ID ATG8_YEAST Reviewed; 117 AA. AC P38182; D6VPS5; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 04-NOV-2026, entry version 213. DE RecName: Full=Autophagy-related protein 8; DE AltName: Full=Autophagy-related ubiquitin-like modifier ATG8; DE AltName: Full=Cytoplasm to vacuole targeting protein 5; DE Flags: Precursor; GN Name=ATG8; Synonyms=APG8, AUT7, CVT5; OrderedLocusNames=YBL078C; GN ORFNames=YBL0732; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7502586; DOI=10.1002/yea.320111112; RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.; RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces RT cerevisiae chromosome II."; RL Yeast 11:1103-1112(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP FUNCTION. RX PubMed=8224160; DOI=10.1016/0014-5793(93)80398-e; RA Tsukada M., Ohsumi Y.; RT "Isolation and characterization of autophagy-defective mutants of RT Saccharomyces cerevisiae."; RL FEBS Lett. 333:169-174(1993). RN [6] RP FUNCTION. RX PubMed=7593182; DOI=10.1083/jcb.131.3.591; RA Harding T.M., Morano K.A., Scott S.V., Klionsky D.J.; RT "Isolation and characterization of yeast mutants in the cytoplasm to RT vacuole protein targeting pathway."; RL J. Cell Biol. 131:591-602(1995). RN [7] RP FUNCTION, INTERACTION WITH ATG4, AND SUBCELLULAR LOCATION. RX PubMed=9649430; DOI=10.1093/emboj/17.13.3597; RA Lang T., Schaeffeler E., Bernreuther D., Bredschneider M., Wolf D.H., RA Thumm M.; RT "Aut2p and Aut7p, two novel microtubule-associated proteins are essential RT for delivery of autophagic vesicles to the vacuole."; RL EMBO J. 17:3597-3607(1998). RN [8] RP FUNCTION. RX PubMed=10525546; DOI=10.1083/jcb.147.2.435; RA Kirisako T., Baba M., Ishihara N., Miyazawa K., Ohsumi M., Yoshimori T., RA Noda T., Ohsumi Y.; RT "Formation process of autophagosome is traced with Apg8/Aut7p in yeast."; RL J. Cell Biol. 147:435-446(1999). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10681575; DOI=10.1074/jbc.275.8.5845; RA Huang W.-P., Scott S.V., Kim J., Klionsky D.J.; RT "The itinerary of a vesicle component, Aut7p/Cvt5p, terminates in the yeast RT vacuole via the autophagy/Cvt pathways."; RL J. Biol. Chem. 275:5845-5851(2000). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BET1 AND NYV1. RX PubMed=10837468; DOI=10.1074/jbc.m000917200; RA Legesse-Miller A., Sagiv Y., Glozman R., Elazar Z.; RT "Aut7p, a soluble autophagic factor, participates in multiple membrane RT trafficking processes."; RL J. Biol. Chem. 275:32966-32973(2000). RN [11] RP FUNCTION, CLEAVAGE BY ATG4, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP GLY-116 AND ARG-117. RX PubMed=11038174; DOI=10.1083/jcb.151.2.263; RA Kirisako T., Ichimura Y., Okada H., Kabeya Y., Mizushima N., Yoshimori T., RA Ohsumi M., Takao T., Noda T., Ohsumi Y.; RT "The reversible modification regulates the membrane-binding state of RT Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting RT pathway."; RL J. Cell Biol. 151:263-276(2000). RN [12] RP FUNCTION, INTERACTION WITH ATG3 AND ATG7, AND LIPIDATION AT GLY-116. RX PubMed=11100732; DOI=10.1038/35044114; RA Ichimura Y., Kirisako T., Takao T., Satomi Y., Shimonishi Y., Ishihara N., RA Mizushima N., Tanida I., Kominami E., Ohsumi M., Noda T., Ohsumi Y.; RT "A ubiquitin-like system mediates protein lipidation."; RL Nature 408:488-492(2000). RN [13] RP SUBCELLULAR LOCATION. RX PubMed=11689437; DOI=10.1093/emboj/20.21.5971; RA Suzuki K., Kirisako T., Kamada Y., Mizushima N., Noda T., Ohsumi Y.; RT "The pre-autophagosomal structure organized by concerted functions of APG RT genes is essential for autophagosome formation."; RL EMBO J. 20:5971-5981(2001). RN [14] RP INTERACTION WITH ATG7. RX PubMed=11139573; DOI=10.1074/jbc.m007737200; RA Komatsu M., Tanida I., Ueno T., Ohsumi M., Ohsumi Y., Kominami E.; RT "The C-terminal region of an Apg7p/Cvt2p is required for homodimerization RT and is essential for its E1 activity and E1-E2 complex formation."; RL J. Biol. Chem. 276:9846-9854(2001). RN [15] RP FUNCTION, CLEAVAGE BY ATG4, AND SUBCELLULAR LOCATION. RX PubMed=11149920; DOI=10.1083/jcb.152.1.51; RA Kim J., Huang W.-P., Klionsky D.J.; RT "Membrane recruitment of Aut7p in the autophagy and cytoplasm to vacuole RT targeting pathways requires Aut1p, Aut2p, and the autophagy conjugation RT complex."; RL J. Cell Biol. 152:51-64(2001). RN [16] RP INTERACTION WITH ATG19. RX PubMed=12479808; DOI=10.1016/s1534-5807(02)00373-8; RA Shintani T., Huang W.-P., Stromhaug P.E., Klionsky D.J.; RT "Mechanism of cargo selection in the cytoplasm to vacuole targeting RT pathway."; RL Dev. Cell 3:825-837(2002). RN [17] RP SUBCELLULAR LOCATION, AND INTERACTION WITH ATG12 AND ATG19. RX PubMed=11675395; DOI=10.1074/jbc.m109134200; RA Kim J., Huang W.-P., Stromhaug P.E., Klionsky D.J.; RT "Convergence of multiple autophagy and cytoplasm to vacuole targeting RT components to a perivacuolar membrane compartment prior to de novo vesicle RT formation."; RL J. Biol. Chem. 277:763-773(2002). RN [18] RP NOMENCLATURE. RX PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x; RA Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y., RA Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.; RT "A unified nomenclature for yeast autophagy-related genes."; RL Dev. Cell 5:539-545(2003). RN [19] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [20] RP CONJUGATION TO PHOSPHATIDYLETHANOLAMINE, AND SUBCELLULAR LOCATION. RX PubMed=15194695; DOI=10.1074/jbc.m401066200; RA Meiling-Wesse K., Barth H., Voss C., Eskelinen E.-L., Epple U.D., Thumm M.; RT "Atg21 is required for effective recruitment of Atg8 to the RT preautophagosomal structure during the Cvt pathway."; RL J. Biol. Chem. 279:37741-37750(2004). RN [21] RP CONJUGATION TO PHOSPHATIDYLETHANOLAMINE. RX PubMed=15277523; DOI=10.1074/jbc.m405860200; RA Ichimura Y., Imamura Y., Emoto K., Umeda M., Noda T., Ohsumi Y.; RT "In vivo and in vitro reconstitution of atg8 conjugation essential for RT autophagy."; RL J. Biol. Chem. 279:40584-40592(2004). RN [22] RP INTERACTION WITH ATG3, AND CONJUGATION TO PHOSPHATIDYLETHANOLAMINE. RX PubMed=20615880; DOI=10.1074/jbc.m110.113670; RA Yamaguchi M., Noda N.N., Nakatogawa H., Kumeta H., Ohsumi Y., Inagaki F.; RT "Autophagy-related protein 8 (Atg8) family interacting motif in Atg3 RT mediates the Atg3-Atg8 interaction and is crucial for the cytoplasm-to- RT vacuole targeting pathway."; RL J. Biol. Chem. 285:29599-29607(2010). RN [23] RP SUBCELLULAR LOCATION. RX PubMed=15155809; DOI=10.1091/mbc.e04-02-0147; RA Stromhaug P.E., Reggiori F., Guan J., Wang C.-W., Klionsky D.J.; RT "Atg21 is a phosphoinositide binding protein required for efficient RT lipidation and localization of Atg8 during uptake of aminopeptidase I by RT selective autophagy."; RL Mol. Biol. Cell 15:3553-3566(2004). RN [24] RP SUBCELLULAR LOCATION. RX PubMed=15449304; DOI=10.1002/yea.1152; RA Suzuki K., Noda T., Ohsumi Y.; RT "Interrelationships among Atg proteins during autophagy in Saccharomyces RT cerevisiae."; RL Yeast 21:1057-1065(2004). RN [25] RP SUBCELLULAR LOCATION. RX PubMed=16079147; DOI=10.1074/jbc.m501701200; RA Meiling-Wesse K., Epple U.D., Krick R., Barth H., Appelles A., Voss C., RA Eskelinen E.L., Thumm M.; RT "Trs85 (Gsg1), a component of the TRAPP complexes, is required for the RT organization of the preautophagosomal structure during selective autophagy RT via the Cvt pathway."; RL J. Biol. Chem. 280:33669-33678(2005). RN [26] RP SUBCELLULAR LOCATION. RX PubMed=15659643; DOI=10.1091/mbc.e04-11-1035; RA Yorimitsu T., Klionsky D.J.; RT "Atg11 links cargo to the vesicle-forming machinery in the cytoplasm to RT vacuole targeting pathway."; RL Mol. Biol. Cell 16:1593-1605(2005). RN [27] RP SUBCELLULAR LOCATION. RX PubMed=16221887; DOI=10.1091/mbc.e05-07-0629; RA Reggiori F., Monastyrska I., Shintani T., Klionsky D.J.; RT "The actin cytoskeleton is required for selective types of autophagy, but RT not nonspecific autophagy, in the yeast Saccharomyces cerevisiae."; RL Mol. Biol. Cell 16:5843-5856(2005). RN [28] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATG4, CLEAVAGE BY ATG4, RP AND MUTAGENESIS OF TYR-49; LEU-50; PHE-77 AND PHE-79. RX PubMed=16680092; DOI=10.1038/sj.embor.7400698; RA Amar N., Lustig G., Ichimura Y., Ohsumi Y., Elazar Z.; RT "Two newly identified sites in the ubiquitin-like protein Atg8 are RT essential for autophagy."; RL EMBO Rep. 7:635-642(2006). RN [29] RP FUNCTION. RX PubMed=17132049; DOI=10.1371/journal.pbio.0040423; RA Bernales S., McDonald K.L., Walter P.; RT "Autophagy counterbalances endoplasmic reticulum expansion during the RT unfolded protein response."; RL PLoS Biol. 4:E423-E423(2006). RN [30] RP FUNCTION. RX PubMed=17404498; DOI=10.4161/auto.4127; RA Zhang Y., Qi H., Taylor R., Xu W., Liu L.F., Jin S.; RT "The role of autophagy in mitochondria maintenance: characterization of RT mitochondrial functions in autophagy-deficient S. cerevisiae strains."; RL Autophagy 3:337-346(2007). RN [31] RP FUNCTION. RX PubMed=17700056; DOI=10.4161/auto.4784; RA Ma J., Jin R., Dobry C.J., Lawson S.K., Kumar A.; RT "Overexpression of autophagy-related genes inhibits yeast filamentous RT growth."; RL Autophagy 3:604-609(2007). RN [32] RP CONJUGATION TO PHOSPHATIDYLETHANOLAMINE, FUNCTION OF THE ATG8-PE CONJUGATE, RP AND SUBUNIT. RX PubMed=17632063; DOI=10.1016/j.cell.2007.05.021; RA Nakatogawa H., Ichimura Y., Ohsumi Y.; RT "Atg8, a ubiquitin-like protein required for autophagosome formation, RT mediates membrane tethering and hemifusion."; RL Cell 130:165-178(2007). RN [33] RP SUBCELLULAR LOCATION. RX PubMed=17295840; DOI=10.1111/j.1365-2443.2007.01050.x; RA Suzuki K., Kubota Y., Sekito T., Ohsumi Y.; RT "Hierarchy of Atg proteins in pre-autophagosomal structure organization."; RL Genes Cells 12:209-218(2007). RN [34] RP CONJUGATION TO PHOSPHATIDYLETHANOLAMINE. RX PubMed=17699586; DOI=10.1091/mbc.e07-05-0485; RA Yorimitsu T., Zaman S., Broach J.R., Klionsky D.J.; RT "Protein kinase A and Sch9 cooperatively regulate induction of autophagy in RT Saccharomyces cerevisiae."; RL Mol. Biol. Cell 18:4180-4189(2007). RN [35] RP SUBCELLULAR LOCATION. RX PubMed=18625846; DOI=10.1083/jcb.200711112; RA Geng J., Baba M., Nair U., Klionsky D.J.; RT "Quantitative analysis of autophagy-related protein stoichiometry by RT fluorescence microscopy."; RL J. Cell Biol. 182:129-140(2008). RN [36] RP CONJUGATION TO PHOSPHATIDYLETHANOLAMINE. RX PubMed=18725539; DOI=10.1083/jcb.200801035; RA Cao Y., Cheong H., Song H., Klionsky D.J.; RT "In vivo reconstitution of autophagy in Saccharomyces cerevisiae."; RL J. Cell Biol. 182:703-713(2008). RN [37] RP SUBCELLULAR LOCATION. RX PubMed=18077553; DOI=10.1091/mbc.e07-08-0826; RA Cheong H., Nair U., Geng J., Klionsky D.J.; RT "The Atg1 kinase complex is involved in the regulation of protein RT recruitment to initiate sequestering vesicle formation for nonspecific RT autophagy in Saccharomyces cerevisiae."; RL Mol. Biol. Cell 19:668-681(2008). RN [38] RP FUNCTION. RX PubMed=18508918; DOI=10.1091/mbc.e07-12-1292; RA Xie Z., Nair U., Klionsky D.J.; RT "Atg8 controls phagophore expansion during autophagosome formation."; RL Mol. Biol. Cell 19:3290-3298(2008). RN [39] RP SUBCELLULAR LOCATION. RX PubMed=19088501; DOI=10.4161/auto.5.2.7201; RA Xie Z., Nair U., Geng J., Szefler M.B., Rothman E.D., Klionsky D.J.; RT "Indirect estimation of the area density of Atg8 on the phagophore."; RL Autophagy 5:217-220(2009). RN [40] RP FUNCTION, INTERACTION WITH ATG19, AND MUTAGENESIS OF ARG-28; LYS-48; RP TYR-49; LEU-50 AND LEU-55. RX PubMed=19398890; DOI=10.4161/auto.5.4.7696; RA Ho K.H., Chang H.E., Huang W.P.; RT "Mutation at the cargo-receptor binding site of Atg8 also affects its RT general autophagy regulation function."; RL Autophagy 5:461-471(2009). RN [41] RP INTERACTION WITH ATG32. RX PubMed=19619494; DOI=10.1016/j.devcel.2009.06.013; RA Okamoto K., Kondo-Okamoto N., Ohsumi Y.; RT "Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria RT via selective autophagy."; RL Dev. Cell 17:87-97(2009). RN [42] RP INTERACTION WITH ATG3, AND CONJUGATION TO PHOSPHATIDYLETHANOLAMINE. RX PubMed=19285500; DOI=10.1016/j.febslet.2009.03.009; RA Hanada T., Satomi Y., Takao T., Ohsumi Y.; RT "The amino-terminal region of Atg3 is essential for association with RT phosphatidylethanolamine in Atg8 lipidation."; RL FEBS Lett. 583:1078-1083(2009). RN [43] RP INDUCTION. RX PubMed=20952643; DOI=10.1128/aem.01535-10; RA Mendes-Ferreira A., Sampaio-Marques B., Barbosa C., Rodrigues F., Costa V., RA Mendes-Faia A., Ludovico P., Leao C.; RT "Accumulation of non-superoxide anion reactive oxygen species mediates RT nitrogen-limited alcoholic fermentation by Saccharomyces cerevisiae."; RL Appl. Environ. Microbiol. 76:7918-7924(2010). RN [44] RP SUBCELLULAR LOCATION. RX PubMed=20154084; DOI=10.1074/jbc.m109.080374; RA Nair U., Cao Y., Xie Z., Klionsky D.J.; RT "Roles of the lipid-binding motifs of Atg18 and Atg21 in the cytoplasm to RT vacuole targeting pathway and autophagy."; RL J. Biol. Chem. 285:11476-11488(2010). RN [45] RP INTERACTION WITH ATG34. RX PubMed=20639194; DOI=10.1074/jbc.m110.143511; RA Suzuki K., Kondo C., Morimoto M., Ohsumi Y.; RT "Selective transport of alpha-mannosidase by autophagic pathways: RT identification of a novel receptor, Atg34p."; RL J. Biol. Chem. 285:30019-30025(2010). RN [46] RP SUBCELLULAR LOCATION. RX PubMed=20065092; DOI=10.1083/jcb.200904075; RA Yen W.L., Shintani T., Nair U., Cao Y., Richardson B.C., Li Z., RA Hughson F.M., Baba M., Klionsky D.J.; RT "The conserved oligomeric Golgi complex is involved in double-membrane RT vesicle formation during autophagy."; RL J. Cell Biol. 188:101-114(2010). RN [47] RP FUNCTION, AND INTERACTION WITH SHP1. RX PubMed=20855502; DOI=10.1083/jcb.201002075; RA Krick R., Bremer S., Welter E., Schlotterhose P., Muehe Y., Eskelinen E.L., RA Thumm M.; RT "Cdc48/p97 and Shp1/p47 regulate autophagosome biogenesis in concert with RT ubiquitin-like Atg8."; RL J. Cell Biol. 190:965-973(2010). RN [48] RP SUBCELLULAR LOCATION. RX PubMed=20855505; DOI=10.1083/jcb.200912089; RA Mari M., Griffith J., Rieter E., Krishnappa L., Klionsky D.J., Reggiori F.; RT "An Atg9-containing compartment that functions in the early steps of RT autophagosome biogenesis."; RL J. Cell Biol. 190:1005-1022(2010). RN [49] RP SUBCELLULAR LOCATION. RX PubMed=22144692; DOI=10.1083/jcb.201106098; RA Bruns C., McCaffery J.M., Curwin A.J., Duran J.M., Malhotra V.; RT "Biogenesis of a novel compartment for autophagosome-mediated RT unconventional protein secretion."; RL J. Cell Biol. 195:979-992(2011). RN [50] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21429936; DOI=10.1242/jcs.076406; RA Mendl N., Occhipinti A., Muller M., Wild P., Dikic I., Reichert A.S.; RT "Mitophagy in yeast is independent of mitochondrial fission and requires RT the stress response gene WHI2."; RL J. Cell Sci. 124:1339-1350(2011). RN [51] RP ATG8-PE DECONJUGATION. RX PubMed=22240591; DOI=10.4161/auto.8.2.18373; RA Nakatogawa H., Ishii J., Asai E., Ohsumi Y.; RT "Atg4 recycles inappropriately lipidated Atg8 to promote autophagosome RT biogenesis."; RL Autophagy 8:177-186(2012). RN [52] RP FUNCTION OF ATG8-PE DECONJUGATION. RX PubMed=22622160; DOI=10.4161/auto.19385; RA Nair U., Yen W.L., Mari M., Cao Y., Xie Z., Baba M., Reggiori F., RA Klionsky D.J.; RT "A role for Atg8-PE deconjugation in autophagosome biogenesis."; RL Autophagy 8:780-793(2012). RN [53] RP ATG8-PE DECONJUGATION. RX PubMed=22652539; DOI=10.4161/auto.19652; RA Yu Z.Q., Ni T., Hong B., Wang H.Y., Jiang F.J., Zou S., Chen Y., RA Zheng X.L., Klionsky D.J., Liang Y., Xie Z.; RT "Dual roles of Atg8-PE deconjugation by Atg4 in autophagy."; RL Autophagy 8:883-892(2012). RN [54] RP INTERACTION WITH ATG1. RX PubMed=22885598; DOI=10.1038/emboj.2012.225; RA Kraft C., Kijanska M., Kalie E., Siergiejuk E., Lee S.S., Semplicio G., RA Stoffel I., Brezovich A., Verma M., Hansmann I., Ammerer G., Hofmann K., RA Tooze S., Peter M.; RT "Binding of the Atg1/ULK1 kinase to the ubiquitin-like protein Atg8 RT regulates autophagy."; RL EMBO J. 31:3691-3703(2012). RN [55] RP CONJUGATION TO PHOSPHATIDYLETHANOLAMINE. RX PubMed=23064152; DOI=10.1038/emboj.2012.278; RA Romanov J., Walczak M., Ibiricu I., Schuchner S., Ogris E., Kraft C., RA Martens S.; RT "Mechanism and functions of membrane binding by the Atg5-Atg12/Atg16 RT complex during autophagosome formation."; RL EMBO J. 31:4304-4317(2012). RN [56] RP FUNCTION. RX PubMed=22768199; DOI=10.1371/journal.pone.0040013; RA Mijaljica D., Prescott M., Devenish R.J.; RT "A late form of nucleophagy in Saccharomyces cerevisiae."; RL PLoS ONE 7:E40013-E40013(2012). RN [57] RP INTERACTION WITH ATG1. RX PubMed=22778255; DOI=10.1074/jbc.c112.387514; RA Nakatogawa H., Ohbayashi S., Sakoh-Nakatogawa M., Kakuta S., Suzuki S.W., RA Kirisako H., Kondo-Kakuta C., Noda N.N., Yamamoto H., Ohsumi Y.; RT "The autophagy-related protein kinase Atg1 interacts with the ubiquitin- RT like protein Atg8 via the Atg8 family interacting motif to facilitate RT autophagosome formation."; RL J. Biol. Chem. 287:28503-28507(2012). RN [58] RP INDUCTION. RX PubMed=22733735; DOI=10.1073/pnas.1200313109; RA Bartholomew C.R., Suzuki T., Du Z., Backues S.K., Jin M., Lynch-Day M.A., RA Umekawa M., Kamath A., Zhao M., Xie Z., Inoki K., Klionsky D.J.; RT "Ume6 transcription factor is part of a signaling cascade that regulates RT autophagy."; RL Proc. Natl. Acad. Sci. U.S.A. 109:11206-11210(2012). RN [59] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [60] RP INTERACTION WITH ATG3, AND CONJUGATION TO PHOSPHATIDYLETHANOLAMINE. RX PubMed=22539722; DOI=10.1126/science.1216990; RA Yi C., Ma M., Ran L., Zheng J., Tong J., Zhu J., Ma C., Sun Y., Zhang S., RA Feng W., Zhu L., Le Y., Gong X., Yan X., Hong B., Jiang F.J., Xie Z., RA Miao D., Deng H., Yu L.; RT "Function and molecular mechanism of acetylation in autophagy regulation."; RL Science 336:474-477(2012). RN [61] RP SUBCELLULAR LOCATION. RX PubMed=23549786; DOI=10.1242/jcs.122960; RA Suzuki K., Akioka M., Kondo-Kakuta C., Yamamoto H., Ohsumi Y.; RT "Fine mapping of autophagy-related proteins during autophagosome formation RT in Saccharomyces cerevisiae."; RL J. Cell Sci. 126:2534-2544(2013). RN [62] RP CONJUGATION TO PHOSPHATIDYLETHANOLAMINE, AND ATG8-PE DECONJUGATION. RX PubMed=28330855; DOI=10.15252/embr.201643146; RA Abreu S., Kriegenburg F., Gomez-Sanchez R., Mari M., Sanchez-Wandelmer J., RA Skytte Rasmussen M., Soares Guimaraes R., Zens B., Schuschnig M., RA Hardenberg R., Peter M., Johansen T., Kraft C., Martens S., Reggiori F.; RT "Conserved Atg8 recognition sites mediate Atg4 association with RT autophagosomal membranes and Atg8 deconjugation."; RL EMBO Rep. 18:765-780(2017). RN [63] RP SUBCELLULAR LOCATION. RX PubMed=30510114; DOI=10.1242/jcs.221655; RA Vigie P., Cougouilles E., Bhatia-Kissova I., Salin B., Blancard C., RA Camougrand N.; RT "The mitochondrial phosphatidylserine decarboxylase Psd1 is involved in RT nitrogen starvation-induced mitophagy in yeast."; RL J. Cell Sci. 132:jcs221655-jcs221655(2019). RN [64] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HFL1. RX PubMed=34088313; DOI=10.1186/s12915-021-01048-7; RA He C.W., Cui X.F., Ma S.J., Xu Q., Ran Y.P., Chen W.Z., Mu J.X., Li H., RA Zhu J., Gong Q., Xie Z.; RT "Membrane recruitment of Atg8 by Hfl1 facilitates turnover of vacuolar RT membrane proteins in yeast cells approaching stationary phase."; RL BMC Biol. 19:117-117(2021). RN [65] RP INTERACTION WITH PHB1 AND PHB2. RX PubMed=38964378; DOI=10.1080/15548627.2024.2371717; RA Garcia-Chavez D., Dominguez-Martin E., Kawasaki L., Ongay-Larios L., RA Ruelas-Ramirez H., Mendoza-Martinez A.E., Pardo J.P., Funes S., Coria R.; RT "Prohibitins, Phb1 and Phb2, function as Atg8 receptors to support yeast RT mitophagy and also play a negative regulatory role in Atg32 processing."; RL Autophagy 20:1-12(2024). RN [66] RP INTERACTION WITH ATG45. RX PubMed=38832010; DOI=10.1016/j.isci.2024.109810; RA Isoda T., Takeda E., Hosokawa S., Hotta-Ren S., Ohsumi Y.; RT "Atg45 is an autophagy receptor for glycogen, a non-preferred cargo of bulk RT autophagy in yeast."; RL IScience 27:109810-109810(2024). RN [67] RP X-RAY CRYSTALLOGRAPHY, INTERACTION WITH ATG19, AND MUTAGENESIS OF ARG-28; RP PRO-52 AND ARG-67. RX PubMed=19021777; DOI=10.1111/j.1365-2443.2008.01238.x; RA Noda N.N., Kumeta H., Nakatogawa H., Satoo K., Adachi W., Ishii J., RA Fujioka Y., Ohsumi Y., Inagaki F.; RT "Structural basis of target recognition by Atg8/LC3 during selective RT autophagy."; RL Genes Cells 13:1211-1218(2008). RN [68] RP STRUCTURE BY NMR OF MUTANT PRO-26, MUTAGENESIS OF LYS-26, AND CONJUGATION RP TO PHOSPHATIDYLETHANOLAMINE. RX PubMed=20428927; DOI=10.1007/s10858-010-9420-1; RA Kumeta H., Watanabe M., Nakatogawa H., Yamaguchi M., Ogura K., Adachi W., RA Fujioka Y., Noda N.N., Ohsumi Y., Inagaki F.; RT "The NMR structure of the autophagy-related protein Atg8."; RL J. Biomol. NMR 47:237-241(2010). RN [69] RP STRUCTURE BY NMR. RX PubMed=20382112; DOI=10.1016/j.bbrc.2010.04.043; RA Schwarten M., Stoldt M., Mohrluder J., Willbold D.; RT "Solution structure of Atg8 reveals conformational polymorphism of the N- RT terminal domain."; RL Biochem. Biophys. Res. Commun. 395:426-431(2010). RN [70] RP STRUCTURE BY NMR, AND X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ATG7. RX PubMed=22055191; DOI=10.1016/j.molcel.2011.08.035; RA Noda N.N., Satoo K., Fujioka Y., Kumeta H., Ogura K., Nakatogawa H., RA Ohsumi Y., Inagaki F.; RT "Structural basis of Atg8 activation by a homodimeric E1, Atg7."; RL Mol. Cell 44:462-475(2011). RN [71] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ATG7. RX PubMed=22056771; DOI=10.1038/nsmb.2165; RA Hong S.B., Kim B.W., Lee K.E., Kim S.W., Jeon H., Kim J., Song H.K.; RT "Insights into noncanonical E1 enzyme activation from the structure of RT autophagic E1 Atg7 with Atg8."; RL Nat. Struct. Mol. Biol. 18:1323-1330(2011). RN [72] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=22308029; DOI=10.1074/jbc.m111.299917; RA Kondo-Okamoto N., Noda N.N., Suzuki S.W., Nakatogawa H., Takahashi I., RA Matsunami M., Hashimoto A., Inagaki F., Ohsumi Y., Okamoto K.; RT "Autophagy-related protein 32 acts as autophagic degron and directly RT initiates mitophagy."; RL J. Biol. Chem. 287:10631-10638(2012). CC -!- FUNCTION: Ubiquitin-like modifier involved in cytoplasm to vacuole CC transport (Cvt) vesicles and autophagosome formation (PubMed:10525546, CC PubMed:10681575, PubMed:10837468, PubMed:11038174, PubMed:11149920, CC PubMed:16680092, PubMed:18508918, PubMed:19398890, PubMed:21429936, CC PubMed:7593182, PubMed:8224160). With ATG4, mediates the delivery of CC the vesicles and autophagosomes to the vacuole via the microtubule CC cytoskeleton (PubMed:9649430). 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 CC (PubMed:17404498, PubMed:22768199). Also participates in membrane CC fusion events that take place in the early secretory pathway CC (PubMed:10837468). Also involved in endoplasmic reticulum-specific CC autophagic process and is essential for the survival of cells subjected CC to severe ER stress (PubMed:17132049). The ATG8-PE conjugate mediates CC tethering between adjacent membranes and stimulates membrane CC hemifusion, leading to expansion of the autophagosomal membrane during CC autophagy (PubMed:11100732, PubMed:17632063, PubMed:20855502). Moreover CC not only conjugation, but also subsequent ATG8-PE deconjugation is an CC important step required to facilitate multiple events during CC macroautophagy, and especially for efficient autophagosome biogenesis, CC the assembly of ATG9-containing tubulovesicular clusters into CC phagophores/autophagosomes, and for the disassembly of PAS-associated CC ATG components (PubMed:17632063, PubMed:20855502, PubMed:22622160). CC Also plays a role in regulation of filamentous growth CC (PubMed:17700056). {ECO:0000269|PubMed:10525546, CC ECO:0000269|PubMed:10681575, ECO:0000269|PubMed:10837468, CC ECO:0000269|PubMed:11038174, ECO:0000269|PubMed:11100732, CC ECO:0000269|PubMed:11149920, ECO:0000269|PubMed:16680092, CC ECO:0000269|PubMed:17132049, ECO:0000269|PubMed:17404498, CC ECO:0000269|PubMed:17632063, ECO:0000269|PubMed:17700056, CC ECO:0000269|PubMed:18508918, ECO:0000269|PubMed:19398890, CC ECO:0000269|PubMed:20855502, ECO:0000269|PubMed:21429936, CC ECO:0000269|PubMed:22622160, ECO:0000269|PubMed:22768199, CC ECO:0000269|PubMed:7593182, ECO:0000269|PubMed:8224160, CC ECO:0000269|PubMed:9649430}. CC -!- FUNCTION: Has a lipidation-independent vacuolar function to facilitate CC the degradation of vacuolar integral membrane proteins during early- CC stationary vacuole turnover (EVT) when cells enter stationary phase. CC {ECO:0000269|PubMed:34088313}. CC -!- SUBUNIT: Conjugation to phosphatidylethanolamine (PE) leads to CC homodimerization (PubMed:17632063, PubMed:19285500, PubMed:20615880, CC PubMed:22539722). Interacts with ATG1 (PubMed:22778255, CC PubMed:22885598). Interacts with ATG3 (PubMed:11100732, CC PubMed:19285500, PubMed:20615880, PubMed:22539722). Interacts with ATG4 CC (PubMed:16680092, PubMed:9649430). Interacts with ATG7 CC (PubMed:11100732, PubMed:11139573, PubMed:22055191, PubMed:22056771). CC Interacts with ATG12 (PubMed:11675395). Interacts with ATG32 CC (PubMed:19619494). Interacts with ATG34 (PubMed:20639194). Interacts CC with ATG19 (via the C-terminal 10 residues) (PubMed:11675395, CC PubMed:12479808, PubMed:19021777, PubMed:19398890). Interacts with the CC endoplasmic reticulum to Golgi v-SNARE protein BET1 (PubMed:10837468). CC Interacts with the vacuolar v-SNARE protein NYV1 (PubMed:10837468). CC Interacts with the UBX domain-containing protein SHP1 CC (PubMed:20855502). Interacts with the vacuolar membrane protein HFL1 CC (PubMed:34088313). Interacts with ATG45 (PubMed:38832010). Interacts CC with the mitochondrial prohibitin complex subunits PHB1 and PHB2; the CC interaction may support mitophagosome assembly (PubMed:38964378). CC {ECO:0000269|PubMed:10837468, ECO:0000269|PubMed:11100732, CC ECO:0000269|PubMed:11139573, ECO:0000269|PubMed:11675395, CC ECO:0000269|PubMed:12479808, ECO:0000269|PubMed:16680092, CC ECO:0000269|PubMed:17632063, ECO:0000269|PubMed:19021777, CC ECO:0000269|PubMed:19285500, ECO:0000269|PubMed:19398890, CC ECO:0000269|PubMed:19619494, ECO:0000269|PubMed:20615880, CC ECO:0000269|PubMed:20639194, ECO:0000269|PubMed:20855502, CC ECO:0000269|PubMed:22055191, ECO:0000269|PubMed:22056771, CC ECO:0000269|PubMed:22539722, ECO:0000269|PubMed:22778255, CC ECO:0000269|PubMed:22885598, ECO:0000269|PubMed:34088313, CC ECO:0000269|PubMed:38832010, ECO:0000269|PubMed:38964378, CC ECO:0000269|PubMed:9649430}. CC -!- INTERACTION: CC P38182; P53104: ATG1; NbExp=3; IntAct=EBI-2684, EBI-2657; CC P38182; P35193: ATG19; NbExp=5; IntAct=EBI-2684, EBI-29291; CC P38182; P40344: ATG3; NbExp=10; IntAct=EBI-2684, EBI-3381; CC P38182; Q12292: ATG34; NbExp=4; IntAct=EBI-2684, EBI-36362; CC P38182; Q06159: ATG39; NbExp=3; IntAct=EBI-2684, EBI-33888; CC P38182; P53867: ATG4; NbExp=3; IntAct=EBI-2684, EBI-29160; CC P38182; Q99325: ATG40; NbExp=3; IntAct=EBI-2684, EBI-3681992; CC P38182; P38862: ATG7; NbExp=12; IntAct=EBI-2684, EBI-2677; CC P38182; P22804: BET1; NbExp=2; IntAct=EBI-2684, EBI-3550; CC P38182; Q08412: CUE5; NbExp=4; IntAct=EBI-2684, EBI-37580; CC P38182; Q14596: NBR1; Xeno; NbExp=7; IntAct=EBI-2684, EBI-742698; CC P38182; Q13501: SQSTM1; Xeno; NbExp=3; IntAct=EBI-2684, EBI-307104; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, cvt vesicle membrane; Lipid- CC anchor {ECO:0000269|PubMed:11100732}. Cytoplasmic vesicle, CC autophagosome membrane {ECO:0000269|PubMed:11149920, CC ECO:0000269|PubMed:11689437, ECO:0000269|PubMed:15659643, CC ECO:0000269|PubMed:16680092, ECO:0000269|PubMed:19398890}; Lipid-anchor CC {ECO:0000269|PubMed:11100732}. Vacuole membrane CC {ECO:0000269|PubMed:23549786, ECO:0000269|PubMed:34088313}; Peripheral CC membrane protein {ECO:0000269|PubMed:34088313}. Mitochondrion membrane CC {ECO:0000269|PubMed:30510114}; Peripheral membrane protein CC {ECO:0000269|PubMed:30510114}. Note=Membrane-associated through a lipid CC anchor. This association needs the 2 ubiquitin-like systems required CC for cytoplasm to vacuole transport and autophagy. ATG18 and ATG21 CC facilitate the recruitment of ATG8-PE to the site of autophagosome CC formation and protect it from premature cleavage by ATG4. Localizes to CC both the isolation membrane (IM) and the vacuole-isolation membrane CC contact site (VICS) during IM expansion. The IM is a membrane sac CC generated from the pre-autophagosomal structure that ultimately expands CC to become a mature autophagosome. Upon starvation, is also recruited to CC into unique membrane structures near SEC13-containing ER exit sites CC which lack components of the Golgi apparatus and the endosomes, and CC which were called a compartments for unconventional protein secretion CC (CUPS). Associates with mitochondria following nitrogen starvation in a CC respiratory carbon source (PubMed:30510114). CC {ECO:0000269|PubMed:30510114}. CC -!- INDUCTION: Up-regulated upon starvation conditions. Expression is under CC the control of UME6 which acts along with a histone deacetylase complex CC including SIN3 and RPD3 to negatively regulate ATG8 levels and CC subsequent autophagic activity. {ECO:0000269|PubMed:20952643, CC ECO:0000269|PubMed:22733735}. CC -!- PTM: The C-terminal Arg-117 residue of ATG8 is removed by ATG4 to CC expose Gly-116 at the C-terminus (PubMed:11038174, PubMed:11149920, CC PubMed:16680092). This Gly-116 forms then a thioester bond with the CC 'Cys-507' of ATG7 (E1-like activating enzyme) before being transferred CC to the 'Cys-234' of ATG3 (the specific E2 conjugating enzyme), in order CC to be finally amidated with phosphatidylethanolamine (PubMed:11100732, CC PubMed:15277523, PubMed:17632063, PubMed:17699586, PubMed:18725539, CC PubMed:19285500, PubMed:20428927, PubMed:20615880, PubMed:22539722, CC PubMed:23064152, PubMed:28330855). This lipid modification anchors ATG8 CC to membranes and can be reversed by ATG4, releasing soluble ATG8 CC (PubMed:22240591, PubMed:22622160, PubMed:22652539, PubMed:28330855). CC {ECO:0000269|PubMed:11038174, ECO:0000269|PubMed:11100732, CC ECO:0000269|PubMed:11149920, ECO:0000269|PubMed:15277523, CC ECO:0000269|PubMed:16680092, ECO:0000269|PubMed:17632063, CC ECO:0000269|PubMed:17699586, ECO:0000269|PubMed:18725539, CC ECO:0000269|PubMed:19285500, ECO:0000269|PubMed:20428927, CC ECO:0000269|PubMed:20615880, ECO:0000269|PubMed:22240591, CC ECO:0000269|PubMed:22539722, ECO:0000269|PubMed:22622160, CC ECO:0000269|PubMed:22652539, ECO:0000269|PubMed:23064152, CC ECO:0000269|PubMed:28330855}. CC -!- MISCELLANEOUS: Present with 2010 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; X79489; CAA56032.1; -; Genomic_DNA. DR EMBL; Z35839; CAA84899.1; -; Genomic_DNA. DR EMBL; AY692870; AAT92889.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07045.1; -; Genomic_DNA. DR PIR; S45432; S45432. DR RefSeq; NP_009475.1; NM_001178318.1. DR PDB; 2KQ7; NMR; -; A=1-117. DR PDB; 2KWC; NMR; -; A=1-116. DR PDB; 2LI5; NMR; -; A=1-116. DR PDB; 2ZPN; X-ray; 2.70 A; A/B/C/D=1-116. DR PDB; 3RUI; X-ray; 1.91 A; B=1-116. DR PDB; 3VH3; X-ray; 2.00 A; B=1-116. DR PDB; 3VH4; X-ray; 2.65 A; B=1-116. DR PDB; 3VXW; X-ray; 3.00 A; A=1-116. DR PDB; 5YEC; X-ray; 2.15 A; B/D=1-116. DR PDB; 6AAG; X-ray; 2.44 A; A/B/C/D/E/F/G=1-116. DR PDB; 6WY6; X-ray; 1.77 A; A/B=1-116. DR PDB; 7BRN; X-ray; 2.23 A; A=1-116. DR AlphaFoldDB; P38182; -. DR BMRB; P38182; -. DR SMR; P38182; -. DR BioGRID; 32625; 797. DR DIP; DIP-1197N; -. DR ELM; P38182; -. DR FunCoup; P38182; 739. DR IntAct; P38182; 23. DR STRING; 4932.YBL078C; -. DR iPTMnet; P38182; -. DR PaxDb; 4932-YBL078C; -. DR PeptideAtlas; P38182; -. DR EnsemblFungi; YBL078C_mRNA; YBL078C; YBL078C. DR GeneID; 852200; -. DR KEGG; sce:YBL078C; -. DR AGR; SGD:S000000174; -. DR SGD; S000000174; ATG8. DR VEuPathDB; FungiDB:YBL078C; -. DR eggNOG; KOG1654; Eukaryota. DR HOGENOM; CLU_119276_0_1_1; -. DR InParanoid; P38182; -. DR OMA; AAMMSMI; -. DR OrthoDB; 6738456at2759; -. DR BioCyc; YEAST:G3O-28969-MONOMER; -. DR Reactome; R-SCE-1632852; Macroautophagy. DR Reactome; R-SCE-8854214; TBC/RABGAPs. DR Reactome; R-SCE-8934903; Receptor Mediated Mitophagy. DR BioGRID-ORCS; 852200; 0 hits in 10 CRISPR screens. DR CD-CODE; 00C0C35B; Synthetic Condensate 000282. DR CD-CODE; 6697AF75; Synthetic Condensate 000332. DR CD-CODE; 7EE86442; Synthetic Condensate 000355. DR CD-CODE; E03F929F; Stress granule. DR EvolutionaryTrace; P38182; -. DR PHI-base; PHI:124479; -. DR PRO; PR:P38182; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P38182; protein. DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB. DR GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central. DR GO; GO:0033110; C:Cvt vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD. DR GO; GO:0005811; C:lipid droplet; IDA:SGD. DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB. DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD. DR GO; GO:0005774; C:vacuolar membrane; EXP:UniProtKB. DR GO; GO:0120095; C:vacuole-isolation membrane contact site; IDA:SGD. DR GO; GO:0008429; F:phosphatidylethanolamine binding; IMP:SGD. DR GO; GO:0031386; F:protein tag activity; IMP:SGD. DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB. DR GO; GO:0097352; P:autophagosome maturation; IBA:GO_Central. DR GO; GO:0006914; P:autophagy; IMP:UniProtKB. DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central. DR GO; GO:0032258; P:cytoplasm to vacuole targeting by the Cvt pathway; IMP:SGD. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD. DR GO; GO:0140042; P:lipid droplet formation; IMP:SGD. DR GO; GO:0061025; P:membrane fusion; IDA:SGD. DR GO; GO:0000423; P:mitophagy; IBA:GO_Central. DR GO; GO:0044804; P:nucleophagy; IMP:SGD. DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD. DR GO; GO:0034497; P:protein localization to phagophore assembly site; IMP:SGD. DR GO; GO:0071211; P:protein targeting to vacuole involved in autophagy; IMP:SGD. DR GO; GO:0031503; P:protein-containing complex localization; IMP:SGD. DR GO; GO:0016241; P:regulation of macroautophagy; IMP:SGD. DR GO; GO:1905153; P:regulation of membrane invagination; IMP:SGD. DR GO; GO:0061709; P:reticulophagy; IMP:SGD. DR CDD; cd16128; Ubl_ATG8; 1. DR FunFam; 3.10.20.90:FF:000010; Autophagy-related protein; 1. DR Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1. DR InterPro; IPR004241; Atg8-like. DR InterPro; IPR029071; Ubiquitin-like_domsf. 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 1: Evidence at protein level; KW 3D-structure; Autophagy; Cytoplasmic vesicle; Lipoprotein; Membrane; KW Mitochondrion; Protein transport; Reference proteome; Transport; KW Ubl conjugation pathway; Vacuole. FT CHAIN 1..116 FT /note="Autophagy-related protein 8" FT /id="PRO_0000017242" FT PROPEP 117 FT /note="Removed in mature form" FT /evidence="ECO:0000269|PubMed:11038174" FT /id="PRO_0000017243" FT SITE 116..117 FT /note="Cleavage; by ATG4" FT /evidence="ECO:0000269|PubMed:11038174" FT LIPID 116 FT /note="Phosphatidylethanolamine amidated glycine" FT /evidence="ECO:0000269|PubMed:11100732" FT MUTAGEN 26 FT /note="K->P: No effect on autophagic activity." FT /evidence="ECO:0000269|PubMed:20428927" FT MUTAGEN 28 FT /note="R->D: Impairs ATG19-binding and autophagic FT activity." FT /evidence="ECO:0000269|PubMed:19021777, FT ECO:0000269|PubMed:19398890" FT MUTAGEN 48 FT /note="K->E: Impairs autophagic activity." FT /evidence="ECO:0000269|PubMed:19398890" FT MUTAGEN 49 FT /note="Y->A: Impairs ATG19-binding, PE-conjugation, and FT autophagic activity." FT /evidence="ECO:0000269|PubMed:16680092, FT ECO:0000269|PubMed:19398890" FT MUTAGEN 50 FT /note="L->A: Impairs ATG19-binding and autophagic FT activity." FT /evidence="ECO:0000269|PubMed:16680092, FT ECO:0000269|PubMed:19398890" FT MUTAGEN 52 FT /note="P->A: Significantly decreases ATG19-binding and FT autophagic activity." FT /evidence="ECO:0000269|PubMed:19021777" FT MUTAGEN 55 FT /note="L->A: Impairs autophagic activity." FT /evidence="ECO:0000269|PubMed:19398890" FT MUTAGEN 67 FT /note="R->A: Significantly decreases ATG19-binding and FT autophagic activity." FT /evidence="ECO:0000269|PubMed:19021777" FT MUTAGEN 77 FT /note="F->A: Impairs interaction with ATG4, cleavage by FT ATG4, PAS localization, and autophagic activity; when FT associated with A-79." FT /evidence="ECO:0000269|PubMed:16680092" FT MUTAGEN 79 FT /note="F->A: Impairs interaction with ATG4, cleavage by FT ATG4, PAS localization, and autophagic activity; when FT associated with A-77." FT /evidence="ECO:0000269|PubMed:16680092" FT MUTAGEN 116 FT /note="G->A: No cleaving of the C-terminal R-117 by ATG4. FT Defect in Cvt pathway and autophagy." FT /evidence="ECO:0000269|PubMed:11038174" FT MUTAGEN 117 FT /note="R->M: Normal processing after G-116 by ATG4." FT /evidence="ECO:0000269|PubMed:11038174" FT HELIX 5..8 FT /evidence="ECO:0007829|PDB:6WY6" FT HELIX 11..24 FT /evidence="ECO:0007829|PDB:6WY6" FT STRAND 28..35 FT /evidence="ECO:0007829|PDB:6WY6" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:5YEC" FT STRAND 48..52 FT /evidence="ECO:0007829|PDB:6WY6" FT HELIX 57..67 FT /evidence="ECO:0007829|PDB:6WY6" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:6WY6" FT STRAND 87..90 FT /evidence="ECO:0007829|PDB:2KWC" FT HELIX 91..98 FT /evidence="ECO:0007829|PDB:6WY6" FT STRAND 105..112 FT /evidence="ECO:0007829|PDB:6WY6" SQ SEQUENCE 117 AA; 13627 MW; 1246CEFF5A038819 CRC64; MKSTFKSEYP FEKRKAESER IADRFKNRIP VICEKAEKSD IPEIDKRKYL VPADLTVGQF VYVIRKRIML PPEKAIFIFV NDTLPPTAAL MSAIYQEHKD KDGFLYVTYS GENTFGR //