TRBP2_BOVIN
ID TRBP2_BOVIN Reviewed; 366 AA.
AC Q0IIG6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=RISC-loading complex subunit TARBP2 {ECO:0000255|HAMAP-Rule:MF_03034};
GN Name=TARBP2 {ECO:0000255|HAMAP-Rule:MF_03034};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-366.
RX PubMed=11282978; DOI=10.1101/gr.170101;
RA Smith T.P.L., Grosse W.M., Freking B.A., Roberts A.J., Stone R.T.,
RA Casas E., Wray J.E., White J., Cho J., Fahrenkrug S.C., Bennett G.L.,
RA Heaton M.P., Laegreid W.W., Rohrer G.A., Chitko-McKown C.G., Pertea G.,
RA Holt I., Karamycheva S., Liang F., Quackenbush J., Keele J.W.;
RT "Sequence evaluation of four pooled-tissue normalized bovine cDNA libraries
RT and construction of a gene index for cattle.";
RL Genome Res. 11:626-630(2001).
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. {ECO:0000255|HAMAP-
CC Rule:MF_03034}.
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 and PRKRA. Interacts with
CC DICER1, AGO2, MOV10, EIF6 and RPL7A (60S ribosome subunit); they form a
CC large RNA-induced silencing complex (RISC). {ECO:0000255|HAMAP-
CC Rule:MF_03034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03034}.
CC Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03034}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03034}.
CC -!- SIMILARITY: Belongs to the TARBP2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03034}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI22654.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC122653; AAI22654.1; ALT_FRAME; mRNA.
DR EMBL; CK769751; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001069146.2; NM_001075678.2.
DR AlphaFoldDB; Q0IIG6; -.
DR BMRB; Q0IIG6; -.
DR SMR; Q0IIG6; -.
DR STRING; 9913.ENSBTAP00000000558; -.
DR PaxDb; Q0IIG6; -.
DR PRIDE; Q0IIG6; -.
DR Ensembl; ENSBTAT00000000558; ENSBTAP00000000558; ENSBTAG00000000435.
DR GeneID; 514674; -.
DR KEGG; bta:514674; -.
DR CTD; 6895; -.
DR VEuPathDB; HostDB:ENSBTAG00000000435; -.
DR VGNC; VGNC:35602; TARBP2.
DR eggNOG; KOG3732; Eukaryota.
DR GeneTree; ENSGT00940000157748; -.
DR HOGENOM; CLU_048292_2_0_1; -.
DR InParanoid; Q0IIG6; -.
DR OMA; GYSCTWD; -.
DR OrthoDB; 1093169at2759; -.
DR TreeFam; TF315953; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000000435; Expressed in retina and 105 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0070578; C:RISC-loading complex; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0035198; F:miRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070883; F:pre-miRNA binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
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:0035264; P:multicellular organism growth; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
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; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0007338; P:single fertilization; IEA:Ensembl.
DR GO; GO:0030422; P:siRNA processing; ISS:UniProtKB.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; RNA-mediated gene silencing; Translation regulation.
FT CHAIN 1..366
FT /note="RISC-loading complex subunit TARBP2"
FT /id="PRO_0000373970"
FT DOMAIN 30..97
FT /note="DRBM 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT DOMAIN 159..227
FT /note="DRBM 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT DOMAIN 293..361
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 135..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..234
FT /note="Sufficient for interaction with PRKRA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT REGION 228..366
FT /note="Sufficient for interaction with DICER1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT REGION 287..366
FT /note="Sufficient for interaction with PRKRA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT COMPBIAS 136..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15633"
FT CONFLICT 241
FT /note="E -> D (in Ref. 2; CK769751)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="I -> L (in Ref. 2; CK769751)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="A -> T (in Ref. 2; CK769751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 38844 MW; 2FA552E15494AE43 CRC64;
MSEEEQGSGT TTGCGLPSIE QMLAANPGKT PISLLQEYGT RIGKTPVYDL LKAEGQAHQP
NFTFRVTVGD TSCTGQGPSK KAAKHKAAEV ALKHLKGGSM LEPALEDSSS FSPLDSSLPE
DVPVFTAAAA ATPVPSAVPT RSSPMEVQPP VSPQQSECNP VGALQELVVQ KGWRLPEYTV
TQESGPAHRK EFTMTCRVER FIEIGSGTSK KLAKRNAAAK MLLRVHTVPL DARDGNEAEP
EDDHFSIGVG SRLDGLRNRG PGCTWDSLRN SVGEKILSLR SCSLGSLGAL GPACCSVLSE
LSEEQAFHVS YLDIEELSLS GLCQCLVELS TQPATVCHGS AATREAARGE AARRALQYLK
IMAGSK
