Atg3
entrez
171415
canonical
uniprot
Q6AZ50
canonical
ensembl
ENSRNOG00000002094
resolver
ensembl
ENSRNOG00055003462
resolver
ensembl
ENSRNOG00060007154
resolver
ensembl
ENSRNOG00065008548
resolver
ensp
ENSRNOP00000002906
resolver
ensp
ENSRNOP00055003988
resolver
ensp
ENSRNOP00060008878
resolver
ensp
ENSRNOP00065010094
resolver
enst
ENSRNOT00000002906
resolver
enst
ENSRNOT00055005374
resolver
enst
ENSRNOT00060011790
resolver
enst
ENSRNOT00065013594
resolver
genesymbol
Atg3
resolver
genesymbol_syn
Apg3l
resolver
uniprot
Q9ESH2
resolver
uniprot_entry
ATG3_RAT
resolver
uniprot_sec
Q9ESH2
resolver
amino_acid_sequence
MQNVINTVKGKALEVAEYLTPVLKESKFKETGVITPEEFVAAGDHLVHHCPTWQWATGEELKVKAYLPTGKQFLVTKNVPCYKRCKQMEYSDELEAIIEEDDGDGGWVDTYHNTGITGITEAVKEITLESKDSIKLQDCSVLCDEEEEEEEGEAADMEEYEESGLLETDEATLDTRRIVEACKAKADAGGEDAILQTRTYDLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMYEDISQDHVKKTVTIENHPHLPPPPMCSVHPCRHAEVMKKIIETVAEGGGELGVHMYLLIFLKFVQAVIPTIEYDYTRHFTM
uniprot
proteins
ec_number
2.3.2.-
uniprot
proteins
function
FUNCTION: E2 conjugating enzyme that catalyzes the covalent conjugation of the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A) to the amino group of phosphatidylethanolamine (PE)-containing lipids in the membrane resulting in membrane-bound ATG8-like proteins which is one of the key steps in the development of autophagic isolation membranes during autophagosome formation. Cycles back and forth between binding to ATG7 for loading with the ATG8-like proteins and binding to E3 enzyme, composed of ATG12, ATG5 and ATG16L1 to promote ATG8-like proteins lipidation (By similarity). Also plays a role as a membrane curvature sensor that facilitates LC3/GABARAP lipidation by sensing local membrane stress associated with lipid-packing defects as occurs with high molar proportions of conical lipids or strident membrane curvature (By similarity). Interacts with negatively-charged membranes promoting membrane tethering and enhancing LC3/GABARAP lipidation (By similarity). Also acts as an autocatalytic E2-like enzyme by catalyzing the conjugation of ATG12 to itself in an ATG7-dependent manner, this complex thus formed, plays a role in mitochondrial homeostasis but not in autophagy. ATG12-ATG3 conjugation promotes late endosome to lysosome trafficking and basal autophagosome maturation via its interaction with PDCD6IP. ATG12-ATG3 conjugate is also formed upon viccina virus infection, leading to the disruption the cellular autophagy which is not necessary for vaccinia survival and proliferation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway (By similarity). {ECO:0000250|UniProtKB:Q9CPX6, ECO:0000250|UniProtKB:Q9NT62}.
uniprot
proteins
mass_dalton
35822
uniprot
proteins
post_translational_modification
PTM: Conjugated to ATG12 at Lys-243. ATG12-conjugation plays a role in regulation of mitochondrial homeostasis and cell death, while it is not involved in PE-conjugation to ATG8-like proteins and autophagy. {ECO:0000250|UniProtKB:Q9CPX6}.; PTM: Cleaved by CASP8 upon death ligand binding such as tumor necrosis factor-alpha. CASP8 cleavage blocks survival-related autophagy and favors apoptosis. {ECO:0000250|UniProtKB:Q9NT62}.
uniprot
proteins
protein_family
ATG3 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
sequence_length
314
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NT62}.
uniprot
proteins