ATG3 Atg3p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Gene symbol: ATG3
Gene description: Atg3p
Primary source: SGD:S000005290
Locus tag: YNR007C
See related: AllianceGenome:SGD:S000005290
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: APG3; AUT1
Summary: Enables Atg8 ligase activity. Involved in several processes, including C-terminal protein lipidation; autophagy of nucleus; and cytoplasm to vacuole transport by the Cvt pathway. Located in phagophore and phagophore assembly site. Orthologous to human ATG3 (autophagy related 3). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See ATG3 in Genome Data Viewer

Location:: chromosome: XIV

Exon count:: 1

Sequence:: Chromosome: XIV; NC_001146.8 (639182..640114, complement)

Chromosome XIV - NC_001146.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001146.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Atg3 promotes Atg8 lipidation via altering lipid diffusion and rearrangement.
Title: Atg3 promotes Atg8 lipidation via altering lipid diffusion and rearrangement.
Atg3 is localized to autophagic structures in Saccharomyces cerevisiae.
Title: Visualization of Atg3 during autophagosome formation in Saccharomyces cerevisiae.
Atg3 is an intrinsically disordered polypeptide and the disorder/order predicted for this protein from its amino acid sequence corresponds to the experimental characteristics
Title: Identification of Atg3 as an intrinsically disordered polypeptide yields insights into the molecular dynamics of autophagy-related proteins in yeast.
Atg3 facilitates cell membrane expansion by ensuring active production of Atg8-PE on the membranes.
Title: Localization of Atg3 to autophagy-related membranes and its enhancement by the Atg8-family interacting motif to promote expansion of the membranes.
Atg12-Atg5 induces a reorientation of the cysteine residue toward the threonine residue, which enhances the conjugase activity of Atg3
Title: Atg12-Atg5 conjugate enhances E2 activity of Atg3 by rearranging its catalytic site.
Autophagic E2 enzymes Atg3 and Atg10 possess insertion regions in the middle of the core fold and may be involved in protein function.
Title: Structure of the autophagic E2 enzyme Atg10.
identified Esa1 as a histone acetyltransferase required for autophagy; identified Atg3 as a substrate for Esa1; acetylation of K19 and K48 of Atg3 regulated autophagy by controlling Atg3 and Atg8 interaction and lipidation of Atg8
Title: Function and molecular mechanism of acetylation in autophagy regulation.
Autophagy-related protein 8 (Atg8) family interacting motif in Atg3 mediates the Atg3-Atg8 interaction and is crucial for the cytoplasm-to-vacuole targeting pathway.
Title: Autophagy-related protein 8 (Atg8) family interacting motif in Atg3 mediates the Atg3-Atg8 interaction and is crucial for the cytoplasm-to-vacuole targeting pathway.
The amino-terminal region of Atg3 is essential for association with phosphatidylethanolamine in Atg8 lipidation.
Title: The amino-terminal region of Atg3 is essential for association with phosphatidylethanolamine in Atg8 lipidation.
the crystallographic structure of Atg3 provides a molecular basis for understanding the unique lipidation reaction that Atg3 carries out
Title: The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables Atg8-family ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables Atg8-family ligase activity	IEA Inferred from Electronic Annotation more info
enables Atg8-family ligase activity	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
involved_in C-terminal protein lipidation	IDA Inferred from Direct Assay more info	PubMed
involved_in C-terminal protein lipidation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in autophagosome assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in autophagosome assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in autophagy	IEA Inferred from Electronic Annotation more info
involved_in autophagy of mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
involved_in autophagy of mitochondrion	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cytoplasm to vacuole targeting by the Cvt pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in glycophagy	IBA Inferred from Biological aspect of Ancestor more info
involved_in nucleophagy	IBA Inferred from Biological aspect of Ancestor more info
involved_in nucleophagy	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in piecemeal microautophagy of the nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein transport	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	HDA more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	IEA Inferred from Electronic Annotation more info
located_in phagophore	IDA Inferred from Direct Assay more info	PubMed
located_in phagophore	IMP Inferred from Mutant Phenotype more info	PubMed
is_active_in phagophore assembly site	IBA Inferred from Biological aspect of Ancestor more info
located_in phagophore assembly site	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: Atg3p

NP_014404.3

E2-like enzyme; involved in autophagy and cytoplasm-to-vacuole targeting (Cvt) pathway; plays a role in formation of Atg8p-phosphatidylethanolamine conjugates, which are involved in membrane dynamics during autophagy and Cvt; interaction with Atg8p regulated by acetylation by NuA4 histone acetyltransferase Esa1p while attenuation of Atg3 acetylation is mediated by histone deacetylase Rpd3p; Atg12p-Atg5p conjugate enhances E2 activity of Atg3p by rearranging its catalytic site

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001146.8 Reference assembly

Range

639182..640114 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001183184.3 → NP_014404.3 TPA: Atg3p [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_014404.3

Status: REVIEWED

UniProtKB/Swiss-Prot

A6ZS81, D6W1I2, P40344

UniProtKB/TrEMBL

A0A6A5Q5D7, B3LPN3, B5VR38, C7GLP8, C8ZFN4, G2WL64, N1NY52

Conserved Domains (2) summary

pfam03986
Location:2 → 141

Autophagy_N; Autophagocytosis associated protein (Atg3), N-terminal domain

pfam03987
Location:32 → 305

Autophagy_act_C; Autophagocytosis associated protein, active-site domain