| IED ID |
IndEnz0002002253 |
| Enzyme Type ID |
protease002253 |
| Protein Name |
Protein lgg-1
|
| Gene Name |
lgg-1 atg-8.1 C32D5.9 |
| Organism |
Caenorhabditis elegans |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Metazoa
Eumetazoa
Bilateria
Protostomia
Ecdysozoa
Nematoda (roundworms)
Chromadorea
Rhabditida
Rhabditina
Rhabditomorpha
Rhabditoidea
Rhabditidae
Peloderinae
Caenorhabditis
Caenorhabditis elegans
|
| Enzyme Sequence |
MKWAYKEENNFEKRRAEGDKIRRKYPDRIPVIVEKAPKSKLHDLDKKKYLVPSDLTVGQFYFLIRKRIQLRPEDALFFFVNNVIPQTMTTMGQLYQDHHEEDLFLYIAYSDESVYGGEVEKKE |
| Enzyme Length |
123 |
| Uniprot Accession Number |
Q09490 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Ubiquitin-like modifier involved in the formation of autophagosomal vacuoles (autophagosomes) (PubMed:26687600). When lipidated mediates tethering between adjacent membranes and stimulates membrane fusion during autophagy (PubMed:26687600, PubMed:21802374). Recruits lipidated-lgg-2 to maturing autophagosomes (PubMed:12958363, PubMed:20523114, PubMed:26687600). Acts in the aggrephagy pathway, which is the macroautophagic degradation of ubiquitinated protein aggregates, and preferentially interacts with autophagy proteins and substrates containing LIR motifs to mediate autophagosome formation and protein aggregate degradation (PubMed:26687600). In particular, binds to components of the unc-51-atg-13 complex to regulate autophagosome formation and cargo sequestration (PubMed:26687600). Required for the degradation of specific sepa-1- and sqst-1-containing protein aggregates during embryogenesis (PubMed:26687600). Involved in allophagy, which is an autophagic process in which paternal mitochondria and organelles are degraded during fertilization, and moreover is required for the formation of lgg-2-positive allophagic autophagosomes in embryos (PubMed:24374177). Involved in the clearance of apoptotic cells by promoting the delivery of engulfed apoptotic cells to the lysosome (PubMed:22451698). Plays a role in the distribution and clearance of germ cell specific P-granules from somatic cells (PubMed:19167332). Also plays a role in the autophagy-mediated degradation of ribosomal RNA and ribosomal proteins in lysosomes (PubMed:30102152). Involved in xenophagy, the autophagy-mediated degradation of pathogens and pathogen products, such as toxins (PubMed:27875098). Required for normal survival when exposed to pathogenic bacteria S.typhimurium probably by promoting autophagic degradation of intracellular S.typhimurium (PubMed:19667176). Also plays a role in membrane-pore repair (PubMed:27875098). Plays a role in mitophagy (PubMed:25896323). Essential for dauer development and longevity, including longevity in response to moderate, short-term heat shock, also known as a hormetic heat shock (PubMed:12958363, PubMed:20523114, PubMed:28198373). {ECO:0000269|PubMed:12958363, ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:19667176, ECO:0000269|PubMed:20523114, ECO:0000269|PubMed:21802374, ECO:0000269|PubMed:22451698, ECO:0000269|PubMed:24374177, ECO:0000269|PubMed:25896323, ECO:0000269|PubMed:26687600, ECO:0000269|PubMed:27875098, ECO:0000269|PubMed:30102152}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Beta strand (5); Chain (1); Helix (4); Lipidation (1); Mutagenesis (11); Propeptide (1); Site (5) |
| Keywords |
3D-structure;Autophagy;Cell membrane;Cell projection;Cytoplasm;Cytoplasmic vesicle;Lipoprotein;Lysosome;Membrane;Mitochondrion;Reference proteome |
| Interact With |
Q17740; K8ESC5-2; G5EC37 |
| Induction |
INDUCTION: Induced in response to a moderate, short-term heat stess, also known as a hormetic heat stess. {ECO:0000269|PubMed:28198373}. |
| Subcellular Location |
SUBCELLULAR LOCATION: Preautophagosomal structure {ECO:0000269|PubMed:12958363, ECO:0000269|PubMed:17327275}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:12958363, ECO:0000269|PubMed:20523114}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:24374177}. Lysosome lumen {ECO:0000269|PubMed:24374177}. Mitochondrion {ECO:0000269|PubMed:25896323}. Cytoplasm {ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:19377305, ECO:0000269|PubMed:20550938, ECO:0000269|PubMed:21802374, ECO:0000269|PubMed:24374177, ECO:0000269|PubMed:28806108, ECO:0000269|PubMed:29255173}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:22451698}. Cell membrane {ECO:0000269|PubMed:24185444, ECO:0000269|PubMed:26687600}; Lipid-anchor {ECO:0000269|PubMed:26687600}. Cell projection, dendrite {ECO:0000269|PubMed:30880001}. Perikaryon {ECO:0000269|PubMed:30880001}. Note=In embryos, diffuse cytoplasmic localization with some areas displaying a more punctate distribution (PubMed:19377305, PubMed:19167332, PubMed:24374177, PubMed:28806108, PubMed:20550938). Specifically, upon fertilization localizes to autophagosomes around the male pronucleus (PubMed:24374177). During the first embryonic divisions and after the 25-cell stage, localizes to a large population of autophagosomes, with another smaller population of autophagosomes containing both lgg-1 and lgg-2 (PubMed:24374177). Localization to autophagosomes is dependent on atg-7 (PubMed:24374177). Co-localizes with sepa-1 in cytoplasmic aggregates (PubMed:19167332, PubMed:28806108). Partially localizes to the phagosome membrane of engulfed apoptotic cells (PubMed:22451698). {ECO:0000269|PubMed:19167332, ECO:0000269|PubMed:19377305, ECO:0000269|PubMed:20550938, ECO:0000269|PubMed:22451698, ECO:0000269|PubMed:24374177, ECO:0000269|PubMed:28806108}. |
| Modified Residue |
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| Post Translational Modification |
PTM: Cleaved by atg-4.1 and/or atg-4.2, after Gly-116 to form a thioester bond with 'Cys-523' of atg-7 (E1-like activating enzyme) before being transferred to 'Cys-255' of atg-3 (E2 conjugating enzyme), in order to be amidated with phosphatidylethanolamine (Probable) (PubMed:26687600, PubMed:22767594). This lipid modification anchors lgg-1 to membranes and can be reversed by atg-4.2, releasing soluble lgg-1 (PubMed:30880001). Lipidation regulates lgg-2-positive autophagosome formation (PubMed:26687600). {ECO:0000269|PubMed:22767594, ECO:0000269|PubMed:26687600, ECO:0000269|PubMed:30880001, ECO:0000305|PubMed:20550938, ECO:0000305|PubMed:21802374, ECO:0000305|PubMed:24185444, ECO:0000305|PubMed:25124690, ECO:0000305|PubMed:30880001}. |
| Signal Peptide |
|
| Structure 3D |
X-ray crystallography (2) |
| Cross Reference PDB |
5AZF;
5AZG;
|
| Mapped Pubmed ID |
14704431;
15338614;
15791247;
17850180;
17901876;
18182484;
19123269;
20382828;
21085631;
21110867;
21177967;
21502138;
21611156;
21906946;
21998252;
22033522;
22105480;
22157748;
22560223;
22560298;
22862955;
22901814;
23335331;
23392608;
23530068;
23619095;
23800452;
24165672;
24185352;
24882217;
25126728;
25487147;
26759963;
26999449;
27562069;
30160610;
30610704;
30910027;
|
| Motif |
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| Gene Encoded By |
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| Mass |
14,764 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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