VMP1_CAEEL
ID VMP1_CAEEL Reviewed; 458 AA.
AC Q9XWU8;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Ectopic P granules protein 3;
GN Name=epg-3 {ECO:0000312|EMBL:CAA21543.2, ECO:0000312|WormBase:Y37D8A.22};
GN ORFNames=Y37D8A.22;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CAA21543.2}
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, 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 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).
CC -!- FUNCTION: Involved in autophagy (PubMed:20550938, PubMed:24374177).
CC Thought to act in autophagasome and omegasome formation
CC (PubMed:20550938). {ECO:0000269|PubMed:20550938,
CC ECO:0000269|PubMed:24374177}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:20550938}.
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: Defective P granule organization and degradation
CC (PubMed:20550938). Early autophagic structures and lgg-1 puncta form an
CC irregular shape and clump together (PubMed:20550938). RNAi-mediated
CC knockdown 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 VMP1 family. {ECO:0000305}.
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DR EMBL; AL032626; CAA21543.2; -; Genomic_DNA.
DR PIR; T26642; T26642.
DR RefSeq; NP_499688.2; NM_067287.5.
DR AlphaFoldDB; Q9XWU8; -.
DR STRING; 6239.Y37D8A.22; -.
DR TCDB; 8.A.97.1.2; the epg-3/vmp1 (epg/vpm) family.
DR EPD; Q9XWU8; -.
DR PaxDb; Q9XWU8; -.
DR PeptideAtlas; Q9XWU8; -.
DR EnsemblMetazoa; Y37D8A.22a.1; Y37D8A.22a.1; WBGene00012559.
DR GeneID; 176712; -.
DR KEGG; cel:CELE_Y37D8A.22; -.
DR UCSC; Y37D8A.22; c. elegans.
DR CTD; 176712; -.
DR WormBase; Y37D8A.22; CE31831; WBGene00012559; epg-3.
DR eggNOG; KOG1109; Eukaryota.
DR GeneTree; ENSGT00390000007230; -.
DR HOGENOM; CLU_033298_0_1_1; -.
DR InParanoid; Q9XWU8; -.
DR OMA; HIAFFTM; -.
DR OrthoDB; 822110at2759; -.
DR PhylomeDB; Q9XWU8; -.
DR PRO; PR:Q9XWU8; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00012559; Expressed in embryo and 3 other tissues.
DR ExpressionAtlas; Q9XWU8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:WormBase.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:UniProtKB.
PE 2: Evidence at transcript level;
KW Autophagy; Cytoplasm; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..458
FT /note="Ectopic P granules protein 3"
FT /id="PRO_0000404706"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 51868 MW; 1F1EF7D9EDEE0C69 CRC64;
MAKKQKKSTE KSERTVEFKE PPKPANSEER LKPAGRGMKP SPSQNTLNRM ERETIVFWRR
PHIVIPYALM EIAHLAVELF FKILAHKTVL LLTAISIGLA VYGYHAPGAH QEHVQTIEKH
ILWWSWWVLL GVLSSIGLGS GLHTFLIYLG PHIAAVTMAA YECQSLDFPQ PPYPESIQCP
STKSSIAVTF WQIVAKVRVE SLLWGAGTAL GELPPYFMAR AARISGQEPD DEEYREFLEL
MNADKESDAD QKLSIVERAK SWVEHNIHRL GFPGILLFAS IPNPLFDLAG ITCGHFLVPF
WSFFGATLIG KALVKMHVQM GFVILAFSDH HAENFVKILE KIPAVGPYIR QPISDLLEKQ
RKALHKTPGE HSEQSTSYLA WGLSLMVTFM ILFFFLSIVN SLAKDYHKRL WERKRRQNKD
LIDEENQSFE EEEEEAVTPP SSCPLLLSDG FEGVVVKK
