TRBP2_MOUSE
ID TRBP2_MOUSE Reviewed; 365 AA.
AC P97473; Q99M41;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=RISC-loading complex subunit TARBP2 {ECO:0000255|HAMAP-Rule:MF_03034};
DE AltName: Full=Protamine-1 RNA-binding protein;
DE Short=PRM-1 RNA-binding protein;
DE AltName: Full=TAR RNA-binding protein 2;
GN Name=Tarbp2; Synonyms=Prbp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=8649414; DOI=10.1128/mcb.16.6.3023;
RA Lee K., Fajardo M.A., Braun R.E.;
RT "A testis cytoplasmic RNA-binding protein that has the properties of a
RT translational repressor.";
RL Mol. Cell. Biol. 16:3023-3034(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH DICER1.
RX PubMed=16142218; DOI=10.1038/sj.embor.7400509;
RA Haase A.D., Jaskiewicz L., Zhang H., Laine S., Sack R., Gatignol A.,
RA Filipowicz W.;
RT "TRBP, a regulator of cellular PKR and HIV-1 virus expression, interacts
RT with Dicer and functions in RNA silencing.";
RL EMBO Rep. 6:961-967(2005).
RN [5]
RP INTERACTION WITH DICER1 AND PRKRA.
RX PubMed=17452327; DOI=10.1074/jbc.m611768200;
RA Kok K.H., Ng M.-H., Ching Y.-P., Jin D.-Y.;
RT "Human TRBP and PACT directly interact with each other and associate with
RT dicer to facilitate the production of small interfering RNA.";
RL J. Biol. Chem. 282:17649-17657(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for formation of the RNA induced silencing complex
CC (RISC). Component of the RISC loading complex (RLC), also known as the
CC micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1,
CC AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required
CC to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load
CC them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal
CC RISC and may subsequently dissociate from DICER1 and TARBP2. May also
CC play a role in the production of short interfering RNAs (siRNAs) from
CC double-stranded RNA (dsRNA) by DICER1 (By similarity). Binds in vitro
CC to the PRM1 3'-UTR. Seems to act as a repressor of translation
CC (PubMed:8649414). {ECO:0000255|HAMAP-Rule:MF_03034,
CC ECO:0000269|PubMed:8649414}.
CC -!- SUBUNIT: Self-associates. Component of the RISC loading complex (RLC),
CC or micro-RNA (miRNA) loading complex (miRLC), which is composed of
CC DICER1, AGO2 and TARBP2. Note that the trimeric RLC/miRLC is also
CC referred to as RISC. Interacts with EIF2AK2/PKR and inhibits its
CC protein kinase activity. Interacts with DHX9 (By similarity). Interacts
CC with DICER1 and PRKRA (PubMed:16142218, PubMed:17452327). Interacts
CC with DICER1, AGO2, MOV10, EIF6 and RPL7A (60S ribosome subunit); they
CC form a large RNA-induced silencing complex (RISC) (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_03034, ECO:0000269|PubMed:16142218,
CC ECO:0000269|PubMed:17452327}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03034,
CC ECO:0000269|PubMed:8649414}. Cytoplasm, perinuclear region
CC {ECO:0000255|HAMAP-Rule:MF_03034}. Nucleus {ECO:0000255|HAMAP-
CC Rule:MF_03034, ECO:0000269|PubMed:8649414}.
CC -!- SIMILARITY: Belongs to the TARBP2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03034}.
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DR EMBL; U79962; AAB38885.1; -; mRNA.
DR EMBL; CH466550; EDL03967.1; -; Genomic_DNA.
DR EMBL; BC002028; AAH02028.1; -; mRNA.
DR CCDS; CCDS27886.1; -.
DR RefSeq; NP_033345.2; NM_009319.3.
DR AlphaFoldDB; P97473; -.
DR SMR; P97473; -.
DR BioGRID; 203969; 5.
DR ComplexPortal; CPX-135; RISC-loading complex, TARBP2 variant.
DR IntAct; P97473; 3.
DR STRING; 10090.ENSMUSP00000023813; -.
DR iPTMnet; P97473; -.
DR PhosphoSitePlus; P97473; -.
DR EPD; P97473; -.
DR MaxQB; P97473; -.
DR PaxDb; P97473; -.
DR PeptideAtlas; P97473; -.
DR PRIDE; P97473; -.
DR ProteomicsDB; 298210; -.
DR Antibodypedia; 15253; 422 antibodies from 35 providers.
DR DNASU; 21357; -.
DR Ensembl; ENSMUST00000023813; ENSMUSP00000023813; ENSMUSG00000023051.
DR GeneID; 21357; -.
DR KEGG; mmu:21357; -.
DR UCSC; uc007xwf.3; mouse.
DR CTD; 6895; -.
DR MGI; MGI:103027; Tarbp2.
DR VEuPathDB; HostDB:ENSMUSG00000023051; -.
DR eggNOG; KOG3732; Eukaryota.
DR GeneTree; ENSGT00940000157748; -.
DR HOGENOM; CLU_048292_2_0_1; -.
DR InParanoid; P97473; -.
DR OMA; GYSCTWD; -.
DR OrthoDB; 1093169at2759; -.
DR PhylomeDB; P97473; -.
DR TreeFam; TF315953; -.
DR Reactome; R-MMU-203927; MicroRNA (miRNA) biogenesis.
DR Reactome; R-MMU-426486; Small interfering RNA (siRNA) biogenesis.
DR BioGRID-ORCS; 21357; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Tarbp2; mouse.
DR PRO; PR:P97473; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P97473; protein.
DR Bgee; ENSMUSG00000023051; Expressed in spermatocyte and 67 other tissues.
DR ExpressionAtlas; P97473; baseline and differential.
DR Genevisible; P97473; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016442; C:RISC complex; IDA:MGI.
DR GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035198; F:miRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070883; F:pre-miRNA binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0035197; F:siRNA binding; ISS:UniProtKB.
DR GO; GO:0098795; P:global gene silencing by mRNA cleavage; ISS:UniProtKB.
DR GO; GO:0035196; P:miRNA processing; ISO:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0050689; P:negative regulation of defense response to virus by host; ISS:UniProtKB.
DR GO; GO:0061351; P:neural precursor cell proliferation; IDA:MGI.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IMP:MGI.
DR GO; GO:0045727; P:positive regulation of translation; IMP:MGI.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISS:UniProtKB.
DR GO; GO:0031054; P:pre-miRNA processing; ISS:UniProtKB.
DR GO; GO:1903798; P:regulation of miRNA maturation; IMP:MGI.
DR GO; GO:0070920; P:regulation of production of small RNA involved in gene silencing by RNA; IBA:GO_Central.
DR GO; GO:0046782; P:regulation of viral transcription; ISS:UniProtKB.
DR GO; GO:0070922; P:RISC complex assembly; ISO:MGI.
DR GO; GO:0007338; P:single fertilization; IMP:MGI.
DR GO; GO:0030422; P:siRNA processing; ISS:UniProtKB.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:MGI.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR CDD; cd19890; DSRM_TARBP2_rpt1; 1.
DR CDD; cd10844; DSRM_TARBP2_rpt2; 1.
DR CDD; cd19893; DSRM_TARBP2_rpt3; 1.
DR HAMAP; MF_03034; TRBP2; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR028605; TRBP2.
DR InterPro; IPR044469; TRBP2_DSRM_1.
DR InterPro; IPR044470; TRBP2_DSRM_2.
DR InterPro; IPR044471; TRBP2_DSRM_3.
DR PANTHER; PTHR46205:SF1; PTHR46205:SF1; 1.
DR Pfam; PF00035; dsrm; 2.
DR SMART; SM00358; DSRM; 3.
DR PROSITE; PS50137; DS_RBD; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; RNA-mediated gene silencing; Translation regulation.
FT CHAIN 1..365
FT /note="RISC-loading complex subunit TARBP2"
FT /id="PRO_0000065623"
FT DOMAIN 30..97
FT /note="DRBM 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT DOMAIN 158..226
FT /note="DRBM 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT DOMAIN 292..360
FT /note="DRBM 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT REGION 22..105
FT /note="Sufficient for interaction with PRKRA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT REGION 151..233
FT /note="Sufficient for interaction with PRKRA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT REGION 227..365
FT /note="Sufficient for interaction with DICER1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT REGION 286..365
FT /note="Sufficient for interaction with PRKRA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15633"
FT CONFLICT 53
FT /note="A -> E (in Ref. 1; AAB38885)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="Q -> T (in Ref. 1; AAB38885)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="F -> L (in Ref. 1; AAB38885)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="R -> H (in Ref. 1; AAB38885)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="T -> A (in Ref. 1; AAB38885)"
FT /evidence="ECO:0000305"
SQ 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
