ID   ATG8_PICST              Reviewed;         139 AA.
AC   A3GFU8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Autophagy-related protein 8;
DE   AltName: Full=Autophagy-related ubiquitin-like modifier ATG8;
DE   Flags: Precursor;
GN   Name=ATG8; ORFNames=PICST_34219;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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 23 residues are removed by ATG4 to expose Gly-116
CC       at 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; AAVQ01000001; EAZ63823.1; -; Genomic_DNA.
DR   RefSeq; XP_001387846.1; XM_001387809.1.
DR   AlphaFoldDB; A3GFU8; -.
DR   SMR; A3GFU8; -.
DR   STRING; 4924.XP_001387846.1; -.
DR   EnsemblFungi; EAZ63823; EAZ63823; PICST_34219.
DR   GeneID; 4851147; -.
DR   KEGG; pic:PICST_34219; -.
DR   eggNOG; KOG1654; Eukaryota.
DR   HOGENOM; CLU_119276_0_1_1; -.
DR   InParanoid; A3GFU8; -.
DR   OMA; AVYQEHK; -.
DR   OrthoDB; 1508198at2759; -.
DR   Proteomes; UP000002258; Chromosome 1.
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   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_0000317898"
FT   PROPEP          117..139
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P38182"
FT                   /id="PRO_0000317899"
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   139 AA;  16148 MW;  0130A9A9D489980D CRC64;
     MRSQFKDEHP FEKRQAEATR IAQRFKDRVP VICEKVENSD IPEIDKRKYL VPVDLSVGQF
     VYVIRKRIKL PSEKAIFIFV NDILPPTAAL ISTIYEEHKD EDGFLYVLYS GENTFGQKKP
     LDLSTIDWSD LSDLDLAQK