ID   ATG8_PODAS              Reviewed;         121 AA.
AC   Q8J282;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Autophagy-related protein 8;
DE   AltName: Full=Autophagy-related ubiquitin-like modifier ATG8;
DE   AltName: Full=Induced during the incompatibility reaction protein 7;
DE   Flags: Precursor;
GN   Name=ATG8; Synonyms=idi-7;
OS   Podospora anserina (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX   NCBI_TaxID=2587412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12519185; DOI=10.1046/j.1365-2958.2003.03208.x;
RA   Pinan-Lucarre B., Paoletti M., Dementhon K., Coulary-Salin B., Clave C.;
RT   "Autophagy is induced during cell death by incompatibility and is essential
RT   for differentiation in the filamentous fungus Podospora anserina.";
RL   Mol. Microbiol. 47:321-333(2003).
RN   [2]
RP   INDUCTION.
RX   PubMed=15341644; DOI=10.1111/j.1365-2958.2004.04235.x;
RA   Dementhon K., Saupe S.J., Clave C.;
RT   "Characterization of IDI-4, a bZIP transcription factor inducing autophagy
RT   and cell death in the fungus Podospora anserina.";
RL   Mol. Microbiol. 53:1625-1640(2004).
RN   [3]
RP   SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16278443; DOI=10.1128/ec.4.11.1765-1774.2005;
RA   Pinan-Lucarre B., Balguerie A., Clave C.;
RT   "Accelerated cell death in Podospora autophagy mutants.";
RL   Eukaryot. Cell 4:1765-1774(2005).
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, ECO:0000269|PubMed:12519185}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC       {ECO:0000269|PubMed:16278443}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P38182}. Vacuole membrane
CC       {ECO:0000269|PubMed:12519185, ECO:0000269|PubMed:16278443}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:P38182}. Note=Punctate structures under
CC       nutrient-rich conditions and large punctate perivacuolar structures and
CC       vacuolar lumen under nitrogen starvation conditions or heterokaryon
CC       incompatibility conditions. {ECO:0000269|PubMed:12519185,
CC       ECO:0000269|PubMed:16278443}.
CC   -!- INDUCTION: Expression is positively regulated by idi-4.
CC       {ECO:0000269|PubMed:15341644}.
CC   -!- PTM: The C-terminal 5 residues may be removed to expose Gly-116 at the
CC       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   -!- DISRUPTION PHENOTYPE: Increases the rate of incompatibility cell death.
CC       {ECO:0000269|PubMed:16278443}.
CC   -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR   EMBL; AF502254; AAN41258.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8J282; -.
DR   SMR; Q8J282; -.
DR   VEuPathDB; FungiDB:PODANS_3_5250; -.
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   2: Evidence at transcript level;
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_0000017234"
FT   PROPEP          117..121
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
FT                   /id="PRO_0000017235"
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;  14025 MW;  EE197A229A507255 CRC64;
     MRSKFKDEHP FEKRKAEAER IRQKYADRIP VICEKVEKSD IATIDKKKYL VPADLTVGQF
     VYVIRKRIKL SPEKAIFIFV DEVLPPTAAL MSSIYEEHKD EDGFLYITYS GENTFGGFET
     A