TRBP2_TETNG
ID TRBP2_TETNG Reviewed; 345 AA.
AC Q4SS66;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=RISC-loading complex subunit tarbp2 {ECO:0000255|HAMAP-Rule:MF_03034};
GN Name=tarbp2; ORFNames=GSTENG00013584001;
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
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. {ECO:0000255|HAMAP-Rule:MF_03034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03034}.
CC -!- SIMILARITY: Belongs to the TARBP2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03034}.
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DR EMBL; CAAE01014479; CAF96516.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4SS66; -.
DR SMR; Q4SS66; -.
DR STRING; 99883.ENSTNIP00000009866; -.
DR Ensembl; ENSTNIT00000010044; ENSTNIP00000009866; ENSTNIG00000007065.
DR KEGG; tng:GSTEN00013584G001; -.
DR GeneTree; ENSGT00940000157748; -.
DR HOGENOM; CLU_048292_0_0_1; -.
DR InParanoid; Q4SS66; -.
DR OMA; GYSCTWD; -.
DR TreeFam; TF315953; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005737; C: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; IEA:InterPro.
DR GO; GO:0035198; F:miRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070883; F:pre-miRNA binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035197; F:siRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031054; P:pre-miRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:1903798; P:regulation of miRNA maturation; IEA:InterPro.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0046782; P:regulation of viral transcription; IEA:InterPro.
DR GO; GO:0030422; P:siRNA processing; IEA:UniProtKB-UniRule.
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; IPR032478; Staufen_C.
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 Pfam; PF16482; Staufen_C; 1.
DR SMART; SM00358; DSRM; 3.
DR PROSITE; PS50137; DS_RBD; 3.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; Repeat; RNA-binding;
KW RNA-mediated gene silencing; Translation regulation.
FT CHAIN 1..345
FT /note="RISC-loading complex subunit tarbp2"
FT /id="PRO_0000373973"
FT DOMAIN 30..97
FT /note="DRBM 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT DOMAIN 140..208
FT /note="DRBM 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT DOMAIN 272..340
FT /note="DRBM 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT REGION 118..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 37199 MW; 4615CAE3300F4243 CRC64;
MNDETASDSW KRNSGCSSIE QMLAVNPGKT PISLLQEYGT RIGKTPVYDL LKAEGQAHQP
NFTFRVAVGE INCTGQGPSK KAAKHKAAEA ALKMLKGGLG APAGFSVGVD GFVEVDVSTD
GDSSQSEMKT SGNSQQTECN PVGALQELVV QKGWRLPEYT VTQESGPAHR KEFTMTCRVE
RFIEIGSGTS KKLAKRNAAA KMLSRIHDVP VDLRTSNDAD PEEDTFNMHM GSRTESGKSK
SFSCTWDSLR NSAGEKILQL RSHPLGIPTD SNFCSLLSDL SLEQRFDVSY LDLEERSLSG
LCQCLVELST QPITVCHGCA SSTDAARASA AHNALQYLKI MAGGK
