Atg4a
entrez
666468
canonical
uniprot
Q8C9S8
canonical
ensembl
ENSMUSG00000079418
resolver
ensp
ENSMUSP00000108595
resolver
ensp
ENSMUSP00000159430
resolver
enst
ENSMUST00000112971
resolver
enst
ENSMUST00000239541
resolver
genesymbol
Atg4a
resolver
genesymbol_syn
Apg4a
resolver
genesymbol_syn
Autl2
resolver
uniprot
A0A7N9VS64
resolver
uniprot
Q5EBK1
resolver
uniprot
Q811B8
resolver
uniprot_entry
A0A7N9VS64_MOUSE
resolver
uniprot_entry
ATG4A_MOUSE
resolver
uniprot_entry
Q5EBK1_MOUSE
resolver
uniprot_sec
Q811B8
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by N-ethylmaleimide. Redox-regulated during autophagy since reducing conditions activate ATG4A whereas an oxidizing environment such as the presence of H(2)O(2) inhibits its activity. {ECO:0000250|UniProtKB:Q8WYN0}.
uniprot
proteins
amino_acid_sequence
MESVMSKYENQILIFPDYLEEFPDTDELVWILGKQHPLKTEKSKLLSDISARLWFTYRRKFSPIGGTGPSSDAGWGCMLRCGQMMLAQALICRHLGRDWNWERQKEQPKEYQRILQCFLDRKDCCYSIHQMAQMGVGEGKSIGEWFGPNTVAQVIKKLALFDEWNSLAVYVSMDNTVVIEDIKKMCCVLPVGAADPAGDFLTASNQSRDTSVPCSAWKPLLLIVPLRLGINQINPVYVEAFKECFKMPQSLGALGGKPNNAYYFIGFLGDELIFLDPHTTQTFVDIEESGLVDDQTFHCLQSPQRMSILNLDPSVALGFFCKEEKDFDNWCSLVQKEILKENLRMFELVQKHPSHWPPFVPPAKPEVTTTGAEFIESTEQLEDFELEEDFEILSVG
uniprot
proteins
ec_number
3.4.22.-
uniprot
proteins
function
FUNCTION: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Preferred substrate is GABARAPL2 followed by MAP1LC3A and GABARAP. Protease activity is also required to counteract formation of high-molecular weight conjugates of ATG8 proteins (ATG8ylation): acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3. In addition to the protease activity, also mediates delipidation of ATG8 family proteins. Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy. Compared to ATG4B, the major protein for proteolytic activation of ATG8 proteins, shows weaker ability to cleave the C-terminal amino acid of ATG8 proteins, while it displays stronger delipidation activity. Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy. {ECO:0000250|UniProtKB:Q8WYN0}.
uniprot
proteins
mass_dalton
45095
uniprot
proteins
protein_family
Peptidase C54 family
uniprot
proteins
pubmed
12446702
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
30808002
uniprot
proteins
sequence_length
396
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BGE6}.
uniprot
proteins