ATG8_LACBI
ID ATG8_LACBI Reviewed; 184 AA.
AC P87068;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Autophagy-related protein 8;
DE AltName: Full=Autophagy-related ubiquitin-like modifier ATG8;
DE Flags: Precursor;
GN Name=ATG8; Synonyms=AUT7;
OS Laccaria bicolor (Bicoloured deceiver) (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomataceae; Laccaria.
OX NCBI_TaxID=29883;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=DR170;
RX PubMed=10074098; DOI=10.1128/jb.181.6.1963-1967.1999;
RA Kim S.-J., Bernreuther D., Thumm M., Podila G.K.;
RT "LB-AUT7, a novel symbiosis-regulated gene from an ectomycorrhizal fungus,
RT Laccaria bicolor, is functionally related to vesicular transport and
RT autophagocytosis.";
RL J. Bacteriol. 181:1963-1967(1999).
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 68 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB53650.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U93506; AAB53650.1; ALT_INIT; mRNA.
DR AlphaFoldDB; P87068; -.
DR SMR; P87068; -.
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 2: Evidence at transcript level;
KW Autophagy; Cytoplasmic vesicle; Lipoprotein; Membrane; Protein transport;
KW Transport; Ubl conjugation pathway; Vacuole.
FT CHAIN 1..116
FT /note="Autophagy-related protein 8"
FT /id="PRO_0000017222"
FT PROPEP 117..184
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P38182"
FT /id="PRO_0000017223"
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 184 AA; 21326 MW; ED36B9F498F13A5A CRC64;
MRSKFKDEHP FEKRKAEAER IRQKYPDRIP VICEKADRTD IPTIDKKKYL VPSDLTVGQF
VYVIRKRIKL APEKAIFIFV DEVLPPTAAL MSAIYEEHKD EDNFLYVSYS GENTFGQEGW
VELPVDDMDK AFICVSAAKK HWVWVLCDVR SSYQNCVLIV PLVQRPVLHT HSSFLSVSFA
LLFV