PID1_CAEEL
ID PID1_CAEEL Reviewed; 169 AA.
AC Q19541;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein pid-1 {ECO:0000305|PubMed:24696453};
DE AltName: Full=PiRNA-induced silencing defective protein 1 {ECO:0000312|WormBase:F18A1.8};
GN Name=pid-1 {ECO:0000312|WormBase:F18A1.8};
GN ORFNames=F18A1.8 {ECO:0000312|WormBase:F18A1.8};
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ARG-61.
RX PubMed=24696453; DOI=10.1101/gad.238220.114;
RA de Albuquerque B.F., Luteijn M.J., Cordeiro Rodrigues R.J.,
RA van Bergeijk P., Waaijers S., Kaaij L.J., Klein H., Boxem M., Ketting R.F.;
RT "PID-1 is a novel factor that operates during 21U-RNA biogenesis in
RT Caenorhabditis elegans.";
RL Genes Dev. 28:683-688(2014).
RN [3]
RP FUNCTION, IDENTIFICATION IN THE PETISCO COMPLEX, INTERACTION WITH ERH-2;
RP PID-3 AND TOFU-6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP 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 [4]
RP FUNCTION, IDENTIFICATION IN THE PETISCO COMPLEX, INTERACTION WITH ERH-2 AND
RP PID-3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-61.
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).
RN [5]
RP FUNCTION.
RX PubMed=33231880; DOI=10.15252/embj.2020105280;
RA Placentino M., de Jesus Domingues A.M., Schreier J., Dietz S., Hellmann S.,
RA de Albuquerque B.F., Butter F., Ketting R.F.;
RT "Intrinsically disordered protein PID-2 modulates Z granules and is
RT required for heritable piRNA-induced silencing in the Caenorhabditis
RT elegans embryo.";
RL EMBO J. 40:e105280-e105280(2021).
CC -!- FUNCTION: Component of the pid-1 variant of the PETISCO complex which
CC is 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 acts as an adapter which binds to the complex via erh-2
CC (PubMed:31147388). Involved in the biogenesis of 21U-RNAs which guide
CC the piwi protein prg-1 to its DNA targets for silencing
CC (PubMed:24696453, PubMed:33231880). Plays a role in small RNA-directed
CC transgenerational epigenetic inheritance (PubMed:33231880).
CC {ECO:0000269|PubMed:24696453, ECO:0000269|PubMed:31147388,
CC ECO:0000269|PubMed:33231880, 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-3; the interaction is direct
CC (PubMed:31216475, PubMed:31147388). Within the complex interacts with
CC erh-2 (PubMed:31216475, PubMed:31147388). Within the complex interacts
CC with tofu-6 (PubMed:31216475). {ECO:0000269|PubMed:31147388,
CC ECO:0000269|PubMed:31216475, ECO:0000305|PubMed:31216475}.
CC -!- INTERACTION:
CC Q19541; Q20057: erh-2; NbExp=4; IntAct=EBI-21447100, EBI-21447087;
CC Q19541; O76616: pid-3; NbExp=4; IntAct=EBI-21447100, EBI-2415582;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24696453,
CC ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}. Nucleus
CC {ECO:0000269|PubMed:24696453}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
CC Note=Expressed predominantly in the cytoplasm (PubMed:24696453). A
CC small fraction is nuclear or located near the nucleus
CC (PubMed:24696453). Dispersedly distributes throughout the cytoplasm in
CC early embryos (PubMed:31147388). Localizes to puncta in the perinuclear
CC region in the germline syncytium (PubMed:31216475, PubMed:31147388).
CC {ECO:0000269|PubMed:24696453, ECO:0000269|PubMed:31147388,
CC ECO:0000269|PubMed:31216475}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the germline (at protein
CC level). {ECO:0000269|PubMed:24696453, ECO:0000269|PubMed:31147388,
CC ECO:0000269|PubMed:31216475}.
CC -!- DEVELOPMENTAL STAGE: Expressed from early embryogenesis (at protein
CC level). {ECO:0000269|PubMed:31147388}.
CC -!- DISRUPTION PHENOTYPE: 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 does not cause chromosome segregation and cell
CC division defects in early embryos (PubMed:31216475).
CC {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
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DR EMBL; BX284602; CCD62046.1; -; Genomic_DNA.
DR PIR; T34224; T34224.
DR RefSeq; NP_495613.1; NM_063212.5.
DR AlphaFoldDB; Q19541; -.
DR ComplexPortal; CPX-4306; PETISCO, pid-1 variant.
DR IntAct; Q19541; 11.
DR STRING; 6239.F18A1.8; -.
DR EPD; Q19541; -.
DR PaxDb; Q19541; -.
DR PeptideAtlas; Q19541; -.
DR EnsemblMetazoa; F18A1.8.1; F18A1.8.1; WBGene00017549.
DR GeneID; 184627; -.
DR KEGG; cel:CELE_F18A1.8; -.
DR UCSC; F18A1.8; c. elegans.
DR CTD; 184627; -.
DR WormBase; F18A1.8; CE04408; WBGene00017549; pid-1.
DR eggNOG; ENOG502THJI; Eukaryota.
DR HOGENOM; CLU_1579909_0_0_1; -.
DR InParanoid; Q19541; -.
DR OMA; KCAERFN; -.
DR OrthoDB; 1480569at2759; -.
DR PRO; PR:Q19541; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00017549; 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:WormBase.
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:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..169
FT /note="Protein pid-1"
FT /id="PRO_0000432405"
FT REGION 137..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 61
FT /note="May be required for interaction with erh-2"
FT /evidence="ECO:0000305|PubMed:31147388"
FT MUTAGEN 61
FT /note="R->C: In xf14; abolishes the interaction with pid-3.
FT May abolish the interaction with erh-2. Reduces stability
FT and reduces levels of a class of 21 nucleotide PIWI-
FT interacting RNAs (piRNAs) that possess a uracil residue at
FT the 5'-end (also called 21U-RNAs)."
FT /evidence="ECO:0000269|PubMed:24696453,
FT ECO:0000269|PubMed:31147388"
SQ SEQUENCE 169 AA; 19007 MW; 5B1A28210AC95343 CRC64;
MSAKREFSHI TLASTPFKKR IDQNSLKTDS DIEKDTNIAH KCAERFNYNT NLHRKVTLSD
RFELAALGYE MKAKPRTIIE KHNDCDEFHF IYRKEKKNDY GTGSPLSAGL SLSNPLPAGR
GFLSPAIQNT SNQFTFSGSP RITPQKHTPV SANHKPARSI FDDIPSNIA
