ID A0A3Q2VXQ9_HAPBU Unreviewed; 345 AA.
AC A0A3Q2VXQ9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=RISC-loading complex subunit TARBP2 {ECO:0000256|HAMAP-Rule:MF_03034};
GN Name=TARBP2 {ECO:0000256|HAMAP-Rule:MF_03034};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000016685.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000016685.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|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:0000256|HAMAP-Rule:MF_03034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03034}.
CC -!- SIMILARITY: Belongs to the TARBP2 family. {ECO:0000256|HAMAP-
CC Rule:MF_03034}.
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 RefSeq; XP_005944378.1; XM_005944316.2.
DR AlphaFoldDB; A0A3Q2VXQ9; -.
DR STRING; 8153.ENSHBUP00000016685; -.
DR Ensembl; ENSHBUT00000025269.1; ENSHBUP00000016685.1; ENSHBUG00000018639.1.
DR GeneID; 102305755; -.
DR CTD; 6895; -.
DR GeneTree; ENSGT00940000157748; -.
DR OMA; QDKDAMG; -.
DR OrthoDB; 3130057at2759; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016442; C:RISC complex; IEA:UniProtKB-UniRule.
DR GO; GO:0070578; C:RISC-loading complex; IEA:InterPro.
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:0098795; P:global gene silencing by mRNA cleavage; IEA:UniProtKB-UniRule.
DR GO; GO:0031054; P:pre-miRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:1903798; P:regulation of miRNA processing; IEA:InterPro.
DR GO; GO:0070921; P:regulation of siRNA processing; 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:0070922; P:RISC complex assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0030422; P:siRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd10844; DSRM_TARBP2_rpt2; 1.
DR CDD; cd19893; DSRM_TARBP2_rpt3; 1.
DR Gene3D; 3.30.160.20; -; 3.
DR HAMAP; MF_03034; TRBP2; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR028605; TRBP2.
DR InterPro; IPR044470; TRBP2_DSRM_2.
DR InterPro; IPR044471; TRBP2_DSRM_3.
DR PANTHER; PTHR46205; LOQUACIOUS, ISOFORM B; 1.
DR PANTHER; PTHR46205:SF1; RISC-LOADING COMPLEX SUBUNIT TARBP2; 1.
DR Pfam; PF00035; dsrm; 2.
DR SMART; SM00358; DSRM; 3.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 3.
DR PROSITE; PS50137; DS_RBD; 3.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03034};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03034};
KW RNA-mediated gene silencing {ECO:0000256|HAMAP-Rule:MF_03034};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW Rule:MF_03034}.
FT DOMAIN 30..97
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 140..208
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 272..340
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
SQ SEQUENCE 345 AA; 37041 MW; E444D36C8F49D970 CRC64;
MNDETASDSW KRNSGCSSIE QMLAVNPGKT PISLLQEYGT RIGKTPVYDL LKAEGQAHQP
NFTFRVSVGE ISCTGQGPSK KAAKHKAAEA ALKMLKGGLG GPAGVGIGVD GFIGVDVSTD
ADGAQSEMKT TGTSQQSECN PVGALQELVV QKGWRLPEYT VTQESGPAHR KEFTMTCRVE
RFVEIGSGTS KKLAKRNAAA KMLSRIHDVP VDMRTSNDPD AEDDTFTMNM GSRVESGKSK
GFSCTWDSLR NSAGEKILQL RSHPLGMPSD SNFCSLLSEL SLEQRFDVSY LDLEERSLSG
LCQCLVELST QPITVCHGFA PNTDGARANA AHNALQYLKI MAGGK
//
