ID M3W8A9_FELCA Unreviewed; 366 AA.
AC M3W8A9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=RISC-loading complex subunit TARBP2 {ECO:0000256|HAMAP-Rule:MF_03034};
GN Name=TARBP2 {ECO:0000256|HAMAP-Rule:MF_03034,
GN ECO:0000313|Ensembl:ENSFCAP00000007182.3,
GN ECO:0000313|VGNC:VGNC:65954};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000007182.3, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000007182.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000007182.3,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000007182.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000007182.3,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000007182.3}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000007182.3};
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. 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:0000256|HAMAP-
CC Rule:MF_03034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03034}.
CC Cytoplasm, perinuclear region {ECO:0000256|HAMAP-Rule:MF_03034}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03034}.
CC -!- SIMILARITY: Belongs to the TARBP2 family. {ECO:0000256|HAMAP-
CC Rule:MF_03034}.
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DR EMBL; AANG04001751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003988820.1; XM_003988771.4.
DR AlphaFoldDB; M3W8A9; -.
DR STRING; 9685.ENSFCAP00000007182; -.
DR PaxDb; 9685-ENSFCAP00000007182; -.
DR Ensembl; ENSFCAT00000007759.6; ENSFCAP00000007182.3; ENSFCAG00000007757.6.
DR GeneID; 101087415; -.
DR KEGG; fca:101087415; -.
DR CTD; 6895; -.
DR VGNC; VGNC:65954; TARBP2.
DR eggNOG; KOG3732; Eukaryota.
DR GeneTree; ENSGT00940000157748; -.
DR HOGENOM; CLU_048292_2_0_1; -.
DR InParanoid; M3W8A9; -.
DR OMA; QDKDAMG; -.
DR OrthoDB; 3130057at2759; -.
DR Proteomes; UP000011712; Chromosome B4.
DR Bgee; ENSFCAG00000007757; Expressed in eyeball of camera-type eye and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0070578; C:RISC-loading complex; IBA:GO_Central.
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:0140311; F:protein sequestering activity; IEA:Ensembl.
DR GO; GO:0035197; F:siRNA binding; IBA:GO_Central.
DR GO; GO:0098795; P:global gene silencing by mRNA cleavage; IEA:UniProtKB-UniRule.
DR GO; GO:0039532; P:negative regulation of cytoplasmic pattern recognition receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0050689; P:negative regulation of defense response to virus by host; IEA:Ensembl.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
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:0070920; P:regulation of regulatory ncRNA processing; IBA:GO_Central.
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:Ensembl.
DR GO; GO:0070922; P:RISC complex assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
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 Nucleus {ECO:0000256|HAMAP-Rule:MF_03034};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
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 159..227
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 293..361
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 22..105
FT /note="Sufficient for interaction with PRKRA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03034"
FT REGION 136..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:0000256|HAMAP-Rule:MF_03034"
FT REGION 228..366
FT /note="Sufficient for interaction with DICER1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03034"
FT REGION 287..366
FT /note="Sufficient for interaction with PRKRA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03034"
SQ SEQUENCE 366 AA; 38799 MW; 64B0D12F177FB844 CRC64;
MSEEEQGSGT TTGCGLPSIE QMLAANPGKT PISLLQEYGT RIGKTPVYDL LKAEGQAHQP
NFTFRVTVGD TSCTGQGPSK KAAKHKAAEV ALKHLKGGSM LEPALEDSSS FSPLDSSLPE
DIPVFTAAVA ATPVPSAVPT RSPPMEVQPP VSPQQSECNP VGALQELVVQ KGWRLPEYTV
TQESGPAHRK EFTMTCRVER FVEIGSGTSK KLAKRNAAAK MLLRVHTVPL DARDGNEAEP
DDDHFSIGVG SRLDGLRNRG PGCTWDSLRN SVGEKILSLR SCSLGALGAL GPACCSVLSE
LSEEQAFHVS YLDIEELSLS GLCQCLVELS TQPATVCHGS AATREAARGE AACRALQYLK
IMAGSK
//
