PID3_CAEEL
ID PID3_CAEEL Reviewed; 307 AA.
AC O76616;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein pid-3 {ECO:0000305};
DE AltName: Full=piRNA biogenesis and chromosome segregation protein 1 {ECO:0000303|PubMed:31216475};
DE AltName: Full=piRNA-induced silencing defective protein 3 {ECO:0000312|WormBase:Y23H5A.3};
GN Name=pid-3 {ECO:0000312|WormBase:Y23H5A.3};
GN Synonyms=pics-1 {ECO:0000303|PubMed:31216475,
GN ECO:0000312|WormBase:Y23H5A.3};
GN ORFNames=Y23H5A.3 {ECO:0000312|WormBase:Y23H5A.3};
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 TOFU-6; TOST-1 AND ERH-2, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP 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, IDENTIFICATION IN THE PETISCO COMPLEXES, INTERACTION WITH PID-1;
RP TOFU-6 AND ERH-2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP 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: 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). Within the pid-1 variant of the
CC PETISCO complex may stabilize 21U-RNA precursor molecules
CC (PubMed:31147388). Promotes the biogenesis of 21U-RNAs
CC (PubMed:31216475). Required for chromosome segregation and cell
CC division in early embryos (PubMed:31216475).
CC {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475,
CC 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 a class of 21 nucleotide PIWI-
CC interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end
CC (also called 21U-RNAs) (PubMed:31147388, PubMed:31216475). Within the
CC complex interacts with pid-1; the interaction is direct
CC (PubMed:31216475, PubMed:31147388). 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). Within the pid-1 and tost-1 variants of the
CC PETISCO complexes interacts with tofu-6 (via the RRM domain) and erh-2
CC (PubMed:31216475, PubMed:31147388). In contrast to the pid-1 variant of
CC the 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 O76616; Q20057: erh-2; NbExp=5; IntAct=EBI-2415582, EBI-21447087;
CC O76616; Q19541: pid-1; NbExp=4; IntAct=EBI-2415582, EBI-21447100;
CC O76616; Q09293: tofu-6; NbExp=8; IntAct=EBI-2415582, EBI-2001908;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31147388}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:31147388}. 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:31147388). {ECO:0000269|PubMed:31147388,
CC ECO:0000269|PubMed:31216475}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline (at protein level).
CC {ECO:0000269|PubMed:31147388}.
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 and erh-2 to the perinuclear region of the germline
CC (PubMed:31216475). Instead erh-2 accumulates in the nucleus
CC (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}.
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DR EMBL; BX284601; CCD70910.1; -; Genomic_DNA.
DR PIR; F87729; F87729.
DR RefSeq; NP_491011.1; NM_058610.5.
DR PDB; 7D1L; X-ray; 1.95 A; C/D=201-282.
DR PDB; 7D2Y; X-ray; 2.68 A; C/D=200-282.
DR PDB; 7EJS; X-ray; 2.39 A; A/B=179-200.
DR PDB; 7O6N; X-ray; 2.17 A; C/D=171-203.
DR PDB; 7OCX; X-ray; 1.70 A; A/B=196-274.
DR PDB; 7OCZ; X-ray; 1.82 A; A/B=196-274.
DR PDBsum; 7D1L; -.
DR PDBsum; 7D2Y; -.
DR PDBsum; 7EJS; -.
DR PDBsum; 7O6N; -.
DR PDBsum; 7OCX; -.
DR PDBsum; 7OCZ; -.
DR AlphaFoldDB; O76616; -.
DR SMR; O76616; -.
DR ComplexPortal; CPX-4306; PETISCO, pid-1 variant.
DR ComplexPortal; CPX-4307; PETISCO, tost-1 variant.
DR IntAct; O76616; 7.
DR STRING; 6239.Y23H5A.3; -.
DR EPD; O76616; -.
DR PaxDb; O76616; -.
DR PeptideAtlas; O76616; -.
DR EnsemblMetazoa; Y23H5A.3.1; Y23H5A.3.1; WBGene00021270.
DR GeneID; 171819; -.
DR KEGG; cel:CELE_Y23H5A.3; -.
DR UCSC; Y23H5A.3; c. elegans.
DR CTD; 171819; -.
DR WormBase; Y23H5A.3; CE18359; WBGene00021270; pid-3.
DR eggNOG; ENOG502ST2D; Eukaryota.
DR HOGENOM; CLU_062695_0_0_1; -.
DR InParanoid; O76616; -.
DR OMA; PWALICS; -.
DR OrthoDB; 1067864at2759; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00021270; 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.
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..307
FT /note="Protein pid-3"
FT /id="PRO_0000452466"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:7O6N"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:7OCX"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:7OCX"
FT HELIX 216..222
FT /evidence="ECO:0007829|PDB:7OCX"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:7OCX"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:7OCX"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:7OCX"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:7OCX"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:7OCX"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:7OCX"
SQ SEQUENCE 307 AA; 34799 MW; C67F7BB3C9FC4C10 CRC64;
MVAHQKADFK SKWAMVVTVN NLNDKKRADL REFSEWFIET LRLEGAFIGH YFNYEAAPVT
IVETLPGNFD SCTNAYQKIH KEHPQVVLVV HILPQSQSNE YEWMKVLASR YGFVRQGLLY
DNCANRFQNV ETDQNSVFRN MCQWIYRSGT AIVRNEGNAC GILHGKDPKP TFDKVLFNSE
DIKDSVFKVL HAEEEPRGAD QENMLKISGY PGMLNTFGIA QLLTPYRVNG ITITGAQSAV
VALENKFQVY QAVQDFNGKK LDRNHKLQVS SLVVSSPAVP LEWPSLKKSK KLVEQVGKPI
RLSKVSS
