Gabarapl2
entrez
93739
canonical
uniprot
P60521
canonical
ensembl
ENSMUSG00000031950
resolver
ensp
ENSMUSP00000034428
resolver
enst
ENSMUST00000034428
resolver
genesymbol
Gabarapl2
resolver
uniprot
O08765
resolver
uniprot
Q9DCP8
resolver
uniprot
Q9UQF7
resolver
uniprot_entry
GBRL2_MOUSE
resolver
uniprot_sec
O08765
resolver
uniprot_sec
Q9DCP8
resolver
uniprot_sec
Q9UQF7
resolver
amino_acid_sequence
MKWMFKEDHSLEHRCVESAKIRAKYPDRVPVIVEKVSGSQIVDIDKRKYLVPSDITVAQFMWIIRKRIQLPSEKAIFLFVDKTVPQSSLTMGQLYEKEKDEDGFLYVAYSGENTFGF
uniprot
proteins
function
FUNCTION: Ubiquitin-like modifier involved in intra-Golgi traffic. Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation. It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 (By similarity). Involved in autophagy. Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (By similarity). {ECO:0000250|UniProtKB:P60519, ECO:0000250|UniProtKB:P60520}.
uniprot
proteins
mass_dalton
13667
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, GABARAPL2-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, GABARAPL2-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 GABARAPL2 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:P60520, ECO:0000269|PubMed:14530254, ECO:0000269|PubMed:33795848}.; PTM: Phosphorylation at Ser-87 and Ser-88 by TBK1 prevents interaction with ATG4 (ATG4A, ATG4B, ATG4C or ATG4D). Phosphorylation by TBK1 on autophagosomes prevents their delipidation by ATG4 and premature removal from nascent autophagosomes. {ECO:0000250|UniProtKB:P60520}.
uniprot
proteins
protein_family
ATG8 family
uniprot
proteins
pubmed
11414770
uniprot
proteins
pubmed
11890701
uniprot
proteins
pubmed
14530254
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21383079
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}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P60520}. Golgi apparatus {ECO:0000250|UniProtKB:P60519}.
uniprot
proteins