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Database: UniProt
Entry: G1PF18_MYOLU
LinkDB: G1PF18_MYOLU
Original site: G1PF18_MYOLU 
ID   G1PF18_MYOLU            Unreviewed;       366 AA.
AC   G1PF18;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
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:ENSMLUP00000009139.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000009139.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000009139.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000009139.2}
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. 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; AAPE02030927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02030928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006095816.1; XM_006095754.2.
DR   AlphaFoldDB; G1PF18; -.
DR   STRING; 59463.ENSMLUP00000009139; -.
DR   Ensembl; ENSMLUT00000010027.2; ENSMLUP00000009139.2; ENSMLUG00000010035.2.
DR   GeneID; 102424011; -.
DR   KEGG; mlf:102424011; -.
DR   CTD; 6895; -.
DR   eggNOG; KOG3732; Eukaryota.
DR   GeneTree; ENSGT00940000157748; -.
DR   HOGENOM; CLU_048292_2_0_1; -.
DR   InParanoid; G1PF18; -.
DR   OMA; QDKDAMG; -.
DR   OrthoDB; 3130057at2759; -.
DR   TreeFam; TF315953; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016442; C:RISC complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0070578; C:RISC-loading complex; IEA:Ensembl.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
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; IEA:UniProtKB-UniRule.
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: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; 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   Nucleus {ECO:0000256|HAMAP-Rule:MF_03034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074};
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          135..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;  38840 MW;  287F5BAAE0D7515F CRC64;
     MSEEEQGSGT TTGCGLPSIE QMLAANPGKT PISLLQEYGT RIGKTPVYDL LKAEGQAHQP
     NFTFRVTVGD TSCTGQGPSK KAAKHKAAEV ALKHLKGGSM LEPALEDSSS FSPLDSSLPE
     DGPVFTAAAA ATPVPSALPT RSPPMEVQPP VSPQQSECNP VGALQELVVQ KGWRLPEYTV
     TQESGPAHRK EFTMTCRVER FVEIGSGTSK KLAKRNAAAK MLLRVHTVPL DARDGNEAEP
     DDDHFSIGVG SRLDGLRNRG PGCTWDSLRN SVGEKILSLR SCSLGSLGAL GPACCSVLSE
     LSEEQAFHVS YLDIEELSLS GLCQCLVELS TQPITVCHGS AATREAARGE AARRALQYLK
     IMAGSK
//
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