ATG8_MAGO7
ID ATG8_MAGO7 Reviewed; 123 AA.
AC Q51MW4; A4RD89; G4NCJ6;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Autophagy-related protein 8 {ECO:0000303|PubMed:19923912};
DE AltName: Full=Autophagy-related ubiquitin-like modifier ATG8 {ECO:0000303|PubMed:19923912};
DE Flags: Precursor;
GN Name=ATG8 {ECO:0000303|PubMed:19923912}; ORFNames=MGG_01062;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP INTERACTION WITH ATG4, AND CLEAVAGE BY ATG4.
RX PubMed=19923912; DOI=10.4161/auto.6.1.10438;
RA Liu T.B., Liu X.H., Lu J.P., Zhang L., Min H., Lin F.C.;
RT "The cysteine protease MoAtg4 interacts with MoAtg8 and is required for
RT differentiation and pathogenesis in Magnaporthe oryzae.";
RL Autophagy 6:74-85(2010).
RN [3]
RP INTERACTION WITH ATG3.
RX PubMed=30776962; DOI=10.1080/15548627.2019.1580104;
RA Yin Z., Chen C., Yang J., Feng W., Liu X., Zuo R., Wang J., Yang L.,
RA Zhong K., Gao C., Zhang H., Zheng X., Wang P., Zhang Z.;
RT "Histone acetyltransferase MoHat1 acetylates autophagy-related proteins
RT MoAtg3 and MoAtg9 to orchestrate functional appressorium formation and
RT pathogenicity in Magnaporthe oryzae.";
RL Autophagy 15:1234-1257(2019).
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 -!- SUBUNIT: Interacts with ATG4, (PubMed:19923912). Interacts with
CC acetylated ATG3 (PubMed:30776962). {ECO:0000269|PubMed:19923912,
CC ECO:0000269|PubMed:30776962}.
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 7 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; CM001235; EHA48293.1; -; Genomic_DNA.
DR RefSeq; XP_003717877.1; XM_003717829.1.
DR AlphaFoldDB; Q51MW4; -.
DR SMR; Q51MW4; -.
DR STRING; 318829.MGG_01062T0; -.
DR EnsemblFungi; MGG_01062T0; MGG_01062T0; MGG_01062.
DR GeneID; 2674322; -.
DR KEGG; mgr:MGG_01062; -.
DR VEuPathDB; FungiDB:MGG_01062; -.
DR eggNOG; KOG1654; Eukaryota.
DR HOGENOM; CLU_119276_0_1_1; -.
DR InParanoid; Q51MW4; -.
DR OMA; AVYQEHK; -.
DR OrthoDB; 1508198at2759; -.
DR PHI-base; PHI:2061; -.
DR PHI-base; PHI:2076; -.
DR PHI-base; PHI:768; -.
DR Proteomes; UP000009058; Chromosome 5.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0075016; P:appressorium formation; IMP:PAMGO_MGG.
DR GO; GO:0048102; P:autophagic cell death; IMP:PAMGO_MGG.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:PAMGO_MGG.
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 1: Evidence at protein level;
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_0000017224"
FT PROPEP 117..123
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:19923912"
FT /id="PRO_0000017225"
FT SITE 116..117
FT /note="Cleavage; by ATG4"
FT /evidence="ECO:0000269|PubMed:19923912"
FT LIPID 116
FT /note="Phosphatidylethanolamine amidated glycine"
FT /evidence="ECO:0000250|UniProtKB:P38182"
SQ SEQUENCE 123 AA; 14397 MW; 6AAC5051F236152B CRC64;
MRSKFKDEHP FEKRKAEAER IRQKYTDRIP VICEKVEKSD IATIDKKKYL VPADLTVGQF
VYVIRKRIKL SPEKAIFIFV QDTLPPTAAL MSSIYELHKD EDGFLYITYS GENTFGDLFE
EVE
