EPG2_CAEEL
ID EPG2_CAEEL Reviewed; 690 AA.
AC Q95XR4;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ectopic P granules protein 2;
GN Name=epg-2 {ECO:0000312|WormBase:Y39G10AR.10};
GN ORFNames=Y39G10AR.10 {ECO:0000312|WormBase:Y39G10AR.10};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20550938; DOI=10.1016/j.cell.2010.04.034;
RA Tian Y., Li Z., Hu W., Ren H., Tian E., Zhao Y., Lu Q., Huang X., Yang P.,
RA Li X., Wang X., Kovacs A.L., Yu L., Zhang H.;
RT "C. elegans screen identifies autophagy genes specific to multicellular
RT organisms.";
RL Cell 141:1042-1055(2010).
RN [3]
RP FUNCTION, INTERACTION WITH SEPA-1, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=24140420; DOI=10.1016/j.molcel.2013.09.014;
RA Li S., Yang P., Tian E., Zhang H.;
RT "Arginine methylation modulates autophagic degradation of PGL granules in
RT C. elegans.";
RL Mol. Cell 52:421-433(2013).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24374177; DOI=10.1016/j.devcel.2013.11.022;
RA Manil-Segalen M., Lefebvre C., Jenzer C., Trichet M., Boulogne C.,
RA Satiat-Jeunemaitre B., Legouis R.;
RT "The C. elegans LC3 acts downstream of GABARAP to degrade autophagosomes by
RT interacting with the HOPS subunit VPS39.";
RL Dev. Cell 28:43-55(2014).
RN [5]
RP INTERACTION WITH LGG-1 AND LGG-2, DOMAIN LIR MOTIF, AND MUTAGENESIS OF
RP 59-LYS--LEU-64; 381-ASP--LEU-385; 683-GLU--VAL-687; 684-TRP--MET-686;
RP TRP-684; GLU-685 AND VAL-687.
RX PubMed=26687600; DOI=10.1016/j.molcel.2015.11.019;
RA Wu F., Watanabe Y., Guo X.Y., Qi X., Wang P., Zhao H.Y., Wang Z.,
RA Fujioka Y., Zhang H., Ren J.Q., Fang T.C., Shen Y.X., Feng W., Hu J.J.,
RA Noda N.N., Zhang H.;
RT "Structural Basis of the Differential Function of the Two C. elegans Atg8
RT Homologs, LGG-1 and LGG-2, in Autophagy.";
RL Mol. Cell 60:914-929(2015).
RN [6]
RP FUNCTION, INTERACTION WITH SEPA-1, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=28806108; DOI=10.1080/15548627.2017.1339843;
RA Zhang G., Lin L., Qi D., Zhang H.;
RT "The composition of a protein aggregate modulates the specificity and
RT efficiency of its autophagic degradation.";
RL Autophagy 13:1487-1495(2017).
CC -!- FUNCTION: Involved in autophagy (PubMed:20550938, PubMed:24140420,
CC PubMed:24374177). Thought to act as an adapter protein that brings PGL
CC granules to autophagic structures containing lgg-1 (PubMed:20550938).
CC Association with other adapters such as sepa-1 is required for the
CC accumulation and degradation of germ cell specific P-granules by
CC autophagy in somatic cells (PubMed:24140420, PubMed:28806108). This
CC ensures exclusive localization of the P-granules in germ cells
CC (PubMed:24140420, PubMed:28806108). May also play a role in the removal
CC of sepa-1 from somatic cells (PubMed:28806108).
CC {ECO:0000269|PubMed:20550938, ECO:0000269|PubMed:24140420,
CC ECO:0000269|PubMed:24374177, ECO:0000269|PubMed:28806108}.
CC -!- SUBUNIT: Interacts with sepa-1 (PubMed:24140420, PubMed:28806108).
CC Interacts (via the LIR motifs) with lgg-1 and lgg-2 (PubMed:26687600).
CC Shows strong interaction with lgg-1 and weak interaction with lgg-2
CC (PubMed:26687600). {ECO:0000269|PubMed:24140420,
CC ECO:0000269|PubMed:26687600, ECO:0000269|PubMed:28806108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20550938,
CC ECO:0000269|PubMed:24140420, ECO:0000269|PubMed:28806108}. Note=Co-
CC localizes with sepa-1 in cytoplasmic aggregates.
CC {ECO:0000269|PubMed:24140420}.
CC -!- DEVELOPMENTAL STAGE: Aggregates of epg-2 peak in abundance at the 100
CC cell stage then decrease until they are very few at the comma stage
CC (PubMed:20550938, PubMed:28806108). Absent from the 200 stage onwards
CC (PubMed:24140420, PubMed:28806108). {ECO:0000269|PubMed:20550938,
CC ECO:0000269|PubMed:24140420, ECO:0000269|PubMed:28806108}.
CC -!- DOMAIN: The LIR motifs (LC3-interacting region) are required for its
CC interaction with lgg-1 and lgg-2. {ECO:0000269|PubMed:26687600}.
CC -!- DISRUPTION PHENOTYPE: No colocalization of P-granule components with
CC lgg-1 (PubMed:20550938). Furthermore, there is an accumulation of pgl-3
CC positive P-granules in somatic cells of embryos (PubMed:28806108).
CC RNAi-mediated knockdown results in increased lgg-2-positive
CC autophagosomes following fertilization and at later embryonic stages
CC (PubMed:24374177). {ECO:0000269|PubMed:20550938,
CC ECO:0000269|PubMed:24374177, ECO:0000269|PubMed:28806108}.
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DR EMBL; FO081209; CCD69908.1; -; Genomic_DNA.
DR RefSeq; NP_490955.1; NM_058554.4.
DR AlphaFoldDB; Q95XR4; -.
DR SMR; Q95XR4; -.
DR BioGRID; 37273; 8.
DR DIP; DIP-27321N; -.
DR IntAct; Q95XR4; 4.
DR STRING; 6239.Y39G10AR.10; -.
DR EPD; Q95XR4; -.
DR PaxDb; Q95XR4; -.
DR PeptideAtlas; Q95XR4; -.
DR PRIDE; Q95XR4; -.
DR EnsemblMetazoa; Y39G10AR.10.1; Y39G10AR.10.1; WBGene00021468.
DR GeneID; 171787; -.
DR KEGG; cel:CELE_Y39G10AR.10; -.
DR UCSC; Y39G10AR.10; c. elegans.
DR CTD; 171787; -.
DR WormBase; Y39G10AR.10; CE26989; WBGene00021468; epg-2.
DR eggNOG; ENOG502THXW; Eukaryota.
DR HOGENOM; CLU_430982_0_0_1; -.
DR InParanoid; Q95XR4; -.
DR OMA; AINQEMI; -.
DR OrthoDB; 1749076at2759; -.
DR PhylomeDB; Q95XR4; -.
DR PRO; PR:Q95XR4; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00021468; Expressed in embryo and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0016236; P:macroautophagy; IMP:WormBase.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Autophagy; Coiled coil; Cytoplasm; Reference proteome.
FT CHAIN 1..690
FT /note="Ectopic P granules protein 2"
FT /id="PRO_0000404707"
FT REGION 381..385
FT /note="Required for interaction with lgg-1"
FT /evidence="ECO:0000269|PubMed:26687600"
FT REGION 666..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 20..181
FT /evidence="ECO:0000255"
FT COILED 359..409
FT /evidence="ECO:0000255"
FT COILED 458..494
FT /evidence="ECO:0000255"
FT COILED 560..643
FT /evidence="ECO:0000255"
FT MOTIF 61..64
FT /note="LIR 1"
FT /evidence="ECO:0000269|PubMed:26687600"
FT MOTIF 684..687
FT /note="LIR 2"
FT /evidence="ECO:0000269|PubMed:26687600"
FT COMPBIAS 666..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 59..64
FT /note="KTYSTL->ATASTA: Impairs the interaction with lgg-1."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 381..385
FT /note="DFKIL->KAKIA: Abolishes the interaction with lgg-1."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 683..687
FT /note="EWEMV->KAKMA: Impairs the interaction with lgg-1."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 684..686
FT /note="WEM->FVE: Impairs the interaction with lgg-1.
FT Abolishes the interaction with lgg-2."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 684
FT /note="W->A: Abolishes the interaction with lgg-1."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 684
FT /note="W->F: Abolishes the interaction with lgg-2, but not
FT with lgg-1."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 685
FT /note="E->K: Abolishes the interaction with lgg-1."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 687
FT /note="V->A: Abolishes the interaction with lgg-1."
FT /evidence="ECO:0000269|PubMed:26687600"
SQ SEQUENCE 690 AA; 79973 MW; 40730553023C5BAE CRC64;
MSANRTVTVF SSSAEDQEPI ELAEDSLQNL DKMLAEEKEE HQLLKDEVVL LRKENVEAKT
YSTLLEIMLD EAEEKASSAQ ETTSEENNLK ILNRDLVAEN LELKEMKEEL RKIWLSDSKK
FQEALTRISD ENTKLQKDCH ELESIRQCAQ FALDNCNEEL EKTQTENEEH ESRIETLERE
VCEKDIAMKD IVERKDEISL QLELQTKEFT SALNDLMYGR EDTLKQIHQM KENWKVKQNE
FEVEITKLKS QNDYFDSERL QLTDRIRALL NELSDVRLEL GSTRLAMKEK AEVTEAVTSF
NKDLRDKLED EIARLGECLQ FRKDEHEQDE AVIAHLEEQL KLGSDKAAAF SSEHSDTIEL
LRESETELME LRMENYDLKE DFKILKEEKE DVNRTCECLR EQLSTTIQER DIEKGQMQSE
MDAKMVAVHQ QYAKQIDNMK YNHMLAINQE LIKGQMALES GKKKHANEIL TVRNELEQSN
AAHQSLRDQC SLLLSSEDDL RTAHLALESK MTLVSEECIA LRVSRANAQK EIGNLTEHHK
LEVALLEDAK SGIQQRLHYA TIEIEQLKKI NEVTQAQFKK ETDEKNAEIN EFQAAMVSMK
QQYNVLGNHC RVLTSQGISD RTTIDKLQET IREHTELAIE TKRIHDAEIV QLNDAHKKLV
DNLGVEELDE EPKASTESEE KAEWEMVDEE
