Atg3
entrez
67841
canonical
uniprot
Q9CPX6
canonical
ensembl
ENSMUSG00000022663
resolver
ensp
ENSMUSP00000023343
resolver
enst
ENSMUST00000023343
resolver
genesymbol
Atg3
resolver
genesymbol_syn
Apg3l
resolver
uniprot
Q3TXJ9
resolver
uniprot_entry
ATG3_MOUSE
resolver
uniprot_sec
Q3TXJ9
resolver
amino_acid_sequence
MQNVINTVKGKALEVAEYLTPVLKESKFKETGVITPEEFVAAGDHLVHHCPTWQWATGEELKVKAYLPTDKQFLVTKNVPCYKRCKQMEYSDELEAIIEEDDGDGGWVDTYHNTGITGITEAVKEITLESKDSIKLQDCSALCDEEDEEDEGEAADMEEYEESGLLETDEATLDTRKIVEACKAKADAGGEDAILQTRTYDLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMYEDISQDHVKKTVTIENHPHLPPPPMCSVHPCRHAEVMKKIIETVAEGGGELGVHMYLLIFLKFVQAVIPTIEYDYTRHFTM
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 (PubMed:18768753). 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 play 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 (PubMed:24747438). 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 (PubMed:20723759). ATG12-ATG3 conjugation promotes late endosome to lysosome trafficking and basal autophagosome maturation via its interaction with PDCD6IP (PubMed:25686249). 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 (PubMed:22024753). Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway (PubMed:24089205). {ECO:0000250|UniProtKB:Q9NT62, ECO:0000269|PubMed:18768753, ECO:0000269|PubMed:20723759, ECO:0000269|PubMed:22024753, ECO:0000269|PubMed:24089205, ECO:0000269|PubMed:24747438, ECO:0000269|PubMed:25686249}.
uniprot
proteins
mass_dalton
35796
uniprot
proteins
mutagenesis
MUTAGEN 4; /note="V->K: Reduces the amount of hydrophobic surface area available to partition into a bilayer. Does not affect the ATG3:GABARAPL1 intermediate. Rescues MAP1LC3B lipidation when transfected in cell lacking ATG3."; /evidence="ECO:0000269|PubMed:24747438"; MUTAGEN 5; /note="I->K: Reduces the amount of hydrophobic surface area available to partition into a bilayer. Does not affect the ATG3:GABARAPL1 intermediate."; /evidence="ECO:0000269|PubMed:24747438"; MUTAGEN 8; /note="V->D: Destroys the amphipathic character and eliminates lipidation activity. Does not affect the ATG3:GABARAPL1 intermediate."; /evidence="ECO:0000269|PubMed:24747438"; MUTAGEN 9; /note="K->D: Eliminates lipidation. Does not affect the ATG3:GABARAPL1 intermediate."; /evidence="ECO:0000269|PubMed:24747438"; MUTAGEN 11; /note="K->D: Eliminates lipidation. Does not affect the ATG3:GABARAPL1 intermediate."; /evidence="ECO:0000269|PubMed:24747438"; MUTAGEN 11; /note="K->L: Does not affect GABARAPL1 lipdation. Rescues MAP1LC3B lipidation when transfected in cell lacking ATG3."; /evidence="ECO:0000269|PubMed:24747438"; MUTAGEN 11; /note="K->R: Rescues MAP1LC3B lipidation when transfected in cell lacking ATG3."; /evidence="ECO:0000269|PubMed:24747438"; MUTAGEN 11; /note="K->W: Rescues MAP1LC3B lipidation when transfected in cell lacking ATG3."; /evidence="ECO:0000269|PubMed:24747438"; MUTAGEN 15; /note="V->K: Destroys the amphipathic character and eliminates lipidation activity. Does not affect the ATG3:GABARAPL1 intermediate."; /evidence="ECO:0000269|PubMed:24747438"; MUTAGEN 19; /note="L->K: Destroys the amphipathic character and eliminates lipidation activity. Does not affect the ATG3:GABARAPL1 intermediate."; /evidence="ECO:0000269|PubMed:24747438"; MUTAGEN 71; /note="K->R: Does not affect ATG12 conjugation."; /evidence="ECO:0000269|PubMed:20723759"; MUTAGEN 83; /note="K->R: Does not affect ATG12 conjugation."; /evidence="ECO:0000269|PubMed:20723759"; MUTAGEN 243; /note="K->R: Abolishes ATG12 conjugation, leading to an expansion in mitochondrial mass and fragmented mitochondrial morphology. Does not affect PE-conjugation to ATG8-like proteins. Reduces autophagosome maturation. Affects multivesicular bodies (MVBs) distribution and morphology. Exhibits defects in late endosome to lysosome trafficking. Does not interacts with PDCD6IP."; /evidence="ECO:0000269|PubMed:20723759, ECO:0000269|PubMed:25686249"; MUTAGEN 264; /note="C->A: Abolishes E2-like activity."; /evidence="ECO:0000269|PubMed:20723759"; MUTAGEN 271; /note="K->R: Does not affect ATG12 conjugation."; /evidence="ECO:0000269|PubMed:20723759"; MUTAGEN 295; /note="K->R: Does not affect ATG12 conjugation."; /evidence="ECO:0000269|PubMed:20723759
uniprot
proteins
post_translational_modification
PTM: Conjugated to ATG12 at Lys-243 (PubMed:20723759). 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 (PubMed:20723759). {ECO:0000269|PubMed:20723759}.; 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
pubmed
16141072
uniprot
proteins
pubmed
18321988
uniprot
proteins
pubmed
18768753
uniprot
proteins
pubmed
20723759
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22024753
uniprot
proteins
pubmed
24089205
uniprot
proteins
pubmed
24747438
uniprot
proteins
pubmed
25686249
uniprot
proteins
pubmed
29712776
uniprot
proteins
sequence_length
314
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NT62}.
uniprot
proteins