ID   ATG8_COLLN              Reviewed;         121 AA.
AC   A4LA70;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Autophagy-related protein 8;
DE   AltName: Full=Autophagy-related ubiquitin-like modifier ATG8;
DE   Flags: Precursor;
GN   Name=ATG8;
OS   Colletotrichum lindemuthianum (Bean anthracnose fungus) (Glomerella
OS   lindemuthiana).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum orbiculare species complex.
OX   NCBI_TaxID=290576;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Charoin-Bard E., Lauge R., Langin T.;
RT   "Involvement of autophagy in the appressorium functionality of the fungal
RT   plant pathogen Colletotrichum lindemuthianum.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ubiquitin-like modifier involved in autophagosomes formation.
CC       With ATG4, mediates the delivery of the 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.
CC       {ECO:0000250|UniProtKB:P38182}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC       {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}.
CC   -!- PTM: The C-terminal 5 residues are removed by ATG4 to expose Gly-116 at
CC       the C-terminus. The c-terminal Gly is then amidated with
CC       phosphatidylethanolamine by an activating system similar to that for
CC       ubiquitin. {ECO:0000250|UniProtKB:P38182}.
CC   -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR   EMBL; EF467326; ABO46011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4LA70; -.
DR   SMR; A4LA70; -.
DR   GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
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_0000317888"
FT   PROPEP          117..121
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
FT                   /id="PRO_0000317889"
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