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ATG14

Domain

The coiled-coil domain is required for BECN1- and PIK3C3-binding and for autophagy.

The final 80 residues in the C-terminus define a minimum required region for autophagosome binding called BATS.

The N-terminal cysteine repeats are required for proper localization to the endoplasmic reticulum.

Function

Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1 (PubMed:18843052, PubMed:19050071). Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine (PubMed:19270696, PubMed:20713597). Promotes BECN1 translocation from the trans-Golgi network to autophagosomes (PubMed:20713597). Enhances PIK3C3 activity in a BECN1-dependent manner. Essential for the autophagy-dependent phosphorylation of BECN1 (PubMed:23878393). Stimulates the phosphorylation of BECN1, but suppresses the phosphorylation PIK3C3 by AMPK (PubMed:23878393). Binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion (PubMed:25686604, PubMed:37632749). Modulates the hepatic lipid metabolism (By similarity).

Post-translational modifications

Ubiquitinated via 'Lys-6', 'Lys-11' and 'Lys-63'-linked polyubiquitin chains on multiple lysines by MARCHF7, leading to ATG14 aggregation and loss of interaction with STX17.

Sequence Similarities

Belongs to the ATG14 family.

Cellular localization

Alternative names

ATG14L, KIAA0831, ATG14, Beclin 1-associated autophagy-related key regulator, Barkor, Autophagy-related protein 14-like protein, Atg14L

swissprot:Q6ZNE5 omim:613515 entrezGene:22863