| IED ID | IndEnz0002003360 |
| Enzyme Type ID | protease003360 |
| Protein Name |
Gamma-aminobutyric acid receptor-associated protein GABA A receptor-associated protein |
| Gene Name | Gabarap |
| 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 | MKFVYKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMGQLYQEHHEEDFFLYIAYSDESVYGL |
| Enzyme Length | 117 |
| Uniprot Accession Number | Q9DCD6 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in autophagy: 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. Also required for the local activation of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex, regulating ubiquitination and degradation of TIAM1, a guanyl-nucleotide exchange factor (GEF) that activates RAC1 and downstream signal transduction. Thereby, regulates different biological processes including the organization of the cytoskeleton, cell migration and proliferation. Involved in apoptosis. {ECO:0000250|UniProtKB:O95166}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (4); Chain (1); Helix (4); Lipidation (2); Propeptide (1); Region (3); Sequence conflict (1); Site (1) |
| Keywords | 3D-structure;Apoptosis;Autophagy;Cytoplasm;Cytoplasmic vesicle;Cytoskeleton;Golgi apparatus;Lipoprotein;Membrane;Microtubule;Protein transport;Reference proteome;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:14530254}. Endomembrane system {ECO:0000250|UniProtKB:P60517}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10899939}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P60517}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P60517}. Note=Largely associated with intracellular membrane structures including the Golgi apparatus and postsynaptic cisternae. Colocalizes with microtubules (PubMed:10899939). Localizes also to discrete punctae along the ciliary axoneme (PubMed:24089209). {ECO:0000269|PubMed:10899939, ECO:0000269|PubMed:14530254, ECO:0000269|PubMed:24089209}. |
| 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, GABARAP-I (PubMed:14530254). The processed form is then activated by APG7L/ATG7, transferred to ATG3 and conjugated to phosphatidylethanolamine (PE) phospholipid to form the membrane-bound form, GABARAP-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 (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:O95166, ECO:0000269|PubMed:14530254, ECO:0000269|PubMed:33795848}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5YIR; 6A9X; |
| Mapped Pubmed ID | 11146101; 11217851; 12466851; 14610273; 15365296; 16307606; 16602821; 16874098; 16954214; 18451111; 18497328; 19225049; 20010802; 20354864; 20577052; 21267068; 21388957; 21677750; 22033522; 22049402; 22948227; 23427251; 23671684; 24240096; 24668264; 24747438; 27124579; 28320742; 28497576; 28604719; 29867141; 30504823; 32876528; 33042141; 33436612; 33591943; 34338405; |
| Motif | |
| Gene Encoded By | |
| Mass | 13,918 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |