LGG1_CAEEL
ID LGG1_CAEEL Reviewed; 123 AA.
AC Q09490;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein lgg-1;
DE Flags: Precursor;
GN Name=lgg-1 {ECO:0000312|WormBase:C32D5.9};
GN Synonyms=atg-8.1 {ECO:0000312|WormBase:C32D5.9};
GN ORFNames=C32D5.9 {ECO:0000312|WormBase:C32D5.9};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Bristol N2;
RA Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA Thierry-Mieg D., Thierry-Mieg J.;
RT "The Caenorhabditis elegans transcriptome project, a complementary view of
RT the genome.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12958363; DOI=10.1126/science.1087782;
RA Melendez A., Talloczy Z., Seaman M., Eskelinen E.L., Hall D.H., Levine B.;
RT "Autophagy genes are essential for dauer development and life-span
RT extension in C. elegans.";
RL Science 301:1387-1391(2003).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17327275; DOI=10.1242/jcs.03401;
RA Toth M.L., Simon P., Kovacs A.L., Vellai T.;
RT "Influence of autophagy genes on ion-channel-dependent neuronal
RT degeneration in Caenorhabditis elegans.";
RL J. Cell Sci. 120:1134-1141(2007).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=19377305; DOI=10.4161/auto.5.5.8624;
RA Tian E., Wang F., Han J., Zhang H.;
RT "epg-1 functions in autophagy-regulated processes and may encode a highly
RT divergent Atg13 homolog in C. elegans.";
RL Autophagy 5:608-615(2009).
RN [6]
RP FUNCTION, INTERACTION WITH SEPA-1, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=19167332; DOI=10.1016/j.cell.2008.12.022;
RA Zhang Y., Yan L., Zhou Z., Yang P., Tian E., Zhang K., Zhao Y., Li Z.,
RA Song B., Han J., Miao L., Zhang H.;
RT "SEPA-1 mediates the specific recognition and degradation of P granule
RT components by autophagy in C. elegans.";
RL Cell 136:308-321(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19667176; DOI=10.1073/pnas.0813319106;
RA Jia K., Thomas C., Akbar M., Sun Q., Adams-Huet B., Gilpin C., Levine B.;
RT "Autophagy genes protect against Salmonella typhimurium infection and
RT mediate insulin signaling-regulated pathogen resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14564-14569(2009).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20523114; DOI=10.4161/auto.6.5.12252;
RA Alberti A., Michelet X., Djeddi A., Legouis R.;
RT "The autophagosomal protein LGG-2 acts synergistically with LGG-1 in dauer
RT formation and longevity in C. elegans.";
RL Autophagy 6:622-633(2010).
RN [9]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND LIPIDATION AT GLY-116.
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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND LIPIDATION AT GLY-116.
RX PubMed=21802374; DOI=10.1016/j.devcel.2011.06.024;
RA Lu Q., Yang P., Huang X., Hu W., Guo B., Wu F., Lin L., Kovacs A.L., Yu L.,
RA Zhang H.;
RT "The WD40 repeat PtdIns(3)P-binding protein EPG-6 regulates progression of
RT omegasomes to autophagosomes.";
RL Dev. Cell 21:343-357(2011).
RN [11]
RP DEVELOPMENTAL STAGE, LIPIDATION, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF
RP GLY-116.
RX PubMed=22767594; DOI=10.1074/jbc.m112.365676;
RA Wu F., Li Y., Wang F., Noda N.N., Zhang H.;
RT "Differential function of the two Atg4 homologues in the aggrephagy pathway
RT in Caenorhabditis elegans.";
RL J. Biol. Chem. 287:29457-29467(2012).
RN [12]
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 [13]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND LIPIDATION.
RX PubMed=24185444; DOI=10.4161/auto.26095;
RA Zhang H., Wu F., Wang X., Du H., Wang X., Zhang H.;
RT "The two C. elegans ATG-16 homologs have partially redundant functions in
RT the basal autophagy pathway.";
RL Autophagy 9:1965-1974(2013).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP GLY-116.
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 [15]
RP LIPIDATION.
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).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25896323; DOI=10.1038/nature14300;
RA Palikaras K., Lionaki E., Tavernarakis N.;
RT "Coordination of mitophagy and mitochondrial biogenesis during ageing in C.
RT elegans.";
RL Nature 521:525-528(2015).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27875098; DOI=10.1080/15548627.2016.1256933;
RA Chen H.D., Kao C.Y., Liu B.Y., Huang S.W., Kuo C.J., Ruan J.W., Lin Y.H.,
RA Huang C.R., Chen Y.H., Wang H.D., Aroian R.V., Chen C.S.;
RT "HLH-30/TFEB-mediated autophagy functions in a cell-autonomous manner for
RT epithelium intrinsic cellular defense against bacterial pore-forming toxin
RT in C. elegans.";
RL Autophagy 13:371-385(2017).
RN [18]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
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).
RN [19]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28198373; DOI=10.1038/ncomms14337;
RA Kumsta C., Chang J.T., Schmalz J., Hansen M.;
RT "Hormetic heat stress and HSF-1 induce autophagy to improve survival and
RT proteostasis in C. elegans.";
RL Nat. Commun. 8:14337-14337(2017).
RN [20]
RP FUNCTION, AND MUTAGENESIS OF 94-LEU--GLU-123.
RX PubMed=30102152; DOI=10.7554/elife.36588;
RA Liu Y., Zou W., Yang P., Wang L., Ma Y., Zhang H., Wang X.;
RT "Autophagy-dependent ribosomal RNA degradation is essential for maintaining
RT nucleotide homeostasis during C. elegans development.";
RL Elife 7:0-0(2018).
RN [21]
RP INTERACTION WITH ALLO-1, AND SUBCELLULAR LOCATION.
RX PubMed=29255173; DOI=10.1038/s41556-017-0008-9;
RA Sato M., Sato K., Tomura K., Kosako H., Sato K.;
RT "The autophagy receptor ALLO-1 and the IKKE-1 kinase control clearance of
RT paternal mitochondria in Caenorhabditis elegans.";
RL Nat. Cell Biol. 20:81-91(2018).
RN [22]
RP SUBCELLULAR LOCATION, AND LIPIDATION.
RX PubMed=30880001; DOI=10.1016/j.devcel.2019.02.013;
RA Hill S.E., Kauffman K.J., Krout M., Richmond J.E., Melia T.J.,
RA Colon-Ramos D.A.;
RT "Maturation and Clearance of Autophagosomes in Neurons Depends on a
RT Specific Cysteine Protease Isoform, ATG-4.2.";
RL Dev. Cell 49:251-266(2019).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-116 IN COMPLEX WITH WEEL
RP PEPTIDE, FUNCTION, INTERACTION WITH SEPA-1; SQST-1; EPG-7; EPG-2; ATG-13;
RP UNC-51; ATG-7 AND ATG-3, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP LIPIDATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-2; 3-TRP-ALA-4;
RP TRP-3; GLU-7; 14-ARG-ARG-15; ARG-28; 94-LEU--GLU-123; ASP-102; ALA-108;
RP 116-GLY--GLU-123 AND GLY-116.
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).
CC -!- FUNCTION: Ubiquitin-like modifier involved in the formation of
CC autophagosomal vacuoles (autophagosomes) (PubMed:26687600). When
CC lipidated mediates tethering between adjacent membranes and stimulates
CC membrane fusion during autophagy (PubMed:26687600, PubMed:21802374).
CC Recruits lipidated-lgg-2 to maturing autophagosomes (PubMed:12958363,
CC PubMed:20523114, PubMed:26687600). Acts in the aggrephagy pathway,
CC which is the macroautophagic degradation of ubiquitinated protein
CC aggregates, and preferentially interacts with autophagy proteins and
CC substrates containing LIR motifs to mediate autophagosome formation and
CC protein aggregate degradation (PubMed:26687600). In particular, binds
CC to components of the unc-51-atg-13 complex to regulate autophagosome
CC formation and cargo sequestration (PubMed:26687600). Required for the
CC degradation of specific sepa-1- and sqst-1-containing protein
CC aggregates during embryogenesis (PubMed:26687600). Involved in
CC allophagy, which is an autophagic process in which paternal
CC mitochondria and organelles are degraded during fertilization, and
CC moreover is required for the formation of lgg-2-positive allophagic
CC autophagosomes in embryos (PubMed:24374177). Involved in the clearance
CC of apoptotic cells by promoting the delivery of engulfed apoptotic
CC cells to the lysosome (PubMed:22451698). Plays a role in the
CC distribution and clearance of germ cell specific P-granules from
CC somatic cells (PubMed:19167332). Also plays a role in the autophagy-
CC mediated degradation of ribosomal RNA and ribosomal proteins in
CC lysosomes (PubMed:30102152). Involved in xenophagy, the autophagy-
CC mediated degradation of pathogens and pathogen products, such as toxins
CC (PubMed:27875098). Required for normal survival when exposed to
CC pathogenic bacteria S.typhimurium probably by promoting autophagic
CC degradation of intracellular S.typhimurium (PubMed:19667176). Also
CC plays a role in membrane-pore repair (PubMed:27875098). Plays a role in
CC mitophagy (PubMed:25896323). Essential for dauer development and
CC longevity, including longevity in response to moderate, short-term heat
CC shock, also known as a hormetic heat shock (PubMed:12958363,
CC PubMed:20523114, PubMed:28198373). {ECO:0000269|PubMed:12958363,
CC ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:19667176,
CC ECO:0000269|PubMed:20523114, ECO:0000269|PubMed:21802374,
CC ECO:0000269|PubMed:22451698, ECO:0000269|PubMed:24374177,
CC ECO:0000269|PubMed:25896323, ECO:0000269|PubMed:26687600,
CC ECO:0000269|PubMed:27875098, ECO:0000269|PubMed:30102152}.
CC -!- SUBUNIT: Interacts with sepa-1 (via the LIR motifs); the interaction is
CC direct (PubMed:19167332, PubMed:26687600). Interacts with allo-1 (via
CC the LIR motif) (PubMed:29255173). Interacts with sqst-1 (via the LIR
CC motifs); the interaction is direct (PubMed:26687600). Both lipidated
CC and unlipidated forms interact with epg-7 (via the LIR motif); the
CC interaction is direct (PubMed:26687600). Interacts with epg-2 (via the
CC LIR motifs); the interaction is direct (PubMed:26687600). Interacts
CC with atg-13; the interaction is direct (PubMed:26687600). Interacts
CC with unc-51 (via the LIR motif); the interaction is direct
CC (PubMed:26687600). Interacts with atg-7; the interaction is direct
CC (PubMed:26687600). Interacts with atg-3 (PubMed:26687600). The
CC interaction with atg-7 and atg-3 may be required for the lipidation of
CC lgg-1 (PubMed:26687600). {ECO:0000269|PubMed:19167332,
CC ECO:0000269|PubMed:26687600, ECO:0000269|PubMed:29255173}.
CC -!- INTERACTION:
CC Q09490; Q17740: ain-1; NbExp=3; IntAct=EBI-325374, EBI-317221;
CC Q09490; K8ESC5-2: atg-4.1; NbExp=3; IntAct=EBI-325374, EBI-331850;
CC Q09490; G5EC37: sepa-1; NbExp=3; IntAct=EBI-325374, EBI-2256317;
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure
CC {ECO:0000269|PubMed:12958363, ECO:0000269|PubMed:17327275}. Cytoplasmic
CC vesicle, autophagosome {ECO:0000269|PubMed:12958363,
CC ECO:0000269|PubMed:20523114}. Cytoplasmic vesicle, autophagosome
CC membrane {ECO:0000269|PubMed:24374177}. Lysosome lumen
CC {ECO:0000269|PubMed:24374177}. Mitochondrion
CC {ECO:0000269|PubMed:25896323}. Cytoplasm {ECO:0000269|PubMed:19167332,
CC ECO:0000269|PubMed:19377305, ECO:0000269|PubMed:20550938,
CC ECO:0000269|PubMed:21802374, ECO:0000269|PubMed:24374177,
CC ECO:0000269|PubMed:28806108, ECO:0000269|PubMed:29255173}. Cytoplasmic
CC vesicle, phagosome membrane {ECO:0000269|PubMed:22451698}. Cell
CC membrane {ECO:0000269|PubMed:24185444, ECO:0000269|PubMed:26687600};
CC Lipid-anchor {ECO:0000269|PubMed:26687600}. Cell projection, dendrite
CC {ECO:0000269|PubMed:30880001}. Perikaryon
CC {ECO:0000269|PubMed:30880001}. Note=In embryos, diffuse cytoplasmic
CC localization with some areas displaying a more punctate distribution
CC (PubMed:19377305, PubMed:19167332, PubMed:24374177, PubMed:28806108,
CC PubMed:20550938). Specifically, upon fertilization localizes to
CC autophagosomes around the male pronucleus (PubMed:24374177). During the
CC first embryonic divisions and after the 25-cell stage, localizes to a
CC large population of autophagosomes, with another smaller population of
CC autophagosomes containing both lgg-1 and lgg-2 (PubMed:24374177).
CC Localization to autophagosomes is dependent on atg-7 (PubMed:24374177).
CC Co-localizes with sepa-1 in cytoplasmic aggregates (PubMed:19167332,
CC PubMed:28806108). Partially localizes to the phagosome membrane of
CC engulfed apoptotic cells (PubMed:22451698).
CC {ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:19377305,
CC ECO:0000269|PubMed:20550938, ECO:0000269|PubMed:22451698,
CC ECO:0000269|PubMed:24374177, ECO:0000269|PubMed:28806108}.
CC -!- TISSUE SPECIFICITY: Expressed in PLML touch receptor neuron and in the
CC ventral nerve cord (PubMed:17327275). Expressed in AIY interneurons
CC (PubMed:30880001). {ECO:0000269|PubMed:17327275,
CC ECO:0000269|PubMed:30880001}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis (PubMed:19167332,
CC PubMed:24374177, PubMed:28806108, PubMed:20550938, PubMed:24185444,
CC PubMed:26687600). First expressed at the 20 cell stage with expression
CC peaking at the 80-100 cell stage, and decreasing as development
CC continues (PubMed:20550938, PubMed:24185444, PubMed:28806108,
CC PubMed:22767594). Undetectable at the comma stage (PubMed:28806108).
CC {ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:20550938,
CC ECO:0000269|PubMed:22767594, ECO:0000269|PubMed:24185444,
CC ECO:0000269|PubMed:24374177, ECO:0000269|PubMed:26687600,
CC ECO:0000269|PubMed:28806108}.
CC -!- INDUCTION: Induced in response to a moderate, short-term heat stess,
CC also known as a hormetic heat stess. {ECO:0000269|PubMed:28198373}.
CC -!- PTM: Cleaved by atg-4.1 and/or atg-4.2, after Gly-116 to form a
CC thioester bond with 'Cys-523' of atg-7 (E1-like activating enzyme)
CC before being transferred to 'Cys-255' of atg-3 (E2 conjugating enzyme),
CC in order to be amidated with phosphatidylethanolamine (Probable)
CC (PubMed:26687600, PubMed:22767594). This lipid modification anchors
CC lgg-1 to membranes and can be reversed by atg-4.2, releasing soluble
CC lgg-1 (PubMed:30880001). Lipidation regulates lgg-2-positive
CC autophagosome formation (PubMed:26687600).
CC {ECO:0000269|PubMed:22767594, ECO:0000269|PubMed:26687600,
CC ECO:0000269|PubMed:30880001, ECO:0000305|PubMed:20550938,
CC ECO:0000305|PubMed:21802374, ECO:0000305|PubMed:24185444,
CC ECO:0000305|PubMed:25124690, ECO:0000305|PubMed:30880001}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown prevents mitophagy
CC (PubMed:25896323). Accumulation of germ cell specific P-granules in
CC somatic cells as indicated by increased numbers of pgl-1 and pgl-3
CC positive granules in embryos and L1 stage larva (PubMed:19167332).
CC RNAi-mediated knockdown results in increased numbers of sepa-1- and
CC lgg-2-expressing protein aggregates in embryos (PubMed:26687600). RNAi-
CC mediated knockdown reduces autophagic degradation of membrane pore-
CC forming toxin Cry5B (PubMed:27875098). Impaired survival when exposed
CC to pathogenic bacteria S.typhimurium (PubMed:19667176). Reduces the
CC number of vacuolated (dying) touch receptor neurons in a mec-4 u231,
CC deg-1 u506 or deg-3 u662 mutants (PubMed:17327275). The extended
CC lifespan of animals exposed to hormetic heat shock early in life is
CC significantly reduced by RNAi-mediated knockdown.
CC {ECO:0000269|PubMed:17327275, ECO:0000269|PubMed:19167332,
CC ECO:0000269|PubMed:19667176, ECO:0000269|PubMed:25896323,
CC ECO:0000269|PubMed:26687600, ECO:0000269|PubMed:27875098,
CC ECO:0000269|PubMed:28198373}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR EMBL; BX284602; CCD66037.1; -; Genomic_DNA.
DR EMBL; AF326943; AAG49393.1; -; mRNA.
DR PIR; T15740; T15740.
DR RefSeq; NP_495277.1; NM_062876.5.
DR PDB; 5AZF; X-ray; 1.60 A; A/B=1-116.
DR PDB; 5AZG; X-ray; 1.81 A; A/B=1-116.
DR PDBsum; 5AZF; -.
DR PDBsum; 5AZG; -.
DR AlphaFoldDB; Q09490; -.
DR SMR; Q09490; -.
DR BioGRID; 39390; 77.
DR DIP; DIP-27176N; -.
DR ELM; Q09490; -.
DR IntAct; Q09490; 9.
DR MINT; Q09490; -.
DR STRING; 6239.C32D5.9; -.
DR EPD; Q09490; -.
DR PaxDb; Q09490; -.
DR PeptideAtlas; Q09490; -.
DR PRIDE; Q09490; -.
DR EnsemblMetazoa; C32D5.9.1; C32D5.9.1; WBGene00002980.
DR GeneID; 174050; -.
DR KEGG; cel:CELE_C32D5.9; -.
DR UCSC; C32D5.9.1; c. elegans.
DR CTD; 174050; -.
DR WormBase; C32D5.9; CE01849; WBGene00002980; lgg-1.
DR eggNOG; KOG1654; Eukaryota.
DR GeneTree; ENSGT00940000168096; -.
DR HOGENOM; CLU_119276_0_0_1; -.
DR InParanoid; Q09490; -.
DR OMA; AVYQEHK; -.
DR OrthoDB; 1508198at2759; -.
DR PhylomeDB; Q09490; -.
DR Reactome; R-CEL-1632852; Macroautophagy.
DR PRO; PR:Q09490; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002980; Expressed in embryo and 4 other tissues.
DR GO; GO:0005776; C:autophagosome; IDA:WormBase.
DR GO; GO:0000421; C:autophagosome membrane; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:WormBase.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050811; F:GABA receptor binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IGI:WormBase.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0097237; P:cellular response to toxic substance; IMP:UniProtKB.
DR GO; GO:0040024; P:dauer larval development; IGI:WormBase.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; IMP:UniProtKB.
DR GO; GO:0001778; P:plasma membrane repair; IMP:UniProtKB.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; IGI:WormBase.
DR GO; GO:0012501; P:programmed cell death; IGI:WormBase.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0098792; P:xenophagy; IMP:UniProtKB.
DR InterPro; IPR004241; Atg8-like.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10969; PTHR10969; 1.
DR Pfam; PF02991; ATG8; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Cell membrane; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; Lipoprotein; Lysosome; Membrane; Mitochondrion;
KW Reference proteome.
FT CHAIN 1..116
FT /note="Protein lgg-1"
FT /id="PRO_0000438282"
FT PROPEP 117..123
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:20550938,
FT ECO:0000305|PubMed:21802374"
FT /id="PRO_0000212377"
FT SITE 25
FT /note="Required for the interaction with unc-51"
FT /evidence="ECO:0000269|PubMed:26687600"
FT SITE 28
FT /note="Required for interaction with sqst-1"
FT /evidence="ECO:0000269|PubMed:26687600"
FT SITE 50
FT /note="Required for the interaction with unc-51"
FT /evidence="ECO:0000269|PubMed:26687600"
FT SITE 104
FT /note="Required for the interaction with unc-51"
FT /evidence="ECO:0000269|PubMed:26687600"
FT SITE 116..117
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:22767594,
FT ECO:0000305|PubMed:20550938, ECO:0000305|PubMed:21802374"
FT LIPID 116
FT /note="Phosphatidylethanolamine amidated glycine"
FT /evidence="ECO:0000269|PubMed:22767594,
FT ECO:0000305|PubMed:20550938, ECO:0000305|PubMed:21802374"
FT MUTAGEN 2
FT /note="K->A: Mildly impaired membrane tethering activity
FT and fusion in vitro."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 3..4
FT /note="WA->GG: Impaired membrane tethering activity and
FT fusion in vitro."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 3
FT /note="W->G: Does not rescue the protein aggregate
FT degradation defect in the lgg-1 bp500 mutant."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 7
FT /note="E->A: Mildly impaired membrane tethering activity
FT and fusion in vitro."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 14..15
FT /note="RR->AA: Severely impaired membrane tethering
FT activity and fusion in vitro. Does not rescue the
FT degradation defect in the lgg-1 bp500 mutant."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 28
FT /note="R->C: In bp523; abolishes interaction with sqst-1
FT and impairs the interaction with epg-7, sepa-1 and unc-51.
FT Defective degradation of sepa-1- and sqst-1-containing
FT aggregates in embryos. No defects in lipidation or puncta
FT formation."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 94..123
FT /note="Missing: In bp500; defective degradation of sepa-1-
FT containing protein aggregates in comma stage embryos.
FT Suppresses the lysosomal accumulation of ribosomal RNA and
FT ribosomal proteins in the rnst-2 qx245 mutant."
FT /evidence="ECO:0000269|PubMed:26687600,
FT ECO:0000269|PubMed:30102152"
FT MUTAGEN 102
FT /note="D->A: Defective degradation of sepa-1-containing
FT protein aggregates in embryos."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 108
FT /note="A->V: Does not rescue the degradation defect in the
FT lgg-1 bp500 mutant."
FT /evidence="ECO:0000269|PubMed:26687600"
FT MUTAGEN 116..123
FT /note="Missing: Impairs interaction with atg-3. Rescues the
FT protein degradation defect in the atg-4.1 bp501 and atg-4.2
FT tm3948 single mutants. Does not rescue the lethal phenotype
FT of the atg-4.1 bp501 and atg-4.2 tm3948 double mutant, but
FT partially rescues the protein degradation defect."
FT /evidence="ECO:0000269|PubMed:22767594,
FT ECO:0000269|PubMed:26687600"
FT MUTAGEN 116
FT /note="G->A: Diffuse cytosolic localization in 500-cell
FT embryos with no punctate pattern of distribution which is
FT in contrast to wild-type. Not cleaved by atg-4.1 and atg-
FT 4.2. Does not rescue the protein degradation defect in the
FT atg-4.1 bp501 mutant. Reduces lgg-2 lipidation and the
FT accumulation of sqst-1-containing aggregates. Abolishes the
FT interaction with atg-3."
FT /evidence="ECO:0000269|PubMed:22767594,
FT ECO:0000269|PubMed:24374177, ECO:0000269|PubMed:26687600"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:5AZF"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:5AZF"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:5AZF"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:5AZF"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:5AZF"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5AZG"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:5AZF"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:5AZF"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:5AZF"
SQ SEQUENCE 123 AA; 14764 MW; BC08727A3101875A CRC64;
MKWAYKEENN FEKRRAEGDK IRRKYPDRIP VIVEKAPKSK LHDLDKKKYL VPSDLTVGQF
YFLIRKRIQL RPEDALFFFV NNVIPQTMTT MGQLYQDHHE EDLFLYIAYS DESVYGGEVE
KKE
