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RISC-loading complex subunit TARBP2

 I3M2Q9_ICTTR            Unreviewed;       275 AA.
I3M2Q9;
11-JUL-2012, integrated into UniProtKB/TrEMBL.
22-NOV-2017, sequence version 2.
22-NOV-2017, entry version 39.
RecName: Full=RISC-loading complex subunit TARBP2 {ECO:0000256|HAMAP-Rule:MF_03034};
Name=TARBP2 {ECO:0000256|HAMAP-Rule:MF_03034,
ECO:0000313|Ensembl:ENSSTOP00000003291};
Ictidomys tridecemlineatus (Thirteen-lined ground squirrel)
(Spermophilus tridecemlineatus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha;
Sciuridae; Xerinae; Marmotini; Ictidomys.
NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000003291, ECO:0000313|Proteomes:UP000005215};
[1] {ECO:0000313|Ensembl:ENSSTOP00000003291}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
The Broad Institute Genome Assembly & Analysis Group;
Computational R&D Group;
and Sequencing Platform;
Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
"The Draft Genome of Spermophilus tridecemlineatus.";
Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Ensembl:ENSSTOP00000003291}
IDENTIFICATION.
Ensembl;
Submitted (MAY-2012) to UniProtKB.
-!- FUNCTION: Required for formation of the RNA induced silencing
complex (RISC). Component of the RISC loading complex (RLC), also
known as the micro-RNA (miRNA) loading complex (miRLC), which is
composed of DICER1, AGO2 and TARBP2. 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. May also play a role in the
production of short interfering RNAs (siRNAs) from double-stranded
RNA (dsRNA) by DICER1. {ECO:0000256|HAMAP-Rule:MF_03034}.
-!- SUBUNIT: Self-associates. Component of the RISC loading complex
(RLC), or micro-RNA (miRNA) loading complex (miRLC), which is
composed of DICER1, AGO2 and TARBP2. Note that the trimeric
RLC/miRLC is also referred to as RISC. Interacts with EIF2AK2/PKR
and inhibits its protein kinase activity. Interacts with DHX9 and
PRKRA. Interacts with DICER1, AGO2, MOV10, EIF6 and RPL7A (60S
ribosome subunit); they form a large RNA-induced silencing complex
(RISC). {ECO:0000256|HAMAP-Rule:MF_03034}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03034}.
Cytoplasm, perinuclear region {ECO:0000256|HAMAP-Rule:MF_03034}.
Nucleus {ECO:0000256|HAMAP-Rule:MF_03034}.
-!- SIMILARITY: Belongs to the TARBP2 family. {ECO:0000256|HAMAP-
Rule:MF_03034}.
-!- CAUTION: The sequence shown here is derived from an Ensembl
automatic analysis pipeline and should be considered as
preliminary data. {ECO:0000313|Ensembl:ENSSTOP00000003291}.
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EMBL; AGTP01037486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_005325110.1; XM_005325053.2.
STRING; 43179.ENSSTOP00000003291; -.
Ensembl; ENSSTOT00000003676; ENSSTOP00000003291; ENSSTOG00000003678.
GeneID; 101959619; -.
CTD; 6895; -.
eggNOG; KOG3732; Eukaryota.
eggNOG; ENOG410XSCK; LUCA.
GeneTree; ENSGT00900000141030; -.
InParanoid; I3M2Q9; -.
OMA; PMEVQPP; -.
OrthoDB; EOG091G0I2L; -.
TreeFam; TF315953; -.
Proteomes; UP000005215; Unassembled WGS sequence.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016442; C:RISC complex; IEA:UniProtKB-UniRule.
GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0035198; F:miRNA binding; IEA:UniProtKB-UniRule.
GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-UniRule.
GO; GO:0035197; F:siRNA binding; IEA:UniProtKB-UniRule.
GO; GO:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; IEA:UniProtKB-UniRule.
GO; GO:0031054; P:pre-miRNA processing; IEA:UniProtKB-UniRule.
GO; GO:0030422; P:production of siRNA involved in RNA interference; IEA:UniProtKB-UniRule.
GO; GO:0046782; P:regulation of viral transcription; IEA:InterPro.
GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; IEA:UniProtKB-UniRule.
HAMAP; MF_03034; TRBP2; 1.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR028605; TRBP2.
PANTHER; PTHR10910:SF61; PTHR10910:SF61; 1.
Pfam; PF00035; dsrm; 2.
SMART; SM00358; DSRM; 3.
PROSITE; PS50137; DS_RBD; 3.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000005215};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03034};
Nucleus {ECO:0000256|HAMAP-Rule:MF_03034};
Reference proteome {ECO:0000313|Proteomes:UP000005215};
RNA-binding {ECO:0000256|HAMAP-Rule:MF_03034, ECO:0000256|PROSITE-
ProRule:PRU00266};
RNA-mediated gene silencing {ECO:0000256|HAMAP-Rule:MF_03034};
Translation regulation {ECO:0000256|HAMAP-Rule:MF_03034}.
SEQUENCE 275 AA; 29399 MW; 76F09B3BDEF25CFD CRC64;
MSEEEQGSGT TTGCRLPSSF SPPDSSLPEE VPVFAAVAVA APVPSTVLIR SPPMEMQPPV
SPQQSECNPV GALQELVVQK GWRLPEYTVT QESGPAHRKE FTMTCRVERF IEIGSGTSKK
LAKRNAAAKM LLRVHTVPLD ARDGNEAEPD DDHFSIGVGS RLDGLRNRGP GCTWDSLRNS
VGEKILSLRS CSLGSLGALG SACCSVLSEL SEEQAFHVSY LDIEELSLSG LCQCLVELST
QPATVCHGSA TTREAARGEA ARRALQYLKI MAGSK


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