ATG8_YEAS7
ID ATG8_YEAS7 Reviewed; 117 AA.
AC A6ZKM4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Autophagy-related protein 8;
DE AltName: Full=Autophagy-related ubiquitin-like modifier ATG8;
DE AltName: Full=Cytoplasm to vacuole targeting protein 5;
DE Flags: Precursor;
GN Name=ATG8; Synonyms=APG8, AUT7, CVT5; ORFNames=SCY_0144;
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: Ubiquitin-like modifier involved in cytoplasm to vacuole
CC transport (Cvt) vesicles and autophagosomes formation. With ATG4,
CC mediates the delivery of the vesicles and autophagosomes to the vacuole
CC via the microtubule cytoskeleton. 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. Participates
CC also in membrane fusion events that take place in the early secretory
CC pathway. Also involved in endoplasmic reticulum-specific autophagic
CC process and is essential for the survival of cells subjected to severe
CC ER stress. The ATG8-PE conjugate mediates tethering between adjacent
CC membranes and stimulates membrane hemifusion, leading to expansion of
CC the autophagosomal membrane during autophagy. Moreover not only
CC conjugation, but also subsequent ATG8-PE deconjugation is an important
CC step required to facilitate multiple events during macroautophagy, and
CC especially for efficient autophagosome biogenesis, the assembly of
CC ATG9-containing tubulovesicular clusters into
CC phagophores/autophagosomes, and for the disassembly of PAS-associated
CC ATG components. Also plays a role in regulation of filamentous growth.
CC {ECO:0000250|UniProtKB:P38182}.
CC -!- SUBUNIT: Conjugation to phosphatidylethanolamine (PE) leads to
CC homodimerization. Interacts with ATG1, ATG3, ATG4, ATG7, ATG12, ATG32,
CC ATG34 and the C-terminal 10 residues domain of ATG19. Interacts also
CC with the endoplasmic reticulum to Golgi v-SNARE protein BET1 and the
CC vacuolar v-SNARE protein NYV1. Interacts with the UBX domain-containing
CC protein SHP1. {ECO:0000250|UniProtKB:P38182}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, cvt vesicle membrane
CC {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P38182}. Cytoplasmic vesicle, autophagosome
CC membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P38182}. Vacuole membrane
CC {ECO:0000250|UniProtKB:P38182}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P38182}. Note=Membrane-associated through a
CC lipid anchor. This association needs the 2 ubiquitin-like systems
CC required for cytoplasm to vacuole transport and autophagy. ATG18 and
CC ATG21 facilitate the recruitment of ATG8-PE to the site of
CC autophagosome formation and protect it from premature cleavage by ATG4.
CC Localizes to both the isolation membrane (IM) and the vacuole-isolation
CC membrane contact site (VICS) during IM expansion. The IM is a membrane
CC sac generated from the pre-autophagosomal structure that ultimately
CC expands to become a mature autophagosome. Upon starvation, is also
CC recruited to into unique membrane structures near SEC13-containing ER
CC exit sites which lack components of the Golgi apparatus and the
CC endosomes, and which were called a compartments for unconventional
CC protein secretion (CUPS). {ECO:0000250|UniProtKB:P38182}.
CC -!- PTM: The C-terminal Arg-117 residue of ATG8 is removed by ATG4 to
CC expose Gly-116 at the C-terminus. This Gly-116 forms then a thioester
CC bond with the 'Cys-507' of ATG7 (E1-like activating enzyme) before
CC being transferred to the 'Cys-234' of ATG3 (the specific E2 conjugating
CC enzyme), in order to be finally amidated with phosphatidylethanolamine.
CC This lipid modification anchors ATG8 to membranes and can be reversed
CC by ATG4, releasing soluble ATG8. {ECO:0000250|UniProtKB:P38182}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR EMBL; AAFW02000011; EDN64543.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZKM4; -.
DR BMRB; A6ZKM4; -.
DR SMR; A6ZKM4; -.
DR EnsemblFungi; EDN64543; EDN64543; SCY_0144.
DR HOGENOM; CLU_119276_0_1_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033110; C:Cvt vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR004241; Atg8-like.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10969; PTHR10969; 1.
DR Pfam; PF02991; ATG8; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasmic vesicle; Lipoprotein; Membrane; Protein transport;
KW Transport; Ubl conjugation pathway; Vacuole.
FT CHAIN 1..116
FT /note="Autophagy-related protein 8"
FT /id="PRO_0000317904"
FT PROPEP 117
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P38182"
FT /id="PRO_0000317905"
FT SITE 116..117
FT /note="Cleavage; by ATG4"
FT /evidence="ECO:0000250|UniProtKB:P38182"
FT LIPID 116
FT /note="Phosphatidylethanolamine amidated glycine"
FT /evidence="ECO:0000250|UniProtKB:P38182"
SQ SEQUENCE 117 AA; 13627 MW; 1246CEFF5A038819 CRC64;
MKSTFKSEYP FEKRKAESER IADRFKNRIP VICEKAEKSD IPEIDKRKYL VPADLTVGQF
VYVIRKRIML PPEKAIFIFV NDTLPPTAAL MSAIYQEHKD KDGFLYVTYS GENTFGR
