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RISC-loading complex subunit TARBP2 (Protamine-1 RNA-binding protein) (PRM-1 RNA-binding protein) (TAR RNA-binding protein 2)

 TRBP2_MOUSE             Reviewed;         365 AA.
P97473; Q99M41;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
30-AUG-2017, entry version 134.
RecName: Full=RISC-loading complex subunit TARBP2 {ECO:0000255|HAMAP-Rule:MF_03034};
AltName: Full=Protamine-1 RNA-binding protein;
Short=PRM-1 RNA-binding protein;
AltName: Full=TAR RNA-binding protein 2;
Name=Tarbp2; Synonyms=Prbp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Testis;
PubMed=8649414; DOI=10.1128/MCB.16.6.3023;
Lee K., Fajardo M.A., Braun R.E.;
"A testis cytoplasmic RNA-binding protein that has the properties of a
translational repressor.";
Mol. Cell. Biol. 16:3023-3034(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH DICER1.
PubMed=16142218; DOI=10.1038/sj.embor.7400509;
Haase A.D., Jaskiewicz L., Zhang H., Laine S., Sack R., Gatignol A.,
Filipowicz W.;
"TRBP, a regulator of cellular PKR and HIV-1 virus expression,
interacts with Dicer and functions in RNA silencing.";
EMBO Rep. 6:961-967(2005).
[5]
INTERACTION WITH DICER1 AND PRKRA.
PubMed=17452327; DOI=10.1074/jbc.M611768200;
Kok K.H., Ng M.-H., Ching Y.-P., Jin D.-Y.;
"Human TRBP and PACT directly interact with each other and associate
with dicer to facilitate the production of small interfering RNA.";
J. Biol. Chem. 282:17649-17657(2007).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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 (By similarity). Binds in vitro to the PRM1
3'-UTR. Seems to act as a repressor of translation
(PubMed:8649414). {ECO:0000255|HAMAP-Rule:MF_03034,
ECO:0000269|PubMed:8649414}.
-!- 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 (By
similarity). Interacts with DICER1 and PRKRA (PubMed:16142218,
PubMed:17452327). Interacts with DICER1, AGO2, MOV10, EIF6 and
RPL7A (60S ribosome subunit); they form a large RNA-induced
silencing complex (RISC) (By similarity). {ECO:0000255|HAMAP-
Rule:MF_03034, ECO:0000269|PubMed:16142218,
ECO:0000269|PubMed:17452327}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03034,
ECO:0000269|PubMed:8649414}. Cytoplasm, perinuclear region
{ECO:0000255|HAMAP-Rule:MF_03034}. Nucleus {ECO:0000255|HAMAP-
Rule:MF_03034, ECO:0000269|PubMed:8649414}.
-!- SIMILARITY: Belongs to the TARBP2 family. {ECO:0000255|HAMAP-
Rule:MF_03034}.
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EMBL; U79962; AAB38885.1; -; mRNA.
EMBL; CH466550; EDL03967.1; -; Genomic_DNA.
EMBL; BC002028; AAH02028.1; -; mRNA.
CCDS; CCDS27886.1; -.
RefSeq; NP_033345.2; NM_009319.3.
UniGene; Mm.291485; -.
ProteinModelPortal; P97473; -.
SMR; P97473; -.
IntAct; P97473; 3.
STRING; 10090.ENSMUSP00000023813; -.
iPTMnet; P97473; -.
PhosphoSitePlus; P97473; -.
EPD; P97473; -.
MaxQB; P97473; -.
PaxDb; P97473; -.
PeptideAtlas; P97473; -.
PRIDE; P97473; -.
Ensembl; ENSMUST00000023813; ENSMUSP00000023813; ENSMUSG00000023051.
GeneID; 21357; -.
KEGG; mmu:21357; -.
UCSC; uc007xwf.3; mouse.
CTD; 6895; -.
MGI; MGI:103027; Tarbp2.
eggNOG; KOG3732; Eukaryota.
eggNOG; ENOG410XSCK; LUCA.
GeneTree; ENSGT00890000139380; -.
HOGENOM; HOG000231919; -.
HOVERGEN; HBG001700; -.
InParanoid; P97473; -.
KO; K18420; -.
OMA; PMEVQPP; -.
OrthoDB; EOG091G0I2L; -.
TreeFam; TF315953; -.
Reactome; R-MMU-203927; MicroRNA (miRNA) biogenesis.
Reactome; R-MMU-426486; Small interfering RNA (siRNA) biogenesis.
PRO; PR:P97473; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000023051; -.
CleanEx; MM_TARBP2; -.
ExpressionAtlas; P97473; baseline and differential.
Genevisible; P97473; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0035068; C:micro-ribonucleoprotein complex; IDA:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016442; C:RISC complex; IEA:InterPro.
GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0070883; F:pre-miRNA binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0035197; F:siRNA binding; ISS:UniProtKB.
GO; GO:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; ISO:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0050689; P:negative regulation of defense response to virus by host; ISS:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IMP:MGI.
GO; GO:0045070; P:positive regulation of viral genome replication; ISS:UniProtKB.
GO; GO:0031054; P:pre-miRNA processing; ISS:UniProtKB.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
GO; GO:0030422; P:production of siRNA involved in RNA interference; ISS:UniProtKB.
GO; GO:0046782; P:regulation of viral transcription; ISS:UniProtKB.
GO; GO:0007338; P:single fertilization; IMP:MGI.
GO; GO:0035087; P:siRNA loading onto RISC involved in RNA interference; ISO:MGI.
GO; GO:0007286; P:spermatid development; IMP:MGI.
GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; ISS:UniProtKB.
HAMAP; MF_03034; TRBP2; 1.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR028605; TRBP2.
PANTHER; PTHR10910:SF124; PTHR10910:SF124; 1.
Pfam; PF00035; dsrm; 2.
SMART; SM00358; DSRM; 3.
PROSITE; PS50137; DS_RBD; 3.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
Translation regulation.
CHAIN 1 365 RISC-loading complex subunit TARBP2.
/FTId=PRO_0000065623.
DOMAIN 30 97 DRBM 1. {ECO:0000255|HAMAP-
Rule:MF_03034}.
DOMAIN 158 226 DRBM 2. {ECO:0000255|HAMAP-
Rule:MF_03034}.
DOMAIN 292 360 DRBM 3. {ECO:0000255|HAMAP-
Rule:MF_03034}.
REGION 22 105 Sufficient for interaction with PRKRA.
{ECO:0000255|HAMAP-Rule:MF_03034}.
REGION 151 233 Sufficient for interaction with PRKRA.
{ECO:0000255|HAMAP-Rule:MF_03034}.
REGION 227 365 Sufficient for interaction with DICER1.
{ECO:0000255|HAMAP-Rule:MF_03034}.
REGION 286 365 Sufficient for interaction with PRKRA.
{ECO:0000255|HAMAP-Rule:MF_03034}.
MOD_RES 151 151 Phosphoserine.
{ECO:0000250|UniProtKB:Q15633}.
CONFLICT 53 53 A -> E (in Ref. 1; AAB38885).
{ECO:0000305}.
CONFLICT 76 76 Q -> T (in Ref. 1; AAB38885).
{ECO:0000305}.
CONFLICT 111 111 F -> L (in Ref. 1; AAB38885).
{ECO:0000305}.
CONFLICT 258 258 R -> H (in Ref. 1; AAB38885).
{ECO:0000305}.
CONFLICT 334 334 T -> A (in Ref. 1; AAB38885).
{ECO:0000305}.
SEQUENCE 365 AA; 38842 MW; 220A1D10D71CC249 CRC64;
MSEEDQGSGT TTGCGLPSIE QMLAANPGKT PISLLQEYGT RIGKTPVYDL LKAEGQAHQP
NFTFRVTVGD TSCTGQGPSK KAAKHKAAEV ALKHLKGGSM LEPALEDSSS FSLLDSSPPE
DTPVVAAEAA APVPSAVLTR SPPMEMQPPV SPQQSECNPV GALQELVVQK GWRLPEYMVT
QESGPAHRKE FTMTCRVERF IEIGSGTSKK LAKRNAAAKM LLRVHTVPLD ARDGNEAEPD
DDHFSIGVSS RLDGLRNRGP GCTWDSLRNS VGEKILSLRS CSVGSLGALG SACCSVLSEL
SEEQAFHVSY LDIEELSLSG LCQCLVELST QPATVCYGSA TTREAARGDA AHRALQYLRI
MAGSK


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