ID   ATG8_SCLS1              Reviewed;         123 AA.
AC   A7E8H4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, 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   Flags: Precursor;
GN   Name=atg8; ORFNames=SS1G_01602;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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 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; CH476622; EDN96676.1; -; Genomic_DNA.
DR   RefSeq; XP_001597408.1; XM_001597358.1.
DR   AlphaFoldDB; A7E8H4; -.
DR   SMR; A7E8H4; -.
DR   STRING; 665079.A7E8H4; -.
DR   EnsemblFungi; EDN96676; EDN96676; SS1G_01602.
DR   GeneID; 5493212; -.
DR   KEGG; ssl:SS1G_01602; -.
DR   VEuPathDB; FungiDB:sscle_01g007550; -.
DR   eggNOG; KOG1654; Eukaryota.
DR   HOGENOM; CLU_119276_0_1_1; -.
DR   InParanoid; A7E8H4; -.
DR   OMA; AVYQEHK; -.
DR   Proteomes; UP000001312; 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_0000317900"
FT   PROPEP          117..123
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
FT                   /id="PRO_0000317901"
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   123 AA;  14294 MW;  86021A602188E8B0 CRC64;
     MRSKFKDEHP FEKRKAEAER IRQKYSDRIP VICEKVEKSD IATIDKKKYL VPSDLTVGQF
     VYVIRKRIKL SPEKAIFIFV DEVLPPTAAL MSSIYEEHKD EDGFLYISYS GENTFGEALE
     EAN