IED ID | IndEnz0002005551 |
Enzyme Type ID | protease005551 |
Protein Name |
Gamma-aminobutyric acid receptor-associated protein-like 1 GABA A receptor-associated protein-like 1 Glandular epithelial cell protein 1 GEC-1 |
Gene Name | Gabarapl1 Apg8l Atg8l Gec1 MNCb-0091 |
Organism | Mus musculus (Mouse) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
Enzyme Sequence | MKFQYKEDHPFEYRKKEGEKIRKKYPDRVPVIVEKAPKARVPDLDKRKYLVPSDLTVGQFYFLIRKRIHLRPEDALFFFVNNTIPPTSATMGQLYEDNHEEDYFLYVAYSDESVYGK |
Enzyme Length | 117 |
Uniprot Accession Number | Q8R3R8 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Ubiquitin-like modifier that increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor. Involved in formation of autophagosomal vacuoles. While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover. {ECO:0000250|UniProtKB:Q9H0R8}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (4); Chain (1); Erroneous initiation (1); Helix (4); Lipidation (2); Propeptide (1); Sequence conflict (2); Site (1) |
Keywords | 3D-structure;Autophagy;Cytoplasm;Cytoplasmic vesicle;Cytoskeleton;Endoplasmic reticulum;Golgi apparatus;Lipoprotein;Membrane;Microtubule;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:14530254}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9H0R8}; Lipid-anchor {ECO:0000250|UniProtKB:Q9H0R8}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q0VGK0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q0VGK0}. Golgi apparatus {ECO:0000250|UniProtKB:Q0VGK0}. |
Modified Residue | |
Post Translational Modification | PTM: The precursor molecule is cleaved by ATG4 (ATG4A, ATG4B, ATG4C or ATG4D) to expose the glycine at the C-terminus and form the cytosolic form, GABARAPL1-I (PubMed:14530254, PubMed:16704426). The processed form is then activated by APG7L/ATG7, transferred to ATG3 and conjugated to phosphatidylethanolamine (PE) phospholipid to form the membrane-bound form, GABARAPL1-II (By similarity). During non-canonical autophagy, the processed form is conjugated to phosphatidylserine (PS) phospholipid (By similarity). ATG4 proteins also mediate the delipidation of PE-conjugated forms required for GABARAPL1 recycling when autophagosomes fuse with lysosomes (PubMed:33795848). In addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins conjugated to PS during non-canonical autophagy (By similarity). ATG4B constitutes the major protein for proteolytic activation (By similarity). ATG4D is the main enzyme for delipidation activity (PubMed:33795848). {ECO:0000250|UniProtKB:Q9H0R8, ECO:0000269|PubMed:14530254, ECO:0000269|PubMed:16704426, ECO:0000269|PubMed:33795848}. |
Signal Peptide | |
Structure 3D | X-ray crystallography (2) |
Cross Reference PDB | 5YIP; 7CDB; |
Mapped Pubmed ID | 11217851; 11374880; 12466851; 15292400; 16602821; 17727637; 18451111; 20010802; 20577052; 21267068; 22079573; 28604719; 29867141; 31693883; 32876528; 33436612; |
Motif | |
Gene Encoded By | |
Mass | 14,044 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |