GABARAPL1
entrez
23710
canonical
uniprot
Q9H0R8
canonical
ensembl
ENSG00000139112
resolver
ensp
ENSP00000266458
resolver
ensp
ENSP00000411256
resolver
genesymbol
GABARAPL1
resolver
genesymbol_syn
GEC1
resolver
hgnc
HGNC:4068
resolver
uniprot
B4E0Y7
resolver
uniprot
Q6FIE6
resolver
uniprot_entry
GBRL1_HUMAN
resolver
uniprot_sec
B4E0Y7
resolver
uniprot_sec
Q6FIE6
resolver
amino_acid_sequence
MKFQYKEDHPFEYRKKEGEKIRKKYPDRVPVIVEKAPKARVPDLDKRKYLVPSDLTVGQFYFLIRKRIHLRPEDALFFFVNNTIPPTSATMGQLYEDNHEEDYFLYVAYSDESVYGK
uniprot
proteins
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:31006537, PubMed:31006538). {ECO:0000269|PubMed:16431922, ECO:0000269|PubMed:20404487, ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}.
uniprot
proteins
mass_dalton
14044
uniprot
proteins
mutagenesis
MUTAGEN 9; /note="H->A: Abolished interaction with ATG4B."; /evidence="ECO:0000269|PubMed:28287329"; MUTAGEN 28; /note="R->A: Does not affect interaction with ATG4B."; /evidence="ECO:0000269|PubMed:28287329"; MUTAGEN 47; /note="R->A: Abolished interaction with ATG4B."; /evidence="ECO:0000269|PubMed:28287329"; MUTAGEN 67; /note="R->A: Abolished interaction with ATG4B."; /evidence="ECO:0000269|PubMed:28287329"; MUTAGEN 116; /note="G->A: No processing of precursor."; /evidence="ECO:0000269|PubMed:20404487
uniprot
proteins
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:28287329, PubMed:29458288, PubMed:30661429). 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}.
uniprot
proteins
protein_family
ATG8 family
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
11374880
uniprot
proteins
pubmed
11414770
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16431922
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17580304
uniprot
proteins
pubmed
20404487
uniprot
proteins
pubmed
20562859
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22354992
uniprot
proteins
pubmed
22470510
uniprot
proteins
pubmed
22948227
uniprot
proteins
pubmed
23043107
uniprot
proteins
pubmed
23112293
uniprot
proteins
pubmed
23690988
uniprot
proteins
pubmed
24668264
uniprot
proteins
pubmed
25127057
uniprot
proteins
pubmed
25684205
uniprot
proteins
pubmed
26347139
uniprot
proteins
pubmed
26355087
uniprot
proteins
pubmed
26929408
uniprot
proteins
pubmed
28287329
uniprot
proteins
pubmed
29420192
uniprot
proteins
pubmed
29458288
uniprot
proteins
pubmed
30661429
uniprot
proteins
pubmed
31006537
uniprot
proteins
pubmed
31006538
uniprot
proteins
pubmed
31722778
uniprot
proteins
pubmed
32315611
uniprot
proteins
pubmed
33909989
uniprot
proteins
pubmed
34338405
uniprot
proteins
sequence_length
117
uniprot
proteins
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}.
uniprot
proteins