ERH2_CAEEL
ID ERH2_CAEEL Reviewed; 113 AA.
AC Q20057;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Enhancer of rudimentary homolog 2 {ECO:0000312|WormBase:F35G12.11};
GN Name=erh-2 {ECO:0000312|WormBase:F35G12.11};
GN ORFNames=F35G12.11 {ECO:0000312|WormBase:F35G12.11};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE PETISCO COMPLEXES, INTERACTION WITH PID-1;
RP TOST-1; TOFU-6 AND PID-3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
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 [3] {ECO:0000305}
RP FUNCTION, SUBUNIT, IDENTIFICATION IN THE PETISCO COMPLEXES, INTERACTION
RP WITH PID-1; TOST-1 AND PID-3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
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: Required for chromosome segregation and cell division in
CC early embryos (PubMed:31216475). Component of the pid-1 and tost-1
CC variants of the PETISCO complexes, which have roles in the biogenesis
CC of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess
CC a uracil residue at the 5'-end (also called 21U-RNAs) and
CC embryogenesis, respectively (PubMed:31147388, PubMed:31216475). Within
CC the tost-1 variant of the PETISCO complex binds to splice leader SL1
CC RNA fragments to possibly play a role in their processing
CC (PubMed:31147388). Promotes the biogenesis of 21U-RNAs
CC (PubMed:31216475). {ECO:0000269|PubMed:31147388,
CC ECO:0000269|PubMed:31216475, ECO:0000305|PubMed:31216475}.
CC -!- SUBUNIT: May form a homodimer (PubMed:31147388). Component of the pid-1
CC variant of the PETISCO complex (also called the pid-3, erh-2, tofu-6,
CC and ife-3 small RNA complex) containing at least pid-1, tofu-6, ife-3,
CC pid-3, and erh-2, which is required for 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) (PubMed:31147388,
CC PubMed:31216475). Within the complex interacts with pid-1
CC (PubMed:31147388, PubMed:31216475). Component of the tost-1 variant of
CC the PETISCO complex (also called the pid-3, erh-2, tofu-6, and ife-3
CC small RNA complex) containing at least tost-1, tofu-6, ife-3, pid-3,
CC and erh-2, which plays an essential role in embryogenesis
CC (PubMed:31147388, PubMed:31216475). Within the complex interacts with
CC tost-1 (PubMed:31216475, PubMed:31147388). Within the pid-1 and tost-1
CC variants of the PETISCO complexes interacts with pid-3
CC (PubMed:31216475, PubMed:31147388). Within the pid-1 and tost-1
CC variants of the PETISCO complexes interacts with tofu-6 (via the RRM
CC domain) (PubMed:31216475). In contrast to the pid-1 variant of the
CC PETISCO complex, the tost-1 variant of the PETISCO complex plays a
CC minor role in the biogenesis of 21U-RNAs (PubMed:31147388).
CC {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475,
CC ECO:0000305|PubMed:31216475}.
CC -!- INTERACTION:
CC Q20057; Q19541: pid-1; NbExp=4; IntAct=EBI-21447087, EBI-21447100;
CC Q20057; O76616: pid-3; NbExp=5; IntAct=EBI-21447087, EBI-2415582;
CC Q20057; Q18490: tost-1; NbExp=3; IntAct=EBI-21447087, EBI-21447173;
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). Localizes to puncta in the perinuclear region in the
CC germline syncytium (PubMed:31216475, PubMed:31147388).
CC {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline (at protein level).
CC {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
CC -!- DEVELOPMENTAL STAGE: Expressed from early embryogenesis (at protein
CC level) (PubMed:31147388). During early embryogenesis, expressed during
CC prophase and interphase in 2- and 4-cell embryos (PubMed:31216475).
CC {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
CC -!- DISRUPTION PHENOTYPE: 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 disrupts the localization of
CC tofu-6 to the perinuclear region of the germline (PubMed:31216475).
CC RNAi-mediated knockdown results in larger tofu-6- and pid-3-expressing
CC foci (PubMed:31216475). RNAi-mediated knockdown results in decreased
CC expression of tost-1 in the germline and in embryos (PubMed:31216475).
CC {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
CC -!- SIMILARITY: Belongs to the E(R) family. {ECO:0000305}.
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DR EMBL; BX284603; CAA86333.2; -; Genomic_DNA.
DR PIR; T21807; T21807.
DR RefSeq; NP_497936.2; NM_065535.5.
DR PDB; 7EJO; X-ray; 2.19 A; A/B=1-103.
DR PDB; 7EJS; X-ray; 2.39 A; A/B=1-103.
DR PDB; 7O6L; X-ray; 1.50 A; A/B=1-99.
DR PDB; 7O6N; X-ray; 2.17 A; A/B=1-99.
DR PDBsum; 7EJO; -.
DR PDBsum; 7EJS; -.
DR PDBsum; 7O6L; -.
DR PDBsum; 7O6N; -.
DR AlphaFoldDB; Q20057; -.
DR SMR; Q20057; -.
DR ComplexPortal; CPX-4306; PETISCO, pid-1 variant.
DR ComplexPortal; CPX-4307; PETISCO, tost-1 variant.
DR IntAct; Q20057; 11.
DR STRING; 6239.F35G12.11.2; -.
DR EPD; Q20057; -.
DR PaxDb; Q20057; -.
DR PeptideAtlas; Q20057; -.
DR EnsemblMetazoa; F35G12.11.1; F35G12.11.1; WBGene00009444.
DR GeneID; 185323; -.
DR KEGG; cel:CELE_F35G12.11; -.
DR UCSC; F35G12.11.1; c. elegans.
DR CTD; 185323; -.
DR WormBase; F35G12.11; CE36485; WBGene00009444; erh-2.
DR eggNOG; KOG1766; Eukaryota.
DR GeneTree; ENSGT00390000003316; -.
DR HOGENOM; CLU_125703_1_0_1; -.
DR InParanoid; Q20057; -.
DR OMA; RETGQYI; -.
DR OrthoDB; 1512482at2759; -.
DR PhylomeDB; Q20057; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00009444; 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:0034585; P:21U-RNA metabolic process; IC:ComplexPortal.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IC:ComplexPortal.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
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; 3.30.2260.10; -; 1.
DR InterPro; IPR035912; EHR_sf.
DR InterPro; IPR000781; ERH.
DR PANTHER; PTHR12373; PTHR12373; 1.
DR Pfam; PF01133; ER; 1.
DR PIRSF; PIRSF016393; Enh_rudimentary; 1.
DR SUPFAM; SSF143875; SSF143875; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW Nucleus; Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..113
FT /note="Enhancer of rudimentary homolog 2"
FT /id="PRO_0000452465"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:7O6L"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:7O6N"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:7O6L"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:7O6L"
FT HELIX 28..43
FT /evidence="ECO:0007829|PDB:7O6L"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:7O6L"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:7O6L"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:7O6L"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:7O6L"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:7O6L"
SQ SEQUENCE 113 AA; 12972 MW; B0DC0A2ECAD40FFE CRC64;
MSTSSHTVLL IQTSPRLDSR TWGDYESVTD ALDALCKMFE DFLSKKSAAP VTYDVSQVYE
FLDKLSDVSM MIFNRETGQY IGRTRAWIKQ QVYEMMRGRC QHPEGGEKVI VGY
