ATG8_PHANO
ID ATG8_PHANO Reviewed; 119 AA.
AC Q0V3Y9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Autophagy-related protein 8;
DE AltName: Full=Autophagy-related ubiquitin-like modifier ATG8;
DE Flags: Precursor;
GN Name=ATG8; ORFNames=SNOG_01275;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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 3 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; CH445326; EAT90924.1; -; Genomic_DNA.
DR RefSeq; XP_001791921.1; XM_001791869.1.
DR AlphaFoldDB; Q0V3Y9; -.
DR SMR; Q0V3Y9; -.
DR STRING; 13684.SNOT_01275; -.
DR EnsemblFungi; SNOT_01275; SNOT_01275; SNOG_01275.
DR GeneID; 5968766; -.
DR KEGG; pno:SNOG_01275; -.
DR eggNOG; KOG1654; Eukaryota.
DR HOGENOM; CLU_119276_0_1_1; -.
DR InParanoid; Q0V3Y9; -.
DR OMA; AVYQEHK; -.
DR OrthoDB; 1508198at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IBA:GO_Central.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
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 Reference proteome; Transport; Ubl conjugation pathway; Vacuole.
FT CHAIN 1..116
FT /note="Autophagy-related protein 8"
FT /id="PRO_0000317896"
FT PROPEP 117..119
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P38182"
FT /id="PRO_0000317897"
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 119 AA; 13876 MW; 38F61030E25A1E48 CRC64;
MRSKFKDEHP FEKRKAEAER IRQKYNDRIP VICEKVEKSD IATIDKKKYL VPADLTVGQF
VYVIRKRIKL SPEKAIFIFV DEVLPPTAAL MSSIYEEHKD EDGFLYITYS GENTFGEAI