PID2_CAEEL
ID PID2_CAEEL Reviewed; 454 AA.
AC Q9N3P1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein pid-2 {ECO:0000305};
DE AltName: Full=Z granule surface protein 1 {ECO:0000303|PubMed:33438773};
DE AltName: Full=piRNA-induced silencing defective protein 2 {ECO:0000312|WormBase:Y48G1C.1};
GN Name=pid-2 {ECO:0000303|PubMed:33231880, ECO:0000312|WormBase:Y48G1C.1};
GN Synonyms=zsp-1 {ECO:0000303|PubMed:33438773};
GN ORFNames=Y48G1C.1 {ECO:0000312|WormBase:Y48G1C.1};
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, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF 122-TRP--PHE-454; GLY-210 AND GLY-387.
RX PubMed=33438773; DOI=10.15252/embj.2020105612;
RA Wan G., Bajaj L., Fields B., Dodson A.E., Pagano D., Fei Y., Kennedy S.;
RT "ZSP-1 is a Z granule surface protein required for Z granule fluidity and
RT germline immortality in Caenorhabditis elegans.";
RL EMBO J. 40:e105612-e105612(2021).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PID-4; PID-5; APP-1 AND PRMT-5, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 122-TRP--PHE-454.
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: Involved in gene silencing mediated by 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 that guide the Piwi protein
CC prg-1 to its DNA targets for silencing (PubMed:33438773,
CC PubMed:33231880). Not required for the biogenesis of 21U-RNAs
CC (PubMed:33231880). May also be involved in gene silencing mediated by
CC 22G-siRNAs (a class of 22 nucleotide endogenous small interfering RNAs
CC (siRNAs) that possess a triphosphorylated guanine residue at the 5'-
CC end) and 26G-siRNAs (a class of 26 nucleotide siRNAs that possess a
CC guanine residue at the 5'-end) (PubMed:33231880). Required for the
CC biogenesis of secondary and tertiary 22G-siRNAs from many loci
CC (PubMed:33231880). Specifically, promotes the production of 22G-siRNAs
CC from the 5' end of target mRNAs (PubMed:33231880). May play a role in
CC the production of 26G-siRNAs (PubMed:33231880). Plays a role in small
CC RNA-directed transgenerational epigenetic inheritance (also called
CC RNAe) over several generations and germline immortality
CC (PubMed:33438773, PubMed:33231880). Together with the argonaut protein
CC hrde-1, promotes the silencing of the DNA transposable element Tc1
CC (PubMed:33231880). Required for the formation of liquid-like
CC condensates in the cytoplasm called Z granules, playing a role in
CC maintaining their assembly, viscosity and morphology in adult germ
CC cells, and localization in early embryos (PubMed:33438773,
CC PubMed:33231880). {ECO:0000269|PubMed:33231880,
CC ECO:0000269|PubMed:33438773}.
CC -!- SUBUNIT: May interact with pid-4, pid-5, app-1 and prmt-5.
CC {ECO:0000269|PubMed:33231880}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:33231880, ECO:0000269|PubMed:33438773}. Cytoplasmic
CC granule {ECO:0000269|PubMed:33438773}. Note=Localizes to perinuclear
CC granules, adjacent to P granules in adult germ cells (PubMed:33438773,
CC PubMed:33231880). These perinuclear granules segregate with germline
CC blastomeres during embryonic development (PubMed:33438773). Localizes
CC to the outer periphery of Z granules, which are liquid-like condensates
CC in the cytoplasm (PubMed:33438773). {ECO:0000269|PubMed:33231880,
CC ECO:0000269|PubMed:33438773}.
CC -!- TISSUE SPECIFICITY: Expressed throughout the mitotic and meiotic
CC regions of the germline and in oocytes. {ECO:0000269|PubMed:33438773}.
CC -!- DEVELOPMENTAL STAGE: Expressed in two cell, 4 cell and 300 cell embryos
CC and in the primordial germ cells, Z2 and Z3 (PubMed:33438773).
CC Expressed in the pachytene stage of the meiotic region of L4 larvae
CC (PubMed:33231880). Expressed in germ cells of L4 larvae
CC (PubMed:33231880). {ECO:0000269|PubMed:33231880,
CC ECO:0000269|PubMed:33438773}.
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DR EMBL; BX284601; CCD71722.1; -; Genomic_DNA.
DR RefSeq; NP_490672.2; NM_058271.7.
DR AlphaFoldDB; Q9N3P1; -.
DR DIP; DIP-24833N; -.
DR IntAct; Q9N3P1; 3.
DR STRING; 6239.Y48G1C.1; -.
DR EPD; Q9N3P1; -.
DR PaxDb; Q9N3P1; -.
DR PeptideAtlas; Q9N3P1; -.
DR EnsemblMetazoa; Y48G1C.1.1; Y48G1C.1.1; WBGene00021676.
DR GeneID; 171599; -.
DR KEGG; cel:CELE_Y48G1C.1; -.
DR UCSC; Y48G1C.1; c. elegans.
DR CTD; 171599; -.
DR WormBase; Y48G1C.1; CE30019; WBGene00021676; pid-2.
DR eggNOG; ENOG502RT5Y; Eukaryota.
DR HOGENOM; CLU_571401_0_0_1; -.
DR InParanoid; Q9N3P1; -.
DR OMA; CPKTWPP; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00021676; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; RNA-mediated gene silencing.
FT CHAIN 1..454
FT /note="Protein pid-2"
FT /id="PRO_0000452724"
FT REGION 31..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 122..454
FT /note="Missing: In xf23 and gg661; displays a gradual
FT decline of fertility over successive generations, also
FT called a mortal germline phenotype (Mrt). Defective
FT formation of liquid-like condensates in the cytoplasm
FT called Z granules, whereby Z granules are larger in size
FT and there are fewer compared to wild-type. There are fewer
FT pid-4-expressing germ cell foci. Does not affect the number
FT of pid-5-expressing germ cell foci. Defective gene
FT silencing mediated by a class of 21 nucleotide PIWI-
FT interacting RNAs (piRNAs) that possess a uracil residue at
FT the 5'-end (also called 21U-RNAs). Does not reduce the
FT levels of 21U-RNAs. Reduces the levels of secondary and
FT tertiary 22G-siRNAs, which are a class of 22 nucleotide
FT small interfering RNAs (siRNAs) that possess a
FT triphosphorylated guanine residue at the 5'-end. Reduces
FT the levels of 26G-siRNAs, which are a class of 26
FT nucleotide siRNAs that possess a guanine residue at the 5'-
FT end. Does not reduce the levels of microRNAs (miRNAs).
FT Disrupts inheritance of small RNA-induced gene silencing.
FT Impairs silencing of the DNA transposable element Tc1.
FT Enhances the impaired silencing of the DNA transposable
FT element Tc1 in a hrde-1 tm1200 mutant background. Results
FT in sterility, a high incidence of females phenotype and
FT defective activity of the PIWI-interacting RNA (piRNA)
FT silencing pathway in a pid-1 xf35 mutant background."
FT /evidence="ECO:0000269|PubMed:33231880,
FT ECO:0000269|PubMed:33438773"
FT MUTAGEN 210
FT /note="G->E: In gg662; disrupts inheritance of small RNA-
FT induced gene silencing."
FT /evidence="ECO:0000269|PubMed:33438773"
FT MUTAGEN 387
FT /note="G->E: In gg663; disrupts inheritance of small RNA-
FT induced gene silencing."
FT /evidence="ECO:0000269|PubMed:33438773"
SQ SEQUENCE 454 AA; 52134 MW; 07836CE5B361E6E5 CRC64;
MTVIIASHWG PQSKQMLPPE PPRIILREVP VQNNQKEHPP VQEIKTVSSK SKEHRVSSSR
KIPDHFDVGP RFYMNVPADG SEVFEDDEKD VENECWAVIE RIGSEDDKFE ASELVEYRDH
DWYIALAINK EKTPDKANYQ HLLYSYRGGI QRIILTPQQT DSIDKTPLVK YKIIGDGLYE
VLPIHSSLPQ TGLISPKYRY NKGVELRIFG IVNWIDFVLD DDHQTHRTMV WTDAVGPIYL
SAADRANIRR KLLLTEMQIF APLRMCHITV KAEFNFSIPD GSPIQWTISS FQPLIEESEK
DPNIGRNLWP ARVLRFDDLV VTKKTPNGYW LKSQRLEGHV NVFAGANQIG IIESAGEKYA
TKGSMMAFVV PCYQNSTFAY FEALIAGPPR VVMIITEGRF LNYCPKTWPP SVRKMRDQYQ
KEHVLKSEVR SSPICMKQPD YCLKSLRGFS ECPF
