ID   TRBP2_XENLA             Reviewed;         351 AA.
AC   Q6GPZ1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=RISC-loading complex subunit tarbp2 {ECO:0000255|HAMAP-Rule:MF_03034};
GN   Name=tarbp2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH72963.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC072963; AAH72963.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001085574.1; NM_001092105.1.
DR   AlphaFoldDB; Q6GPZ1; -.
DR   SMR; Q6GPZ1; -.
DR   DNASU; 444000; -.
DR   GeneID; 444000; -.
DR   KEGG; xla:444000; -.
DR   CTD; 444000; -.
DR   Xenbase; XB-GENE-866097; tarbp2.L.
DR   OrthoDB; 1093169at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 444000; Expressed in ovary and 20 other tissues.
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   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome; Repeat; RNA-binding;
KW   RNA-mediated gene silencing; Translation regulation.
FT   CHAIN           1..351
FT                   /note="RISC-loading complex subunit tarbp2"
FT                   /id="PRO_0000373974"
FT   DOMAIN          29..96
FT                   /note="DRBM 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT   DOMAIN          150..218
FT                   /note="DRBM 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT   DOMAIN          278..346
FT                   /note="DRBM 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03034"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   351 AA;  38172 MW;  B3DC45024247B6AC CRC64;
     MSENGDCEHQ TSSGFPSIEQ MLASSPGKTP ISLLQEYGTR VGKTPVYDLL KAEGQAHQPN
     FTFRVSVGDI NCTGQGPSKK AAKHKAAEVA LSLLKEGEMF GVMCEENSVV LSVEQPAELK
     EVADVSPPPT TRNHTIEMKP PLSAQQSECN PVGALQELVV QKGWRLPEYT VTQESGPAHR
     KEFTMTCRVE RFLEIGSGTS KKLAKRNAAA KMLLQIHQVP AEHRESGETE PEEDQFSVGK
     LDGSRSRGTA CTWDSLRNSS GEKILHLRSN PLTILSSGFC SLLQDLSEEQ SFQISYLDID
     ERSLSGLCQC LVELSTQPTT VCHGSATTRD AARANAAHNA LQYLKIMAGG K