ID   ATG8_GLOLA              Reviewed;         121 AA.
AC   C4B4E4;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Autophagy-related protein 8 {ECO:0000303|PubMed:19363139};
DE   AltName: Full=Autophagy-related ubiquitin-like modifier ATG8 {ECO:0000250|UniProtKB:P38182};
DE   Flags: Precursor;
GN   Name=ATG8 {ECO:0000303|PubMed:19363139};
OS   Glomerella lagenarium (Anthracnose fungus) (Colletotrichum lagenarium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX   NCBI_TaxID=5462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=19363139; DOI=10.1105/tpc.108.060996;
RA   Asakura M., Ninomiya S., Sugimoto M., Oku M., Yamashita S., Okuno T.,
RA   Sakai Y., Takano Y.;
RT   "Atg26-mediated pexophagy is required for host invasion by the plant
RT   pathogenic fungus Colletotrichum orbiculare.";
RL   Plant Cell 21:1291-1304(2009).
CC   -!- FUNCTION: Ubiquitin-like modifier involved in cytoplasm to vacuole
CC       transport (Cvt) vesicles and autophagosomes formation
CC       (PubMed:19363139). With ATG4, mediates the delivery of the vesicles and
CC       autophagosomes to the vacuole via the microtubule cytoskeleton (By
CC       similarity). Required for selective autophagic degradation of the
CC       nucleus (nucleophagy) as well as for mitophagy which contributes to
CC       regulate mitochondrial quantity and quality by eliminating the
CC       mitochondria to a basal level to fulfill cellular energy requirements
CC       and preventing excess ROS production (By similarity). Participates also
CC       in membrane fusion events that take place in the early secretory
CC       pathway (By similarity). Also involved in endoplasmic reticulum-
CC       specific autophagic process and is essential for the survival of cells
CC       subjected to severe ER stress (By similarity). The ATG8-PE conjugate
CC       mediates tethering between adjacent membranes and stimulates membrane
CC       hemifusion, leading to expansion of the autophagosomal membrane during
CC       autophagy (By similarity). Moreover not only conjugation, but also
CC       subsequent ATG8-PE deconjugation is an important step required to
CC       facilitate multiple events during macroautophagy, and especially for
CC       efficient autophagosome biogenesis, the assembly of ATG9-containing
CC       tubulovesicular clusters into phagophores/autophagosomes, and for the
CC       disassembly of PAS-associated ATG components (By similarity).
CC       Contributes to normal formation of appressoria in the earlier steps of
CC       morphogenesis and to pathogenicity (PubMed:19363139).
CC       {ECO:0000250|UniProtKB:P38182, ECO:0000269|PubMed:19363139}.
CC   -!- SUBUNIT: Conjugation to phosphatidylethanolamine (PE) leads to
CC       homodimerization (By similarity). Interacts with ATG1, ATG3, ATG4, ATG7
CC       and ATG12 (By similarity). {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:0000269|PubMed:19363139}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P38182}. Vacuole membrane
CC       {ECO:0000269|PubMed:19363139}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P38182}. Note=Membrane-associated through a
CC       lipid anchor (By similarity). This association needs the 2 ubiquitin-
CC       like systems required for cytoplasm to vacuole transport and autophagy
CC       (By similarity). Localizes to both the isolation membrane (IM) and the
CC       vacuole-isolation membrane contact site (VICS) during IM expansion (By
CC       similarity). The IM is a membrane sac generated from the pre-
CC       autophagosomal structure that ultimately expands to become a mature
CC       autophagosome (By similarity). {ECO:0000250|UniProtKB:P38182}.
CC   -!- PTM: The C-terminal 5 residues of ATG8 are removed by ATG4 to expose
CC       Gly-116 at the C-terminus (By similarity). This Gly-116 forms then a
CC       thioester bond with ATG7 (E1-like activating enzyme) before being
CC       transferred to ATG3 (the specific E2 conjugating enzyme), in order to
CC       be finally amidated with phosphatidylethanolamine (By similarity). This
CC       lipid modification anchors ATG8 to membranes and can be reversed by
CC       ATG4, releasing soluble ATG8 (By similarity).
CC       {ECO:0000250|UniProtKB:P38182}.
CC   -!- DISRUPTION PHENOTYPE: Exhibits slightly reduced growth on nutrient-rich
CC       medium, and displays a severe reduction in conidiation
CC       (PubMed:19363139). Leads to the loss of pathogenicity on cucumber
CC       cotyledons (PubMed:19363139). Is defective in the early stages of
CC       infection-related morphogenesis, such as in germination
CC       (PubMed:19363139). {ECO:0000269|PubMed:19363139}.
CC   -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR   EMBL; AB365480; BAH60888.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4B4E4; -.
DR   SMR; C4B4E4; -.
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; Vacuole.
FT   CHAIN           1..121
FT                   /note="Autophagy-related protein 8"
FT                   /id="PRO_0000443895"
FT   PROPEP          117..121
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
FT                   /id="PRO_0000443896"
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   121 AA;  14041 MW;  C0609DBCE3AE1246 CRC64;
     MRSKFKDEHP FEKRKAEAER IRQKYSDRIP VICEKVEKSD IATIDKKKYL VPADLTVGQF
     VYVIRKRIKL SPEKAIFIFV DEVLPPTAAL MSSIYEEHKD EDGFLYITYS GENTFGGFET
     A