EPG5_CAEEL
ID EPG5_CAEEL Reviewed; 1599 AA.
AC Q18892;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Ectopic P granules protein 5;
GN Name=epg-5 {ECO:0000312|WormBase:C56C10.12};
GN ORFNames=C56C10.12 {ECO:0000312|WormBase:C56C10.12};
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]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION 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, AND SUBCELLULAR LOCATION.
RX PubMed=22451698; DOI=10.1083/jcb.201111053;
RA Li W., Zou W., Yang Y., Chai Y., Chen B., Cheng S., Tian D., Wang X.,
RA Vale R.D., Ou G.;
RT "Autophagy genes function sequentially to promote apoptotic cell corpse
RT degradation in the engulfing cell.";
RL J. Cell Biol. 197:27-35(2012).
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 FUNCTION.
RX PubMed=25124690; DOI=10.15252/embr.201438618;
RA Wu Y., Cheng S., Zhao H., Zou W., Yoshina S., Mitani S., Zhang H., Wang X.;
RT "PI3P phosphatase activity is required for autophagosome maturation and
RT autolysosome formation.";
RL EMBO Rep. 15:973-981(2014).
CC -!- FUNCTION: Involved in the maturation of autophagosomes into
CC autolysosomes during starvation-induced autotrophy (PubMed:20550938,
CC PubMed:22451698, PubMed:24374177, PubMed:25124690). Specifically,
CC involved in the clearance of apoptotic cells by promoting the delivery
CC of engulfed apoptotic cells to the lysosome (PubMed:22451698).
CC {ECO:0000269|PubMed:20550938, ECO:0000269|PubMed:22451698,
CC ECO:0000269|PubMed:24374177, ECO:0000269|PubMed:25124690}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20550938}.
CC Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:22451698};
CC Peripheral membrane protein {ECO:0000305|PubMed:20550938}; Cytoplasmic
CC side {ECO:0000305|PubMed:20550938}. Note=Partially localizes to the
CC phagosome membrane of engulfed apoptotic cells.
CC {ECO:0000269|PubMed:22451698}.
CC -!- TISSUE SPECIFICITY: Expressed in pharyngeal and body wall muscles and
CC intestine cells. {ECO:0000269|PubMed:20550938}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed during embryogenesis.
CC {ECO:0000269|PubMed:20550938}.
CC -!- DISRUPTION PHENOTYPE: Increased number and reduced size of P granules
CC (pgl-3-positive and lgg-1-positive) and sqst-1-positive protein
CC aggregates in embryos (PubMed:20550938). RNAi-mediated knockdown
CC results in increased lgg-2-positive autophagosomes following
CC fertilization and at later embryonic stages (PubMed:24374177).
CC {ECO:0000269|PubMed:20550938, ECO:0000269|PubMed:24374177}.
CC -!- SIMILARITY: Belongs to the EPG5 family. {ECO:0000305}.
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DR EMBL; BX284602; CCD68183.1; -; Genomic_DNA.
DR PIR; T15854; T15854.
DR RefSeq; NP_495343.1; NM_062942.3.
DR AlphaFoldDB; Q18892; -.
DR BioGRID; 533112; 5.
DR STRING; 6239.C56C10.12; -.
DR iPTMnet; Q18892; -.
DR EPD; Q18892; -.
DR PaxDb; Q18892; -.
DR PeptideAtlas; Q18892; -.
DR EnsemblMetazoa; C56C10.12.1; C56C10.12.1; WBGene00016968.
DR UCSC; C56C10.12; c. elegans.
DR WormBase; C56C10.12; CE02566; WBGene00016968; epg-5.
DR eggNOG; KOG3622; Eukaryota.
DR GeneTree; ENSGT00390000007354; -.
DR HOGENOM; CLU_003383_0_0_1; -.
DR InParanoid; Q18892; -.
DR OMA; FECRLTE; -.
DR OrthoDB; 42984at2759; -.
DR PhylomeDB; Q18892; -.
DR PRO; PR:Q18892; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00016968; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097352; P:autophagosome maturation; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:WormBase.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:UniProtKB.
DR InterPro; IPR029651; EPG-5.
DR PANTHER; PTHR31139:SF4; PTHR31139:SF4; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Cytoplasm; Cytoplasmic vesicle; Membrane; Reference proteome.
FT CHAIN 1..1599
FT /note="Ectopic P granules protein 5"
FT /id="PRO_0000306261"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1599 AA; 179994 MW; BC4E8E7429339091 CRC64;
MAELVRPKKP KHRERAQSDY TPPIPDRPAI VNGLRLPAAP SHTIEDLPER SASPEPEDQD
ISLTEDSLKR EEASEPLKDV RSSPVRPAPP PPRVSQEREA PPIPPRSMIF PRSTSMVAES
RKESTTAVAP KRSVAVASYP AVPELAELPS YTDALQHPQV YPSINGGLQH SHSATAIPEK
TRFSAPVERE RVREGEAPPM YPSIKTYERN EHGLMTEENL VTFYHNPLYE HAEMFVDQFI
KTEEVPTQSG SLFPLLARLR TVCDLMTVSE VKGKENTEEL QKCLRECWVQ QSLSVDAKGK
CGDNNDGTGR ASYFSFELQQ AVLDQMKKLL STNRSNLMDH SVCEETSFRS IALQIQWQVI
IINNNFMAEN GLSTNCPPSL IASVPMTPGR VALRTALSDI FYHLRYPRLS KRFIDTLVGW
IKELTCVLNM RQSCDDGIFL LCHLLRLPSP IDQWASPFVQ TFIQSQSAPK LKLDYCVALL
THLLNPIKAR ESFLRHVAQS EKEESTWEIL ADDDDGEANE FSFVTINESD LTAFLDQFPI
SELYSIAYLA FTSYSDKGSQ FTAMIAFQLL LMKILDNGLT SYSQPGYKMF CKQIGISLKH
SVRELCSNWR LIRDQVRPGE EHHLQKEVDR VVLLALNYLI HQDTLGLFQF VVSLPYAVVS
EECRSRCEYA LRSNKKMSIH EIYDTPICEV RARISSQGIS KRIGALGAQD SEFLVNSLAS
IGSYSNSDVS QLLKELIDVC FCDEDTRDDL YKCGGEAIGQ ILIKRPETLH QLLTIIDRNL
QHMDSYAINV LSSSRLFECR LTEPMISIIG KWLINNPPEH GANRLARRVL SGLHWGLAVD
GHNLWIDVDV HTIAADTVVK AHSVHCSRSN SMISKSINKI SKLASKVGDA ESLFQQFCWD
LLVKLKLPTI PSSLVQNDLT AHYVRIVQNC EDDVVVYLEK GVPLLSDLVT SGSSVASVVL
LSRLIAQHYQ NVNLMAADKN FMTTFERLLH IDQLPYAVQW LSGPSSTPTP IVKLICSAIS
YYSAKLPPRD YLRAWITLLC AARTGWNEDA VTYQIVGTIA RIAFVNDTHK LYEITGIIFQ
AYQQQLAAEK NQSKGIMSMF SSDNTVSPLI PDSMLSISPF ASYVMLRVEQ KSFNTFYGHF
FETLTKKDKY TLDNAVKKAS SKCSITVPVE RLAIFRWAKL VTVCNDHQLL PILLQQLSGS
AYRLRKANNL NLCYARRLID DPQMQDVMAA CRKAIEESTI ETKGLSKAVV GWLFTKHEVT
RTGFDFSVFD LDYLLQLILA GDKNMWLDFV NMPYFNSEEF SERKLYSVTC QLSPKNRESP
LPPEIGSPRS RSSAKPFPVL PVHSGLPQAP LIDPSILFQQ HTVLQLASPF INTIKQLSKQ
FAQSGDRMSM DDDSYCKQIK ALYQPTQQTI PVEIRCSYCS KPKACTMSIK PNVLNSEIDL
QMTQNRTKRF EFWNELYASI VDKAAVATAS IEHLSVLVAK MTSALHPGTR NNVQLTGHSL
FYLITSSVGE NELLFSVASD SFCNSLRSLG EEYVKFRPEE QMDVMQLALD GFVLSEPLVE
VFTPEVLNSD DLCTAYRKLS DAVRMPERSK MALQLLGKQ
