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 30-NOV-2016, entry version 63. 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. OX NCBI_TaxID=425011; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=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., RA Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., RA Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., RA Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M., RA Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., RA van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., RA Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., RA 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., RA van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., RA van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., RA Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., RA Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., RA Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., RA Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., RA Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.; RT "Genome sequencing and analysis of the versatile cell factory RT Aspergillus 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., RA Ram A.F.; RT "Autophagy promotes survival in aging submerged cultures of the RT filamentous fungus Aspergillus niger."; RL Appl. Microbiol. Biotechnol. 97:8205-8218(2013). CC -!- FUNCTION: Ubiquitin-like modifier involved in autophagosomes CC formation. With atg4, mediates the delivery of the autophagosomes CC to the vacuole via the microtubule cytoskeleton. Required for CC selective autophagic degradation of the nucleus (nucleophagy) as CC well as for mitophagy which contributes to regulate mitochondrial CC quantity and quality by eliminating the mitochondria to a basal CC level to fulfill cellular energy requirements and preventing CC excess ROS production. Participates also in membrane fusion events CC that take place in the early secretory pathway. Also involved in CC endoplasmic reticulum-specific autophagic process and is essential CC for the survival of cells subjected to severe ER stress. The atg8- CC PE conjugate mediates tethering between adjacent membranes and CC stimulates membrane hemifusion, leading to expansion of the CC autophagosomal membrane during autophagy (By similarity). Besides CC its function in nutrient recycling, autophagy plays important CC roles in physiological adaptation by organelle turnover (such as CC mitochondrial turnover) and protection against cell death upon CC carbon depletion in submerged cultures (PubMed:23700238). CC {ECO:0000250|UniProtKB:P38182, 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- CC 116 at the C-terminus. The c-terminal Gly is then amidated with CC phosphatidylethanolamine by an activating system similar to that CC for 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 ProteinModelPortal; A2QPN1; -. DR EnsemblFungi; CAK45131; CAK45131; An07g10020. DR GeneID; 4982271; -. DR KEGG; ang:ANI_1_1284064; -. DR HOGENOM; HOG000232034; -. DR KO; K08341; -. DR OrthoDB; EOG092C5HB8; -. 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 CDD; cd01611; GABARAP; 1. DR InterPro; IPR004241; Atg8-like. DR InterPro; IPR029071; Ubiquitin-rel_dom. DR PANTHER; PTHR10969; PTHR10969; 1. DR Pfam; PF02991; Atg8; 1. DR SUPFAM; SSF54236; SSF54236; 1. PE 3: Inferred from homology; KW Autophagy; Complete proteome; Cytoplasmic vesicle; Lipoprotein; KW Membrane; Protein transport; Reference proteome; Transport; KW Ubl conjugation pathway; Vacuole. FT CHAIN 1 116 Autophagy-related protein 8. FT /FTId=PRO_0000317876. FT PROPEP 117 118 Removed in mature form. FT {ECO:0000250|UniProtKB:P38182}. FT /FTId=PRO_0000317877. FT SITE 116 117 Cleavage; by atg4. FT {ECO:0000250|UniProtKB:P38182}. FT LIPID 116 116 Phosphatidylethanolamine amidated FT glycine. {ECO:0000250|UniProtKB:P38182}. SQ SEQUENCE 118 AA; 13738 MW; 85E8807255E14793 CRC64; MRSKFKDEHP FEKRKAEAER IRQKYADRIP VICEKVEKSD IATIDKKKYL VPADLTVGQF VYVIRKRIKL SPEKAIFIFV DEVLPPTAAL MSSIYEEHKD EDGFLYITYS GENTFGDC //