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 29-MAY-2024, entry version 85. 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 ATCC MYA-4892 / 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=ATCC MYA-4892 / CBS 513.88 / FGSC A1513; 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}. 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; AM270155; CAK45131.1; -; Genomic_DNA. DR RefSeq; XP_001392077.1; XM_001392040.2. DR AlphaFoldDB; A2QPN1; -. DR SMR; A2QPN1; -. DR EnsemblFungi; CAK45131; CAK45131; An07g10020. DR GeneID; 4982271; -. DR KEGG; ang:An07g10020; -. DR VEuPathDB; FungiDB:An07g10020; -. DR HOGENOM; CLU_119276_0_1_1; -. DR OrthoDB; 652940at2759; -. 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:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:TreeGrafter. DR GO; GO:0008429; F:phosphatidylethanolamine binding; IEA:TreeGrafter. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:TreeGrafter. DR GO; GO:0043936; P:asexual sporulation resulting in formation of a cellular spore; IMP:AspGD. DR GO; GO:0000045; P:autophagosome assembly; IEA:TreeGrafter. DR GO; GO:0006914; P:autophagy; IMP:AspGD. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IEA:TreeGrafter. DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:AspGD. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. 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_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 //