ID A0A3B3ZTP4_9GOBI Unreviewed; 345 AA.
AC A0A3B3ZTP4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=RISC-loading complex subunit TARBP2 {ECO:0000256|HAMAP-Rule:MF_03034};
GN Name=TARBP2 {ECO:0000256|HAMAP-Rule:MF_03034};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000007844.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000007844.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B3ZTP4; -.
DR STRING; 409849.ENSPMGP00000007844; -.
DR Ensembl; ENSPMGT00000008350.1; ENSPMGP00000007844.1; ENSPMGG00000006497.1.
DR OrthoDB; 3130057at2759; -.
DR Proteomes; UP000261520; 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; cd19890; DSRM_TARBP2_rpt1; 1.
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; IPR044469; TRBP2_DSRM_1.
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 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"
FT REGION 120..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 37185 MW; CCFD9578CACC2228 CRC64;
MNDEIAPDSW KRNSGCSSIE QMLAVNPGKT PISLLQEYGT RIGKTPVYDL LKAEGQAHQP
NFTFRVSVGE ISCTGQGPSK KAAKHKAAEA ALKMLKGGLG GPFGVSTDVD GLIGVDVAVD
GDSSPSDMKT SSNSQQSECN PVGALQELVV QKGWRLPEYT VTQESGPAHR KEFTMTCRVE
RFMEIGSGTS KKLAKRNAAA KMLSRIHDVP VDLRSSNEAD AEDDTFTLHM GSRADSGKSK
SFSCTWDSLR NSAGEKILQL RSHPLGIPSD SNFCSLLTDL STEQRFDVSY LDLEERSLSG
LCQCLVELST QPITVCHGFA PSVDDARANA AYNALQYLKI MAGGK
//
