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ATG3

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In molecular biology, autophagy related 3 (Atg3) is the E2 enzyme for the LC3 lipidation process.[5] It is essential for autophagy. The super protein complex, the Atg16L complex, consists of multiple Atg12-Atg5 conjugates. Atg16L has an E3-like role in the LC3 lipidation reaction. The activated intermediate, LC3-Atg3 (E2), is recruited to the site where the lipidation takes place.[6]

AliasesATG3, APG3-LIKE, APG3, autophagy related 3, APG3L, PC3-96
External IDsOMIM: 609606; MGI: 1915091; GeneCards: ATG3
PDBOrtholog search: PDBe RCSB
Quick facts Identifiers, Aliases ...
ATG3
Identifiers
AliasesATG3, APG3-LIKE, APG3, autophagy related 3, APG3L, PC3-96
External IDsOMIM: 609606; MGI: 1915091; GeneCards: ATG3
Available structures
PDBOrtholog search: PDBe RCSB
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001278712
NM_022488

NM_026402
NM_001356366

RefSeq (protein)

NP_001265641
NP_071933

NP_080678
NP_001343295

Location (UCSC)Chr 3: 112.53 – 112.56 MbChr 16: 44.98 – 45.01 Mb
PubMed search[3][4]
Wikidata
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Quick facts Autophagocytosis associated protein N-terminal, Identifiers ...
Autophagocytosis associated protein N-terminal
Identifiers
SymbolAutophagy_N
PfamPF03986
InterProIPR007134
Available protein structures:
PDB  IPR007134 PF03986 (ECOD; PDBsum)  
AlphaFold
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Quick facts Autophagocytosis associated protein active site domain, Identifiers ...
Autophagocytosis associated protein active site domain
Identifiers
SymbolAutophagy_act_C
PfamPF03987
InterProIPR007135
Available protein structures:
PDB  IPR007135 PF03987 (ECOD; PDBsum)  
AlphaFold
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Quick facts Autophagocytosis associated protein C-terminal, Identifiers ...
Autophagocytosis associated protein C-terminal
Identifiers
SymbolAutophagy_Cterm
PfamPF10381
InterProIPR019461
Available protein structures:
PDB  IPR019461 PF10381 (ECOD; PDBsum)  
AlphaFold
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Atg3 catalyses the conjugation of Atg8 and phosphatidylethanolamine (PE). Atg3 has an alpha/beta-fold, and its core region is topologically similar to canonical E2 enzymes. Atg3 has two regions inserted in the core region and another with a long alpha-helical structure that protrudes from the core region as far as 30 A.[7] It interacts with atg8 through an intermediate thioester bond between Cys-288 and the C-terminal Gly of atg8. It also interacts with the C-terminal region of the E1-like atg7 enzyme.

Autophagocytosis is a starvation-induced process responsible for transport of cytoplasmic proteins to the lysosome/vacuole. Atg3 is a ubiquitin like modifier that is topologically similar to the canonical E2 enzyme.[8] It catalyses the conjugation of Atg8 and phosphatidylethanolamine.[9]

Atg3 consists of three domains, an N-terminal domain, a catalytic domain and a C-terminal domain. The catalytic domain contains a cysteine residue within an HPC motif, this is the putative active-site residue for recognition of the Apg5 subunit of the autophagosome complex.[10] The small C-terminal domain is likely to be a distinct binding region for the stability of the autophagosome complex.[11] It carries a highly characteristic conserved FLKF sequence motif.

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