UniProt functional annotation for P38862



	UniProt functional annotation for P38862

UniProt code: P38862.

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).

Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.

Function: E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for its conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Plays a role in the regulation of filamentous growth and chronological longevity. {ECO:0000269|PubMed:10233148, ECO:0000269|PubMed:10233150, ECO:0000269|PubMed:11100732, ECO:0000269|PubMed:11149920, ECO:0000269|PubMed:12965207, ECO:0000269|PubMed:15277523, ECO:0000269|PubMed:16027116, ECO:0000269|PubMed:17632063, ECO:0000269|PubMed:17890363, ECO:0000269|PubMed:18544538, ECO:0000269|PubMed:18701704, ECO:0000269|PubMed:18725539, ECO:0000269|PubMed:19061865, ECO:0000269|PubMed:19302372, ECO:0000269|PubMed:22055191, ECO:0000269|PubMed:22768199, ECO:0000269|PubMed:22785534, ECO:0000269|PubMed:23660403, ECO:0000269|PubMed:29295865, ECO:0000269|PubMed:7593182, ECO:0000269|PubMed:8224160, ECO:0000269|PubMed:9759731}.

Subunit: Homodimer; homodimerization is required for ATP-binding (PubMed:11139573, PubMed:21193819, PubMed:29295865). Interacts with ATG8 through a thioester bond between Cys-507 and the C-terminal 'Gly- 116' of ATG8 and with ATG12 through a thioester bond between Cys-507 and the C-terminal 'Gly-186' of ATG12 (PubMed:10233150, PubMed:11100732, PubMed:16874032, PubMed:18544538, PubMed:22055191). Interacts also with ATG3 (PubMed:11139573, PubMed:17227760, PubMed:22056771, PubMed:23142976). {ECO:0000269|PubMed:10233150, ECO:0000269|PubMed:11100732, ECO:0000269|PubMed:11139573, ECO:0000269|PubMed:16874032, ECO:0000269|PubMed:17227760, ECO:0000269|PubMed:18544538, ECO:0000269|PubMed:21193819, ECO:0000269|PubMed:22055191, ECO:0000269|PubMed:22056771, ECO:0000269|PubMed:23142976, ECO:0000269|PubMed:29295865}.

Subcellular location: Cytoplasm. Preautophagosomal structure.

Domain: The C-terminal 40 residues are required for homodimerization, as well as the interactions with ATG3, ATG8 and ATG12; and the C- terminal 17 residues are required for the ATG8 lipidation.

Domain: The GxGxxG motif is important for the function, possibly through binding with ATP.

Similarity: Belongs to the ATG7 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.



Function:		E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for its conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Plays a role in the regulation of filamentous growth and chronological longevity. {ECO:0000269\|PubMed:10233148, ECO:0000269\|PubMed:10233150, ECO:0000269\|PubMed:11100732, ECO:0000269\|PubMed:11149920, ECO:0000269\|PubMed:12965207, ECO:0000269\|PubMed:15277523, ECO:0000269\|PubMed:16027116, ECO:0000269\|PubMed:17632063, ECO:0000269\|PubMed:17890363, ECO:0000269\|PubMed:18544538, ECO:0000269\|PubMed:18701704, ECO:0000269\|PubMed:18725539, ECO:0000269\|PubMed:19061865, ECO:0000269\|PubMed:19302372, ECO:0000269\|PubMed:22055191, ECO:0000269\|PubMed:22768199, ECO:0000269\|PubMed:22785534, ECO:0000269\|PubMed:23660403, ECO:0000269\|PubMed:29295865, ECO:0000269\|PubMed:7593182, ECO:0000269\|PubMed:8224160, ECO:0000269\|PubMed:9759731}.


Subunit:		Homodimer; homodimerization is required for ATP-binding (PubMed:11139573, PubMed:21193819, PubMed:29295865). Interacts with ATG8 through a thioester bond between Cys-507 and the C-terminal 'Gly- 116' of ATG8 and with ATG12 through a thioester bond between Cys-507 and the C-terminal 'Gly-186' of ATG12 (PubMed:10233150, PubMed:11100732, PubMed:16874032, PubMed:18544538, PubMed:22055191). Interacts also with ATG3 (PubMed:11139573, PubMed:17227760, PubMed:22056771, PubMed:23142976). {ECO:0000269\|PubMed:10233150, ECO:0000269\|PubMed:11100732, ECO:0000269\|PubMed:11139573, ECO:0000269\|PubMed:16874032, ECO:0000269\|PubMed:17227760, ECO:0000269\|PubMed:18544538, ECO:0000269\|PubMed:21193819, ECO:0000269\|PubMed:22055191, ECO:0000269\|PubMed:22056771, ECO:0000269\|PubMed:23142976, ECO:0000269\|PubMed:29295865}.
Subcellular location:		Cytoplasm. Preautophagosomal structure.
Domain:		The C-terminal 40 residues are required for homodimerization, as well as the interactions with ATG3, ATG8 and ATG12; and the C- terminal 17 residues are required for the ATG8 lipidation.
Domain:		The GxGxxG motif is important for the function, possibly through binding with ATP.
Similarity:		Belongs to the ATG7 family. {ECO:0000305}.