MF_03031}.
MOD_RES 2 2 Nitrated tyrosine.
{ECO:0000250|UniProtKB:Q8CJG0,
ECO:0000255|HAMAP-Rule:MF_03031}.
MOD_RES 388 388 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKV8}.
MOD_RES 701 701 4-hydroxyproline. {ECO:0000255|HAMAP-
Rule:MF_03031}.
MOD_RES 829 829 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKV8}.
SEQUENCE 860 AA; 97318 MW; A5B0798C66481C9C CRC64;
MYSGAGPVLA SPAPTTSPIP GYAFKPPPRP DFGTTGRTIK LQANFFEMDI PKIDIYHYEL
DIKPEKCPRR VNREIVEHMV QHFKTQIFGD RKPVFDGRKN LYTAMPLPIG RDKVELEVTL
PGEGKDRIFK VSIKWVSCVS LQALHDALSG RLPSVPFETI QALDVVMRHL PSMRYTPVGR
SFFTASEGCS NPLGGGREVW FGFHQSVRPS LWKMMLNIDV SATAFYKAQP VIEFVCEVLD
FKSIEEQQKP LTDSQRVKFT KEIKGLKVEI THCGQMKRKY RVCNVTRRPA SHQTFPLQQE
SGQTVECTVA QYFKDRHKLV LRYPHLPCLQ VGQEQKHTYL PLEVCNIVAG QRCIKKLTDN
QTSTMIRATA RSAPDRQEEI SKLMRSASFN TDPYVREFGI MVKDEMTDVT GRVLQPPSIL
YGGRNKAIAT PVQGVWDMRN KQFHTGIEIK VWAIACFAPQ RQCTEVHLKS FTEQLRKISR
DAGMPIQGQP CFCKYAQGAD SVEPMFRHLK NTYAGLQLVV VILPGKTPVY AEVKRVGDTV
LGMATQCVQM KNVQRTTPQT LSNLCLKINV KLGGVNNILL PQGRPPVFQQ PVIFLGADVT
HPPAGDGKKP SIAAVVGSMD AHPNRYCATV RVQQHRQEII QDLAAMVREL LIQFYKSTRF
KPTRIIFYRD GVSEGQFQQV LHHELLAIRE ACIKLEKEYQ PGITFIVVQK RHHTRLFCTD
KNERVGKSGN IPAGTTVDTK ITHPTEFDFY LCSHAGIQGT SRPSHYHVLW DDNRFSSDEL
QILTYQLCHT YVRCTRSVSI PAPAYYAHLV AFRARYHLVD KEHDSAEGSH TSGQSNGRDH
QALAKAVQVH QDTLRTMYFA


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