DEPS1_CAEEL
ID DEPS1_CAEEL Reviewed; 619 AA.
AC Q9N303; V6CLC9;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=P-granule-associated protein deps-1 {ECO:0000305};
DE AltName: Full=Defective P granules and sterile protein deps-1 {ECO:0000312|WormBase:Y65B4BL.2a};
GN Name=deps-1 {ECO:0000303|PubMed:18234720, ECO:0000312|WormBase:Y65B4BL.2a};
GN ORFNames=Y65B4BL.2 {ECO:0000312|WormBase:Y65B4BL.2a};
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 DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 116-ARG--VAL-619 AND
RP 408-GLN--VAL-619.
RX PubMed=18234720; DOI=10.1242/dev.015552;
RA Spike C.A., Bader J., Reinke V., Strome S.;
RT "DEPS-1 promotes P-granule assembly and RNA interference in C. elegans germ
RT cells.";
RL Development 135:983-993(2008).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=27015309; DOI=10.1016/j.cell.2016.02.057;
RA Houri-Ze'evi L., Korem Y., Sheftel H., Faigenbloom L., Toker I.A.,
RA Dagan Y., Awad L., Degani L., Alon U., Rechavi O.;
RT "A Tunable Mechanism Determines the Duration of the Transgenerational Small
RT RNA Inheritance in C. elegans.";
RL Cell 165:88-99(2016).
RN [4] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF 116-ARG--VAL-619.
RX PubMed=29769721; DOI=10.1038/s41586-018-0132-0;
RA Wan G., Fields B.D., Spracklin G., Shukla A., Phillips C.M., Kennedy S.;
RT "Spatiotemporal regulation of liquid-like condensates in epigenetic
RT inheritance.";
RL Nature 557:679-683(2018).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH EDG-1 AND PRG-1, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 102-HIS--VAL-619 AND 116-ARG--VAL-619.
RX PubMed=32843637; DOI=10.1038/s41467-020-18089-1;
RA Suen K.M., Braukmann F., Butler R., Bensaddek D., Akay A., Lin C.C.,
RA Milonaityte D., Doshi N., Sapetschnig A., Lamond A., Ladbury J.E.,
RA Miska E.A.;
RT "DEPS-1 is required for piRNA-dependent silencing and PIWI condensate
RT organisation in Caenorhabditis elegans.";
RL Nat. Commun. 11:4242-4242(2020).
CC -!- FUNCTION: Component of P-granules which is required for P-granule
CC formation and integrity in adult germ cells (PubMed:18234720). Promotes
CC the accumulation of glh-1 mRNA and localization of pgl-1 to P-granules
CC (PubMed:18234720). Involved in RNA-mediated gene silencing (RNAi) in
CC the germline (PubMed:18234720, PubMed:32843637). In particular, it is
CC required for piwi-interacting RNA (piRNA) gene silencing and positively
CC regulates the formation of secondary 22G-RNAs, which are RNA-dependent
CC RNA polymerase-derived endo-siRNAs, typically 22 nucleotides in length
CC with a 5'guanosine residue (PubMed:32843637). Its role in RNAi may also
CC be through positively regulating the expression of the dsRNA-binding
CC protein rde-4 (PubMed:18234720). Plays a role in small RNA-directed
CC transgenerational epigenetic inheritance (PubMed:27015309,
CC PubMed:29769721). {ECO:0000269|PubMed:18234720,
CC ECO:0000269|PubMed:27015309, ECO:0000269|PubMed:29769721,
CC ECO:0000269|PubMed:32843637}.
CC -!- SUBUNIT: Interacts (via N-terminus) with prg-1; the interaction is
CC direct (PubMed:32843637). May interact with edg-1 (PubMed:32843637).
CC {ECO:0000269|PubMed:32843637}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:18234720,
CC ECO:0000269|PubMed:32843637}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:32843637}. Note=Localizes to P-granules in germ
CC cells at all stages of development (PubMed:18234720). Co-localizes with
CC prg-1 at peri-nuclear P-granules in the proliferative zone and
CC transition zone, at pachytene, in oocytes and in embryos
CC (PubMed:32843637). In the distal loop, a higher proportion of deps-1
CC than prg-1 dissociates from the perinuclear region (PubMed:32843637).
CC In the adult germline, co-localizes with znfx-1 at P-granules and with
CC pgl-1 at P-granules in the pachytene region (PubMed:32843637).
CC {ECO:0000269|PubMed:18234720, ECO:0000269|PubMed:32843637}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y65B4BL.2a};
CC IsoId=Q9N303-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y65B4BL.2b};
CC IsoId=Q9N303-2; Sequence=VSP_060860;
CC -!- TISSUE SPECIFICITY: Expressed in germ cells.
CC {ECO:0000269|PubMed:18234720}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of development from
CC embryogenesis to adulthood (PubMed:18234720). Expressed at all
CC embryonic stages (PubMed:18234720). {ECO:0000269|PubMed:18234720}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in sterility and
CC disrupts the localization of pgl-1 to P-granules at 24.5 degrees
CC Celsius. {ECO:0000269|PubMed:18234720}.
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DR EMBL; BX284601; CCD73489.1; -; Genomic_DNA.
DR EMBL; BX284601; CDK13412.1; -; Genomic_DNA.
DR RefSeq; NP_001293193.1; NM_001306264.1. [Q9N303-2]
DR RefSeq; NP_490742.1; NM_058341.4. [Q9N303-1]
DR AlphaFoldDB; Q9N303; -.
DR STRING; 6239.Y65B4BL.2; -.
DR EPD; Q9N303; -.
DR PaxDb; Q9N303; -.
DR PeptideAtlas; Q9N303; -.
DR EnsemblMetazoa; Y65B4BL.2a.1; Y65B4BL.2a.1; WBGene00022034. [Q9N303-1]
DR EnsemblMetazoa; Y65B4BL.2b.1; Y65B4BL.2b.1; WBGene00022034. [Q9N303-2]
DR GeneID; 171642; -.
DR KEGG; cel:CELE_Y65B4BL.2; -.
DR UCSC; Y65B4BL.2; c. elegans. [Q9N303-1]
DR CTD; 171642; -.
DR WormBase; Y65B4BL.2a; CE25536; WBGene00022034; deps-1. [Q9N303-1]
DR WormBase; Y65B4BL.2b; CE49430; WBGene00022034; deps-1. [Q9N303-2]
DR eggNOG; ENOG502S2C2; Eukaryota.
DR HOGENOM; CLU_410628_0_0_1; -.
DR InParanoid; Q9N303; -.
DR OMA; PKLEKWM; -.
DR OrthoDB; 999263at2759; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022034; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q9N303; baseline and differential.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
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 Alternative splicing; Cytoplasm; Reference proteome;
KW RNA-mediated gene silencing.
FT CHAIN 1..619
FT /note="P-granule-associated protein deps-1"
FT /id="PRO_0000451760"
FT REGION 62..101
FT /note="Required for prg-1 binding"
FT /evidence="ECO:0000269|PubMed:32843637"
FT REGION 563..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..45
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060860"
FT MUTAGEN 102..619
FT /note="Missing: In mj605; reduces P-granule localization
FT and is diffusely localized in the cytoplasm. Abolishes prg-
FT 1 binding. Does not affect the mRNA or protein levels of
FT prg-1. Defective RNA-mediated gene silencing (RNAi),
FT specifically abolishing piwi-interacting RNA (piRNA) gene
FT silencing."
FT /evidence="ECO:0000269|PubMed:32843637"
FT MUTAGEN 116..619
FT /note="Missing: In bn124; disrupts pgl-1 localization to P-
FT granules. Abolishes piwi-interacting RNA (piRNA) gene
FT silencing. Smaller Z granules, which are liquid-like
FT condensates in the cytoplasm. Abolishes the binding of the
FT epigenetic inheritance factor znfx-1 to RNA."
FT /evidence="ECO:0000269|PubMed:18234720,
FT ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:32843637"
FT MUTAGEN 408..619
FT /note="Missing: In bn128; disrupts pgl-1 localization to P-
FT granules."
FT /evidence="ECO:0000269|PubMed:18234720"
SQ SEQUENCE 619 AA; 69258 MW; 7AEE40954C8D9770 CRC64;
MSERQSKYFD YQGIVISSTG QDNQDSETDL VYLIQAHGKA APKNIMYGVS KCAFVPTNLE
RNFDNIEEAK NLERRSKIPL KFGEVILWNE SDCDHDKRII LHIKREKPIY EASSSRNGLI
LKVGGVIQPT STTSFWTPLC TVTMPETEAT RAEPDVWLYA WIRFETTMKS GLDPFNMTAT
FESFDSCDPS DQARVCEAPW NAGSPDSKFG VWRPDPKPAD SDDEIDIEPR EGWHLPEDKW
AEVIKMQLGL YVGERLLICK ELSQFDFIIP LQKPFSRGTD KTLIYPAVGE YFHFSAIWSM
QHNGFLIYEL QPVPLLRQHV TSVNGNLLTR VVPASIRGLF VDKEGTLGLI DDPHHLLSFF
EFHPAGYEFL KAMAEVRAVR TSENKSVRYR IVRTSGMSIF ENWLRDTQFV VGPVKGIRIN
EDTVICAKHP NVYFKIPNNL KEGIPIGGGV QFVGKRQAGV DSEIMITECS PCPAFTCKNY
SVSGDTRLFQ VYLKPNCDHE QLAESDSMGF VDFRELETPC RGKFLAWVRE SITVNDCRRA
ATIMEVCSTA ICPPLIAMSA NSSRATSART TPAGSSIGSR SSIQSRASAA TSVSSNRFVG
PSSRRTPSGT PQSSTSSRV
