ATG8_ASPNC
ID ATG8_ASPNC Reviewed; 118 AA.
AC A2QPN1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Autophagy-related protein 8;
DE AltName: Full=Autophagy-related ubiquitin-like modifier atg8;
DE Flags: Precursor;
GN Name=atg8; ORFNames=An07g10020;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP FUNCTION.
RX PubMed=23700238; DOI=10.1007/s00253-013-4971-1;
RA Nitsche B.M., Burggraaf-van Welzen A.M., Lamers G., Meyer V., Ram A.F.;
RT "Autophagy promotes survival in aging submerged cultures of the filamentous
RT fungus Aspergillus niger.";
RL Appl. Microbiol. Biotechnol. 97:8205-8218(2013).
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 (By similarity). Besides
CC its function in nutrient recycling, autophagy plays important roles in
CC physiological adaptation by organelle turnover (such as mitochondrial
CC turnover) and protection against cell death upon carbon depletion in
CC submerged cultures (PubMed:23700238). {ECO:0000250|UniProtKB:P38182,
CC ECO:0000269|PubMed:23700238}.
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 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; AM270155; CAK45131.1; -; Genomic_DNA.
DR RefSeq; XP_001392077.1; XM_001392040.2.
DR AlphaFoldDB; A2QPN1; -.
DR SMR; A2QPN1; -.
DR PaxDb; A2QPN1; -.
DR EnsemblFungi; CAK45131; CAK45131; An07g10020.
DR GeneID; 4982271; -.
DR KEGG; ang:ANI_1_1284064; -.
DR VEuPathDB; FungiDB:An07g10020; -.
DR HOGENOM; CLU_119276_0_1_1; -.
DR Proteomes; UP000006706; Chromosome 4L.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0043936; P:asexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0006914; P:autophagy; IMP:AspGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:AspGD.
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_0000317876"
FT PROPEP 117..118
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P38182"
FT /id="PRO_0000317877"
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; 13738 MW; 85E8807255E14793 CRC64;
MRSKFKDEHP FEKRKAEAER IRQKYADRIP VICEKVEKSD IATIDKKKYL VPADLTVGQF
VYVIRKRIKL SPEKAIFIFV DEVLPPTAAL MSSIYEEHKD EDGFLYITYS GENTFGDC
