TOFU6_CAEEL
ID TOFU6_CAEEL Reviewed; 367 AA.
AC Q09293; Q9BMU5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Embryonic developmental protein tofu-6 {ECO:0000305};
DE AltName: Full=21U-RNA biogenesis fouled up protein 6 {ECO:0000312|WormBase:EEED8.1};
DE AltName: Full=Maternal effect lethal protein 47 {ECO:0000305};
GN Name=tofu-6 {ECO:0000312|WormBase:EEED8.1};
GN Synonyms=mel-47 {ECO:0000312|WormBase:EEED8.1};
GN ORFNames=EEED8.1 {ECO:0000312|WormBase:EEED8.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Bristol N2;
RA Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA Thierry-Mieg D., Thierry-Mieg J.;
RT "The Caenorhabditis elegans transcriptome project, a complementary view of
RT the genome.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17171368; DOI=10.1007/s00438-006-0191-z;
RA Minasaki R., Streit A.;
RT "MEL-47, a novel protein required for early cell divisions in the nematode
RT Caenorhabditis elegans.";
RL Mol. Genet. Genomics 277:315-328(2007).
RN [4]
RP FUNCTION, IDENTIFICATION IN THE PETISCO COMPLEXES, INTERACTION WITH IFE-3;
RP PID-3; PID-1; TOST-1 AND ERH-2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 52-GLN--LEU-367; 144-SER--SER-253 AND 270-TRP--LEU-367.
RX PubMed=31216475; DOI=10.1016/j.celrep.2019.05.076;
RA Zeng C., Weng C., Wang X., Yan Y.H., Li W.J., Xu D., Hong M., Liao S.,
RA Dong M.Q., Feng X., Xu C., Guang S.;
RT "Functional Proteomics Identifies a PICS Complex Required for piRNA
RT Maturation and Chromosome Segregation.";
RL Cell Rep. 27:3561-3572(2019).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE PETISCO COMPLEXES, INTERACTION WITH IFE-3
RP AND PID-3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 52-GLN--LEU-367 AND
RP 270-TRP--LEU-367.
RX PubMed=31147388; DOI=10.1101/gad.322446.118;
RA Cordeiro Rodrigues R.J., de Jesus Domingues A.M., Hellmann S., Dietz S.,
RA de Albuquerque B.F.M., Renz C., Ulrich H.D., Sarkies P., Butter F.,
RA Ketting R.F.;
RT "PETISCO is a novel protein complex required for 21U RNA biogenesis and
RT embryonic viability.";
RL Genes Dev. 33:857-870(2019).
CC -!- FUNCTION: Component of the pid-1 and tost-1 variants of the PETISCO
CC complexes, which have roles in the biogenesis of a class of 21
CC nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue
CC at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively
CC (PubMed:31147388, PubMed:31216475). Promotes the biogenesis of 21U-RNAs
CC (PubMed:31216475). Required for chromosome segregation and cell
CC division in early embryos (PubMed:17171368, PubMed:31216475). May have
CC a role in DNA replication (PubMed:17171368).
CC {ECO:0000269|PubMed:17171368, ECO:0000269|PubMed:31147388,
CC ECO:0000269|PubMed:31216475, ECO:0000305|PubMed:31216475}.
CC -!- SUBUNIT: Component of the pid-1 variant of the PETISCO complex (also
CC called the pid-3, erh-2, tofu-6, and ife-3 small RNA complex)
CC containing at least pid-1, tofu-6, ife-3, pid-3, and erh-2, which is
CC required for the biogenesis of 21 nucleotide PIWI-interacting RNAs
CC (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-
CC RNAs) (PubMed:31147388, PubMed:31216475). Within the pid-1 variant of
CC the PETISCO complex interacts with pid-1 (PubMed:31216475). Component
CC of the tost-1 variant of the PETISCO complex (also called the pid-3,
CC erh-2, tofu-6, and ife-3 small RNA complex) containing at least tost-1,
CC tofu-6, ife-3, pid-3, and erh-2, which plays an essential role in
CC embryogenesis (PubMed:31147388, PubMed:31216475). Within the tost-1
CC variant of the PETISCO complex interacts with tost-1 (PubMed:31216475).
CC Within the pid-1 and tost-1 variants of the PETISCO complexes interacts
CC (via C-terminus) with ife-3 (PubMed:31216475, PubMed:31147388). Within
CC the pid-1 and tost-1 variants of the PETISCO complexes interacts (via
CC the RRM domain) with pid-3 (PubMed:31216475, PubMed:31147388). Within
CC the pid-1 and tost-1 variants of the PETISCO complexes interacts (via
CC the RRM domain) with erh-2 (PubMed:31216475). In contrast to the pid-1
CC variant of the PETISCO complex, the tost-1 variant of the PETISCO
CC complex plays a minor role in the biogenesis of 21U-RNAs
CC (PubMed:31147388). {ECO:0000269|PubMed:31147388,
CC ECO:0000269|PubMed:31216475, ECO:0000305|PubMed:31216475}.
CC -!- INTERACTION:
CC Q09293; O61955: ife-3; NbExp=5; IntAct=EBI-2001908, EBI-330119;
CC Q09293; O76616: pid-3; NbExp=8; IntAct=EBI-2001908, EBI-2415582;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31147388,
CC ECO:0000269|PubMed:31216475}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}. Nucleus
CC {ECO:0000269|PubMed:31216475}. Note=Dispersedly distributes throughout
CC the cytoplasm in early embryos (PubMed:31147388). During early
CC embryogenesis, localizes to the nucleus at prophase of cell division,
CC and remains in the cytosol at interphase in 2- and 4-cell embryos
CC (PubMed:31216475). Does not localize to cytoplasmic granules in oocytes
CC and embryos (PubMed:31216475). Localizes to puncta in the perinuclear
CC region in the germline syncytium (PubMed:31147388, PubMed:31216475).
CC Localization to the perinuclear region in the germline is dependent on
CC pid-1, tost-1, pics-1 and erh-2 (PubMed:31216475).
CC {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
CC -!- TISSUE SPECIFICITY: Expression is restricted to the germline (at
CC protein level). {ECO:0000269|PubMed:17171368,
CC ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Relatively high levels of expression in early embryos, weakly
CC detectable in subsequent developmental stages and enriched in adults
CC (at protein level) (PubMed:31147388). During early embryogenesis,
CC expressed during prophase and interphase in 2- and 4-cell embryos
CC (PubMed:31216475). {ECO:0000269|PubMed:17171368,
CC ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
CC -!- DISRUPTION PHENOTYPE: Worms whose mothers are lacking mel-47 exhibit
CC prolonged interphase between the two and four cell stages of
CC development. Mutants arrest as early embryos ranging from 50 to 80
CC cells with no signs of morphogenesis. Chromatin bridges which connect
CC nuclei remain present after cytokinesis appears complete. RNAi-mediated
CC knockdown results in maternal effect lethal (Mel phenotype)
CC (PubMed:31147388). RNAi-mediated knockdown results in chromosome
CC segregation and cell division defects in early embryos
CC (PubMed:31216475). RNAi-mediated knockdown results in defective
CC activity of the PIWI-interacting RNA (piRNA) silencing pathway
CC (PubMed:31147388). RNAi-mediated knockdown results in the failure of
CC pid-1, pid-3 and erh-2 to localize to perinuclear granules, but instead
CC they accumulate in the nucleus (PubMed:31216475).
CC {ECO:0000269|PubMed:17171368, ECO:0000269|PubMed:31147388,
CC ECO:0000269|PubMed:31216475}.
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DR EMBL; BX284602; CCD68728.1; -; Genomic_DNA.
DR EMBL; AF303251; AAG50209.1; -; mRNA.
DR RefSeq; NP_001293507.1; NM_001306578.1.
DR PDB; 7D1L; X-ray; 1.95 A; A/B=1-92.
DR PDB; 7D2Y; X-ray; 2.68 A; A/B=1-92.
DR PDB; 7OCX; X-ray; 1.70 A; C/D=1-99.
DR PDBsum; 7D1L; -.
DR PDBsum; 7D2Y; -.
DR PDBsum; 7OCX; -.
DR AlphaFoldDB; Q09293; -.
DR SMR; Q09293; -.
DR ComplexPortal; CPX-4306; PETISCO, pid-1 variant.
DR ComplexPortal; CPX-4307; PETISCO, tost-1 variant.
DR IntAct; Q09293; 10.
DR STRING; 6239.EEED8.1.2; -.
DR iPTMnet; Q09293; -.
DR EPD; Q09293; -.
DR PaxDb; Q09293; -.
DR PeptideAtlas; Q09293; -.
DR EnsemblMetazoa; EEED8.1.1; EEED8.1.1; WBGene00017132.
DR GeneID; 24104386; -.
DR KEGG; cel:CELE_EEED8.1; -.
DR UCSC; EEED8.1.1; c. elegans.
DR CTD; 24104386; -.
DR WormBase; EEED8.1; CE26746; WBGene00017132; tofu-6.
DR eggNOG; ENOG502SX3Q; Eukaryota.
DR HOGENOM; CLU_754855_0_0_1; -.
DR InParanoid; Q09293; -.
DR OMA; NDWNLFH; -.
DR OrthoDB; 915062at2759; -.
DR PRO; PR:Q09293; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00017132; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0034518; C:RNA cap binding complex; IPI:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034585; P:21U-RNA metabolic process; IC:ComplexPortal.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0040016; P:embryonic cleavage; IMP:WormBase.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IMP:WormBase.
DR GO; GO:1990511; P:piRNA biosynthetic process; IMP:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:UniProtKB.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IMP:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW Developmental protein; Nucleus; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..367
FT /note="Embryonic developmental protein tofu-6"
FT /id="PRO_0000082014"
FT DOMAIN 13..92
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 298..345
FT /note="Required for ife-3 interaction"
FT /evidence="ECO:0000269|PubMed:31216475"
FT MUTAGEN 52..367
FT /note="Missing: In it20; embryonic lethal with embryos
FT arresting between the 64-128 cell stage. Reduces the number
FT of type I and II 21U-RNAs (a class of 21 nucleotide PIWI-
FT interacting RNAs (piRNAs) that possess a uracil residue at
FT the 5'-end)."
FT /evidence="ECO:0000269|PubMed:31147388,
FT ECO:0000269|PubMed:31216475"
FT MUTAGEN 144..253
FT /note="Missing: In ust95; reduces the accumulation of type
FT I and II 21U-RNAs. Unlike wild-type, does not localize to
FT perinuclear foci. Does not cause sterility. Does not
FT exhibit chromosome segregation defects."
FT /evidence="ECO:0000269|PubMed:31216475"
FT MUTAGEN 270..367
FT /note="Missing: In y2; sterile. Maternal effect lethal
FT (Mel) phenotype. Reduces the number of type I and II 21U-
FT RNAs (a class of 21 nucleotide PIWI-interacting RNAs
FT (piRNAs) that possess a uracil residue at the 5'-end)."
FT /evidence="ECO:0000269|PubMed:31147388,
FT ECO:0000269|PubMed:31216475"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:7OCX"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:7OCX"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:7OCX"
FT STRAND 49..62
FT /evidence="ECO:0007829|PDB:7OCX"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:7OCX"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:7OCX"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:7OCX"
SQ SEQUENCE 367 AA; 41102 MW; BF614E40CFC97A8B CRC64;
MASSSTAYYL KDAGFHIRNI PKAWNDWNLF HVFQNFGKVS YCRVVGQSND GQVQLGFVNM
MSVADADEVR KNLNDGNLIG ENFTLKVTDH KNVGGSLLPM ASNSVQKLVS SPPSKSGPVL
LSSSWLPLNK DIEVEVVDYL PSSSVAPDLF ALTLLRINDS SMKEKYDSMH EKMNAYAQIV
PFDSELEIGY DGVFRDAPRS VRRVRRISAT KLYLVDFGKI INYEKAKCFQ LPKVFQSMPT
RVSLCGLDGL TWSPVAIPSF DNIREVVKKW GQMENSTLHA MACGFQGSIN MINLFCGKSI
LADRLQRKGV CEYLPRSQQP HYAYSRETLL QHNNSGVTAQ ISNDADVVKD LLKKIDGVKN
MLRELEL
