ATG3_YEAS7
ID ATG3_YEAS7 Reviewed; 310 AA.
AC A6ZS81;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Autophagy-related protein 3;
DE AltName: Full=Autophagy-related E2-like conjugation enzyme ATG3;
GN Name=ATG3; ORFNames=SCY_4792;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole
CC transport (Cvt) and autophagy. Required for selective autophagic
CC degradation of the nucleus (nucleophagy) as well as for mitophagy which
CC contributes to regulate mitochondrial quantity and quality by
CC eliminating the mitochondria to a basal level to fulfill cellular
CC energy requirements and preventing excess ROS production. Responsible
CC for the E2-like covalent binding of phosphatidylethanolamine to the C-
CC terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3
CC and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine
CC (PE). This step is required for the membrane association of ATG8. The
CC formation of the ATG8-phosphatidylethanolamine conjugate is essential
CC for autophagy and for the cytoplasm to vacuole transport (Cvt). The
CC ATG8-PE conjugate mediates tethering between adjacent membranes and
CC stimulates membrane hemifusion, leading to expansion of the
CC autophagosomal membrane during autophagy (By similarity).
CC {ECO:0000250}.
CC -!- ACTIVITY REGULATION: ATG12-ATG5 induces reorientation of the ATG3
CC structure, increasing conjugation activity of ATG3. {ECO:0000250}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with ATG8 through an
CC intermediate thioester bond between Cys-234 and the C-terminal Gly of
CC ATG8 (By similarity). Also interacts with the 40 amino acid C-terminal
CC region of the E1-like ATG7 enzyme. Interacts also with the ATG12-ATG5
CC conjugate (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The N-terminal region (residues 1-7) is involved in
CC phosphatidylethanolamine-binding and is required for ATG8-PE
CC conjugation. {ECO:0000250}.
CC -!- DOMAIN: The flexible region (FR) is required for ATG7-binding.
CC {ECO:0000250}.
CC -!- DOMAIN: The handle region (HR) contains the ATG8 interaction motif
CC (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-
CC vacuole targeting pathway (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylated by NuA4 complex acetyltransferase ESA1 at Lys-19 and
CC Lys-48. Acetylation regulates autophagy by controlling ATG8 interaction
CC and lipidation. Deacetylated by histone deacetylase RPD3 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFW02000067; EDN62813.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZS81; -.
DR SMR; A6ZS81; -.
DR EnsemblFungi; EDN62813; EDN62813; SCY_4792.
DR HOGENOM; CLU_027518_2_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR007135; Atg3/Atg10.
DR PANTHER; PTHR12866; PTHR12866; 1.
DR Pfam; PF03987; Autophagy_act_C; 1.
PE 3: Inferred from homology;
KW Acetylation; Autophagy; Cytoplasm; Protein transport; Transport;
KW Ubl conjugation pathway.
FT CHAIN 1..310
FT /note="Autophagy-related protein 3"
FT /id="PRO_0000317831"
FT REGION 83..163
FT /note="Flexible region"
FT /evidence="ECO:0000250"
FT REGION 238..285
FT /note="Handle region"
FT /evidence="ECO:0000250"
FT MOTIF 270..273
FT /note="ATG8 interaction motif (AIM)"
FT /evidence="ECO:0000250"
FT ACT_SITE 234
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1..7
FT /ligand="1,2-diacylglycero-3-phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:57613"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="N6-acetyllysine; by ESA1"
FT /evidence="ECO:0000250|UniProtKB:P40344"
FT MOD_RES 48
FT /note="N6-acetyllysine; by ESA1"
FT /evidence="ECO:0000250|UniProtKB:P40344"
SQ SEQUENCE 310 AA; 35887 MW; 52CCFB216B18CF0C CRC64;
MIRSTLSSWR EYLTPITHKS TFLTTGQITP EEFVQAGDYL CHMFPTWKWN EESSDISYRD
FLPKNKQFLI IRKVPCDKRA EQCVEVEGPD VIMKGFAEDG DEDDVLEYIG SETEHVQSTP
AGGTKDSSID DIDELIQDME IKEEDENDDT EEFNAKGGLA KDMAQERYYD LYIAYSTSYR
VPKMYIVGFN SNGSPLSPEQ MFEDISADYR TKTATIEKLP FYKNSVLSVS IHPCKHANVM
KILLDKVRVV RQRRRKELQE EQELDGVGDW EDLQDDIDDS LRVDQYLIVF LKFITSVTPS
IQHDYTMEGW
