Gabarapl1
entrez
57436
canonical
uniprot
Q8R3R8
canonical
ensembl
ENSMUSG00000030161
resolver
ensp
ENSMUSP00000032264
resolver
ensp
ENSMUSP00000145175
resolver
enst
ENSMUST00000032264
resolver
enst
ENSMUST00000204956
resolver
genesymbol
Gabarapl1
resolver
genesymbol_syn
Apg8l
resolver
genesymbol_syn
Atg8l
resolver
genesymbol_syn
Gec1
resolver
uniprot
Q3TG14
resolver
uniprot
Q3TJB9
resolver
uniprot
Q3TXZ5
resolver
uniprot
Q9JJ97
resolver
uniprot_entry
GBRL1_MOUSE
resolver
uniprot_sec
Q3TG14
resolver
uniprot_sec
Q3TJB9
resolver
uniprot_sec
Q3TXZ5
resolver
uniprot_sec
Q9JJ97
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. 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}.
uniprot
proteins
mass_dalton
14044
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: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}.
uniprot
proteins
protein_family
ATG8 family
uniprot
proteins
pubmed
11414770
uniprot
proteins
pubmed
14530254
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16704426
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
26776506
uniprot
proteins
pubmed
33795848
uniprot
proteins
pubmed
34338405
uniprot
proteins
sequence_length
117
uniprot
proteins
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}.
uniprot
proteins