Detail Information for IndEnz0002003359
IED ID IndEnz0002003359
Enzyme Type ID protease003359
Protein Name Gamma-aminobutyric acid receptor-associated protein-like 1
Early estrogen-regulated protein
GABA
A
receptor-associated protein-like 1
Glandular epithelial cell protein 1
GEC-1
Gene Name GABARAPL1 GEC1
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MKFQYKEDHPFEYRKKEGEKIRKKYPDRVPVIVEKAPKARVPDLDKRKYLVPSDLTVGQFYFLIRKRIHLRPEDALFFFVNNTIPPTSATMGQLYEDNHEEDYFLYVAYSDESVYGK
Enzyme Length 117
Uniprot Accession Number Q9H0R8
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 (PubMed:16431922). Involved in formation of autophagosomal vacuoles (PubMed:20404487). While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:20404487). 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 (PubMed:31006538, PubMed:31006537). {ECO:0000269|PubMed:16431922, ECO:0000269|PubMed:20404487, ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Beta strand (5); Chain (1); Helix (4); Lipidation (2); Mutagenesis (5); Propeptide (1); Site (2)
Keywords 3D-structure;Alternative splicing;Autophagy;Cytoplasm;Cytoplasmic vesicle;Cytoskeleton;Endoplasmic reticulum;Golgi apparatus;Lipoprotein;Membrane;Microtubule;Reference proteome
Interact With Q8IVF2-2; Q8IVF2-3; O75143; Q2TAZ0; Q9NT62; Q8WYN0; Q9Y4P1; O95352; O60238; J3KQ12; Q9NW68; Q9P1Z2; Q13137; Q14677; Q9NRI5-2; Q8WXU2; P63167; Q8TF40; Q9BQS8; P40939; P55084; O00410; Q86V97; Q8WVZ9; P60409; P60411; Q9BQD3; Q9UH92-3; Q14596; Q8NI08; P46934; P46934-3; Q8TD19; Q12857-2; O75323; Q92636; P41145; Q9H4L5; Q96AQ6; P10644; P28070; Q15256-5; Q9Y3P9; Q8WWW0; Q14257; Q86VR2; Q14151; Q8IZE3; Q8IZE3-2; Q13501; O95210; Q13188; Q13043; Q13033-2; Q86VP1; Q8TC07; Q3MII6; Q9UPU7; B9A6K1; Q92609; O15040; Q9BT49; Q0P631; Q15025; Q96A56; Q9GZZ9; O75385; C9J7I0; Q8IZQ1; O15209; Q9Z2F7
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:20404487, ECO:0000269|PubMed:30661429, ECO:0000305|PubMed:23690988}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:20404487}; Lipid-anchor {ECO:0000269|PubMed:20404487}. 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:20404487, PubMed:29458288, PubMed:30661429, PubMed:28287329). 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 (PubMed:20404487, PubMed:29458288). During non-canonical autophagy, the processed form is conjugated to phosphatidylserine (PS) phospholipid (PubMed:33909989). ATG4 proteins also mediate the delipidation of PE-conjugated forms required for GABARAPL1 recycling when autophagosomes fuse with lysosomes (PubMed:20404487, PubMed:29458288, PubMed:33909989). In addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins conjugated to PS during non-canonical autophagy (PubMed:33909989). ATG4B constitutes the major protein for proteolytic activation (PubMed:30661429). ATG4D is the main enzyme for delipidation activity (By similarity). {ECO:0000250|UniProtKB:Q8R3R8, ECO:0000269|PubMed:20404487, ECO:0000269|PubMed:28287329, ECO:0000269|PubMed:29458288, ECO:0000269|PubMed:30661429, ECO:0000269|PubMed:33909989}.; PTM: (Microbial infection) The Legionella effector RavZ is a deconjugating enzyme that hydrolyzes the amide bond between the C-terminal glycine residue and an adjacent aromatic residue in ATG8 proteins conjugated to phosphatidylethanolamine (PE), producing an ATG8 protein that is resistant to reconjugation by the host machinery due to the cleavage of the reactive C-terminal glycine (PubMed:23112293, PubMed:31722778). RavZ is also able to mediate delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed:33909989). {ECO:0000269|PubMed:23112293, ECO:0000269|PubMed:31722778, ECO:0000269|PubMed:33909989}.
Signal Peptide
Structure 3D NMR spectroscopy (1); X-ray crystallography (10)
Cross Reference PDB 2L8J; 2R2Q; 5DPT; 5LXH; 5LXI; 6HOI; 6HOL; 6YOO; 7AA7; 7AA9; 7JHX;
Mapped Pubmed ID 11825910; 14625090; 15187094; 16189514; 18321988; 19001416; 19250911; 19322194; 19549685; 19596235; 20010802; 20197771; 20628624; 21177865; 21516116; 21597319; 21620860; 21893048; 22120110; 22170151; 22959883; 23602568; 24647565; 24747438; 24879149; 25416956; 25568151; 26050226; 26474850; 27623937; 28655748; 28729737; 29535191; 30767700; 32685442; 33374830; 33674710;
Motif
Gene Encoded By
Mass 14,044
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda