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 13-NOV-2013, entry version 45. 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 cytoplasm to vacuole CC transport (Cvt) vesicles and autophagosomes formation. With atg4, CC mediates the delivery of the vesicles and autophagosomes to the CC vacuole via the microtubule cytoskeleton. Required for selective CC autophagic degradation of the nucleus (nucleophagy) as well as for CC mitophagy which contributes to regulate mitochondrial quantity and CC quality by eliminating the mitochondria to a basal level to CC fulfill cellular energy requirements and preventing excess ROS CC production. Participates also in membrane fusion events that take CC place in the early secretory pathway. Also involved in endoplasmic CC reticulum-specific autophagic process and is essential for the CC survival of cells subjected to severe ER stress. The atg8-PE CC 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. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, cvt vesicle membrane; CC Lipid-anchor (By similarity). Cytoplasmic vesicle, autophagosome CC membrane; Lipid-anchor (By similarity). Vacuole membrane; Lipid- CC anchor (By similarity). 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 (By similarity). CC -!- SIMILARITY: Belongs to the ATG8 family. 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 SMR; A2QPN1; 1-113. DR STRING; 5061.CADANGAP00006155; -. DR EnsemblFungi; CADANGAT00006276; CADANGAP00006155; CADANGAG00006276. DR GeneID; 4982271; -. DR KEGG; ang:ANI_1_1284064; -. DR eggNOG; NOG249730; -. DR HOGENOM; HOG000232034; -. DR KO; K08341; -. DR OrthoDB; EOG7712KX; -. DR GO; GO:0000421; C:autophagic vacuole membrane; IEA:UniProtKB-SubCell. DR GO; GO:0033110; C:Cvt vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi. DR GO; GO:0019898; C:extrinsic to membrane; IEA:EnsemblFungi. DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi. DR GO; GO:0000407; C:pre-autophagosomal structure; IEA:EnsemblFungi. DR GO; GO:0043936; P:asexual sporulation resulting in formation of a cellular spore; IMP:ASPGD. DR GO; GO:0000045; P:autophagic vacuole assembly; IEA:EnsemblFungi. DR GO; GO:0006914; P:autophagy; IMP:ASPGD. DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:ASPGD. DR GO; GO:0032258; P:CVT pathway; IEA:EnsemblFungi. DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IEA:EnsemblFungi. DR GO; GO:0000422; P:mitochondrion degradation; IEA:EnsemblFungi. DR GO; GO:0034727; P:piecemeal microautophagy of nucleus; IEA:EnsemblFungi. DR InterPro; IPR004241; Atg8_fam. DR PANTHER; PTHR10969; PTHR10969; 1. DR Pfam; PF02991; Atg8; 1. PE 3: Inferred from homology; KW Autophagy; Complete proteome; Cytoplasmic vesicle; Lipoprotein; KW Membrane; Protein transport; Transport; Ubl conjugation pathway; KW Vacuole. FT CHAIN 1 116 Autophagy-related protein 8. FT /FTId=PRO_0000317876. FT PROPEP 117 118 Removed in mature form (By similarity). FT /FTId=PRO_0000317877. FT SITE 116 117 Cleavage; by atg4 (By similarity). FT LIPID 116 116 Phosphatidylethanolamine amidated glycine FT (By similarity). SQ SEQUENCE 118 AA; 13738 MW; 85E8807255E14793 CRC64; MRSKFKDEHP FEKRKAEAER IRQKYADRIP VICEKVEKSD IATIDKKKYL VPADLTVGQF VYVIRKRIKL SPEKAIFIFV DEVLPPTAAL MSSIYEEHKD EDGFLYITYS GENTFGDC //