ID ATG8_CANGA Reviewed; 118 AA.
AC Q6FXR8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=Autophagy-related protein 8;
DE AltName: Full=Autophagy-related ubiquitin-like modifier ATG8;
DE Flags: Precursor;
GN Name=ATG8; Synonyms=AUT7; OrderedLocusNames=CAGL0A04675g;
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 2 residues are removed to expose Gly-116 at the C-
CC 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; CR380947; CAG57864.1; -; Genomic_DNA.
DR RefSeq; XP_444971.1; XM_444971.1.
DR AlphaFoldDB; Q6FXR8; -.
DR SMR; Q6FXR8; -.
DR STRING; 284593.Q6FXR8; -.
DR EnsemblFungi; CAGL0A04675g-T; CAGL0A04675g-T-p1; CAGL0A04675g.
DR GeneID; 2886410; -.
DR KEGG; cgr:CAGL0A04675g; -.
DR CGD; CAL0126897; CAGL0A04675g.
DR VEuPathDB; FungiDB:B1J91_A04675g; -.
DR VEuPathDB; FungiDB:CAGL0A04675g; -.
DR eggNOG; KOG1654; Eukaryota.
DR HOGENOM; CLU_119276_0_1_1; -.
DR InParanoid; Q6FXR8; -.
DR OMA; AVYQEHK; -.
DR Proteomes; UP000002428; Chromosome A.
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; IEA:EnsemblFungi.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:EnsemblFungi.
DR GO; GO:0000407; C:phagophore assembly site; IEA:EnsemblFungi.
DR GO; GO:0120095; C:vacuole-isolation membrane contact site; IEA:EnsemblFungi.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IEA:EnsemblFungi.
DR GO; GO:0031386; F:protein tag activity; IEA:EnsemblFungi.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR GO; GO:0061025; P:membrane fusion; IEA:EnsemblFungi.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IEA:EnsemblFungi.
DR GO; GO:0071211; P:protein targeting to vacuole involved in autophagy; IEA:EnsemblFungi.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0031503; P:protein-containing complex localization; IEA:EnsemblFungi.
DR GO; GO:0016241; P:regulation of macroautophagy; IEA:EnsemblFungi.
DR GO; GO:1905153; P:regulation of membrane invagination; IEA:EnsemblFungi.
DR GO; GO:0061709; P:reticulophagy; IEA:EnsemblFungi.
DR CDD; cd16128; Ubl_ATG8; 1.
DR InterPro; IPR004241; Atg8-like.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10969:SF4; GAMMA-AMINOBUTYRIC ACID RECEPTOR-ASSOCIATED PROTEIN-LIKE 2; 1.
DR PANTHER; PTHR10969; MICROTUBULE-ASSOCIATED PROTEINS 1A/1B LIGHT CHAIN 3-RELATED; 1.
DR Pfam; PF02991; ATG8; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 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_0000017212"
FT PROPEP 117..118
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P38182"
FT /id="PRO_0000017213"
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 118 AA; 13795 MW; 9684FF0B6C08D450 CRC64;
MKSSFKSEYP FEKRKAESER ISEKFQNRIP VICEKAEKSD IPEVDKRKYL VPADLTVGQF
VYVIRKRIML PPEKAIFIFV NDTLPPTASL MSQVYQEHKD KDGFLYVTYS GENTFGYQ
//
