ATG9_YEAST
ID ATG9_YEAST Reviewed; 997 AA.
AC Q12142; D6VRJ9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Autophagy-related protein 9 {ECO:0000303|PubMed:14536056};
DE AltName: Full=Cytoplasm to vacuole targeting protein 7 {ECO:0000303|PubMed:7593182};
GN Name=ATG9 {ECO:0000303|PubMed:14536056};
GN Synonyms=APG9 {ECO:0000303|PubMed:8224160},
GN AUT9 {ECO:0000303|PubMed:8663607}, CVT7 {ECO:0000303|PubMed:7593182};
GN OrderedLocusNames=YDL149W {ECO:0000312|SGD:S000002308};
GN ORFNames=D1560 {ECO:0000303|PubMed:8972581};
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].
RX PubMed=8972581;
RX DOI=10.1002/(sici)1097-0061(199612)12:15%3c1587::aid-yea46%3e3.0.co;2-6;
RA Delaveau T.T.D., Blugeon C., Jacq C., Perea J.;
RT "Analysis of a 23 kb region on the left arm of yeast chromosome IV.";
RL Yeast 12:1587-1592(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 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 [5]
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 [6]
RP FUNCTION.
RX PubMed=8663607; DOI=10.1074/jbc.271.30.17621;
RA Harding T.M., Hefner-Gravink A., Thumm M., Klionsky D.J.;
RT "Genetic and phenotypic overlap between autophagy and the cytoplasm to
RT vacuole protein targeting pathway.";
RL J. Biol. Chem. 271:17621-17624(1996).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10735854; DOI=10.1128/jb.182.8.2125-2133.2000;
RA Lang T., Reiche S., Straub M., Bredschneider M., Thumm M.;
RT "Autophagy and the cvt pathway both depend on AUT9.";
RL J. Bacteriol. 182:2125-2133(2000).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10662773; DOI=10.1083/jcb.148.3.465;
RA Noda T., Kim J., Huang W.-P., Baba M., Tokunaga C., Ohsumi Y.,
RA Klionsky D.J.;
RT "Apg9p/Cvt7p is an integral membrane protein required for transport vesicle
RT formation in the Cvt and autophagy pathways.";
RL J. Cell Biol. 148:465-480(2000).
RN [9]
RP FUNCTION.
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 [10]
RP INTERACTION WITH ATG2.
RX PubMed=11382760; DOI=10.1074/jbc.m102342200;
RA Wang C.-W., Kim J., Huang W.-P., Abeliovich H., Stromhaug P.E.,
RA Dunn W.A. Jr., Klionsky D.J.;
RT "Apg2 is a novel protein required for the cytoplasm to vacuole targeting,
RT autophagy, and pexophagy pathways.";
RL J. Biol. Chem. 276:30442-30451(2001).
RN [11]
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 [12]
RP FUNCTION, AND INTERACTION WITH ATG23.
RX PubMed=14504273; DOI=10.1074/jbc.m309238200;
RA Tucker K.A., Reggiori F., Dunn W.A. Jr., Klionsky D.J.;
RT "Atg23 is essential for the cytoplasm to vacuole targeting pathway and
RT efficient autophagy but not pexophagy.";
RL J. Biol. Chem. 278:48445-48452(2003).
RN [13]
RP SUBCELLULAR LOCATION, INTERACTION WITH ATG18, AND TRAFFICKING.
RX PubMed=14723849; DOI=10.1016/s1534-5807(03)00402-7;
RA Reggiori F., Tucker K.A., Stromhaug P.E., Klionsky D.J.;
RT "The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from
RT the pre-autophagosomal structure.";
RL Dev. Cell 6:79-90(2004).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=15138258; DOI=10.1074/jbc.m404399200;
RA Shintani T., Klionsky D.J.;
RT "Cargo proteins facilitate the formation of transport vesicles in the
RT cytoplasm to vacuole targeting pathway.";
RL J. Biol. Chem. 279:29889-29894(2004).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=16874040; DOI=10.4161/auto.1.2.1840;
RA Reggiori F., Shintani T., Nair U., Klionsky D.J.;
RT "Atg9 cycles between mitochondria and the pre-autophagosomal structure in
RT yeasts.";
RL Autophagy 1:101-109(2005).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=16787937; DOI=10.1242/jcs.03047;
RA Reggiori F., Klionsky D.J.;
RT "Atg9 sorting from mitochondria is impaired in early secretion and VFT-
RT complex mutants in Saccharomyces cerevisiae.";
RL J. Cell Sci. 119:2903-2911(2006).
RN [17]
RP INTERACTION WITH ATG11; ATG23 AND ATG27, AND MUTAGENESIS OF HIS-192.
RX PubMed=17178909; DOI=10.1083/jcb.200606084;
RA He C., Song H., Yorimitsu T., Monastyrska I., Yen W.-L., Legakis J.E.,
RA Klionsky D.J.;
RT "Recruitment of Atg9 to the preautophagosomal structure by Atg11 is
RT essential for selective autophagy in budding yeast.";
RL J. Cell Biol. 175:925-935(2006).
RN [18]
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 [19]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [20]
RP FUNCTION.
RX PubMed=17329962; DOI=10.4161/auto.3912;
RA He C., Klionsky D.J.;
RT "Atg9 trafficking in autophagy-related pathways.";
RL Autophagy 3:271-274(2007).
RN [21]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17426440; DOI=10.4161/auto.4129;
RA Legakis J.E., Yen W.L., Klionsky D.J.;
RT "A cycling protein complex required for selective autophagy.";
RL Autophagy 3:422-432(2007).
RN [22]
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 [23]
RP SUBCELLULAR LOCATION, AND TRAFFICKING.
RX PubMed=17135291; DOI=10.1091/mbc.e06-07-0612;
RA Yen W.-L., Legakis J.E., Nair U., Klionsky D.J.;
RT "Atg27 is required for autophagy-dependent cycling of Atg9.";
RL Mol. Biol. Cell 18:581-593(2007).
RN [24]
RP INTERACTION WITH ATG11.
RX PubMed=17192412; DOI=10.1091/mbc.e06-08-0683;
RA Chang C.Y., Huang W.P.;
RT "Atg19 mediates a dual interaction cargo sorting mechanism in selective
RT autophagy.";
RL Mol. Biol. Cell 18:919-929(2007).
RN [25]
RP FUNCTION.
RX PubMed=18818209; DOI=10.1074/jbc.m802403200;
RA Kanki T., Klionsky D.J.;
RT "Mitophagy in yeast occurs through a selective mechanism.";
RL J. Biol. Chem. 283:32386-32393(2008).
RN [26]
RP SUBCELLULAR LOCATION, AND TRAFFICKING.
RX PubMed=18287533; DOI=10.1091/mbc.e07-09-0892;
RA Monastyrska I., He C., Geng J., Hoppe A.D., Li Z., Klionsky D.J.;
RT "Arp2 links autophagic machinery with the actin cytoskeleton.";
RL Mol. Biol. Cell 19:1962-1975(2008).
RN [27]
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 [28]
RP FUNCTION.
RX PubMed=18829864; DOI=10.1091/mbc.e08-05-0544;
RA He C., Baba M., Cao Y., Klionsky D.J.;
RT "Self-interaction is critical for Atg9 transport and function at the
RT phagophore assembly site during autophagy.";
RL Mol. Biol. Cell 19:5506-5516(2008).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [30]
RP INTERACTION WITH ATG11 AND ATG17, AND SUBCELLULAR LOCATION.
RX PubMed=19371383; DOI=10.1111/j.1365-2443.2009.01299.x;
RA Sekito T., Kawamata T., Ichikawa R., Suzuki K., Ohsumi Y.;
RT "Atg17 recruits Atg9 to organize the pre-autophagosomal structure.";
RL Genes Cells 14:525-538(2009).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND SER-144, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [32]
RP SUBCELLULAR LOCATION, TRAFFICKING, AND INTERACTION WITH COG3 AND COG4.
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 [33]
RP SUBCELLULAR LOCATION, AND TRAFFICKING.
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 [34]
RP SUBCELLULAR LOCATION, AND TRAFFICKING.
RX PubMed=20444978; DOI=10.1091/mbc.e09-11-0969;
RA Geng J., Nair U., Yasumura-Yorimitsu K., Klionsky D.J.;
RT "Post-Golgi Sec proteins are required for autophagy in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 21:2257-2269(2010).
RN [35]
RP SUBCELLULAR LOCATION, AND TRAFFICKING.
RX PubMed=20444982; DOI=10.1091/mbc.e09-04-0345;
RA van der Vaart A., Griffith J., Reggiori F.;
RT "Exit from the Golgi is required for the expansion of the autophagosomal
RT phagophore in yeast Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 21:2270-2284(2010).
RN [36]
RP SUBCELLULAR LOCATION, AND TRAFFICKING.
RX PubMed=20861302; DOI=10.1091/mbc.e10-05-0457;
RA Ohashi Y., Munro S.;
RT "Membrane delivery to the yeast autophagosome from the Golgi-endosomal
RT system.";
RL Mol. Biol. Cell 21:3998-4008(2010).
RN [37]
RP SUBCELLULAR LOCATION, AND TRAFFICKING.
RX PubMed=21784249; DOI=10.1016/j.cell.2011.06.022;
RA Nair U., Jotwani A., Geng J., Gammoh N., Richerson D., Yen W.L.,
RA Griffith J., Nag S., Wang K., Moss T., Baba M., McNew J.A., Jiang X.,
RA Reggiori F., Melia T.J., Klionsky D.J.;
RT "SNARE proteins are required for macroautophagy.";
RL Cell 146:290-302(2011).
RN [38]
RP SUBCELLULAR LOCATION, AND TRAFFICKING.
RX PubMed=21576396; DOI=10.1083/jcb.201102092;
RA Mao K., Wang K., Zhao M., Xu T., Klionsky D.J.;
RT "Two MAPK-signaling pathways are required for mitophagy in Saccharomyces
RT cerevisiae.";
RL J. Cell Biol. 193:755-767(2011).
RN [39]
RP SUBCELLULAR LOCATION, AND TRAFFICKING.
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 [40]
RP SUBCELLULAR LOCATION, AND TRAFFICKING.
RX PubMed=22447937; DOI=10.1074/jbc.m112.344952;
RA Umekawa M., Klionsky D.J.;
RT "Ksp1 kinase regulates autophagy via the target of rapamycin complex 1
RT (TORC1) pathway.";
RL J. Biol. Chem. 287:16300-16310(2012).
RN [41]
RP SUBCELLULAR LOCATION, AND TRAFFICKING.
RX PubMed=22977244; DOI=10.1074/jbc.m112.371591;
RA Wang K., Yang Z., Liu X., Mao K., Nair U., Klionsky D.J.;
RT "Phosphatidylinositol 4-kinases are required for autophagic membrane
RT trafficking.";
RL J. Biol. Chem. 287:37964-37972(2012).
RN [42]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH TRS85.
RX PubMed=23129774; DOI=10.1074/jbc.m112.411454;
RA Kakuta S., Yamamoto H., Negishi L., Kondo-Kakuta C., Hayashi N., Ohsumi Y.;
RT "Atg9 vesicles recruit vesicle-tethering proteins Trs85 and Ypt1 to the
RT autophagosome formation site.";
RL J. Biol. Chem. 287:44261-44269(2012).
RN [43]
RP SUBCELLULAR LOCATION, TRAFFICKING, AND FUNCTION.
RX PubMed=22826123; DOI=10.1083/jcb.201202061;
RA Yamamoto H., Kakuta S., Watanabe T.M., Kitamura A., Sekito T.,
RA Kondo-Kakuta C., Ichikawa R., Kinjo M., Ohsumi Y.;
RT "Atg9 vesicles are an important membrane source during early steps of
RT autophagosome formation.";
RL J. Cell Biol. 198:219-233(2012).
RN [44]
RP SUBCELLULAR LOCATION.
RX PubMed=22509044; DOI=10.1073/pnas.1121299109;
RA Lipatova Z., Belogortseva N., Zhang X.Q., Kim J., Taussig D., Segev N.;
RT "Regulation of selective autophagy onset by a Ypt/Rab GTPase module.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:6981-6986(2012).
RN [45]
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 [46]
RP PHOSPHORYLATION BY ATG1, SUBCELLULAR LOCATION, INTERACTION WITH ATG18, AND
RP FUNCTION.
RX PubMed=24905091; DOI=10.4161/auto.28971;
RA Papinski D., Kraft C.;
RT "Atg1 kinase organizes autophagosome formation by phosphorylating Atg9.";
RL Autophagy 10:1338-1340(2014).
RN [47]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATG18, PHOSPHORYLATION AT
RP SER-19; SER-657; SER-802; THR-804; SER-831; SER-842; SER-948 AND SER-969,
RP AND MUTAGENESIS OF SER-19; SER-657; SER-802; THR-804; SER-831; SER-842;
RP SER-948 AND SER-969.
RX PubMed=24440502; DOI=10.1016/j.molcel.2013.12.011;
RA Papinski D., Schuschnig M., Reiter W., Wilhelm L., Barnes C.A.,
RA Maiolica A., Hansmann I., Pfaffenwimmer T., Kijanska M., Stoffel I.,
RA Lee S.S., Brezovich A., Lou J.H., Turk B.E., Aebersold R., Ammerer G.,
RA Peter M., Kraft C.;
RT "Early steps in autophagy depend on direct phosphorylation of Atg9 by the
RT Atg1 kinase.";
RL Mol. Cell 53:471-483(2014).
RN [48]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ATG41.
RX PubMed=26565778; DOI=10.1080/15548627.2015.1107692;
RA Yao Z., Delorme-Axford E., Backues S.K., Klionsky D.J.;
RT "Atg41/Icy2 regulates autophagosome formation.";
RL Autophagy 11:2288-2299(2015).
RN [49]
RP FUNCTION, INDUCTION BY ATG23 AND ATG27, PHOSPHORYLATION AT SER-122;
RP SER-864; SER-792 AND THR-794, AND MUTAGENESIS OF SER-122.
RX PubMed=27050455; DOI=10.1080/15548627.2016.1157237;
RA Feng Y., Backues S.K., Baba M., Heo J.M., Harper J.W., Klionsky D.J.;
RT "Phosphorylation of Atg9 regulates movement to the phagophore assembly site
RT and the rate of autophagosome formation.";
RL Autophagy 12:648-658(2016).
RN [50]
RP INTERACTION WITH ATG11.
RX PubMed=31356628; DOI=10.1371/journal.pbio.3000377;
RA Matscheko N., Mayrhofer P., Rao Y., Beier V., Wollert T.;
RT "Atg11 tethers Atg9 vesicles to initiate selective autophagy.";
RL PLoS Biol. 17:e3000377-e3000377(2019).
RN [51]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 325-GLU--ASN-329; PHE-385;
RP LYS-389; GLN-392; 497-TRP--LEU-501; LEU-545; ARG-560; GLN-576;
RP 640-THR--GLU-645; 661-TYR--SER-670; 678-GLN--PHE-683; ARG-723 AND
RP 761-GLU--PHE-775.
RX PubMed=33106658; DOI=10.1038/s41594-020-00518-w;
RA Matoba K., Kotani T., Tsutsumi A., Tsuji T., Mori T., Noshiro D.,
RA Sugita Y., Nomura N., Iwata S., Ohsumi Y., Fujimoto T., Nakatogawa H.,
RA Kikkawa M., Noda N.N.;
RT "Atg9 is a lipid scramblase that mediates autophagosomal membrane
RT expansion.";
RL Nat. Struct. Mol. Biol. 27:1185-1193(2020).
RN [52]
RP FUNCTION.
RX PubMed=32883836; DOI=10.1126/science.aaz7714;
RA Sawa-Makarska J., Baumann V., Coudevylle N., von Buelow S., Nogellova V.,
RA Abert C., Schuschnig M., Graef M., Hummer G., Martens S.;
RT "Reconstitution of autophagosome nucleation defines Atg9 vesicles as seeds
RT for membrane formation.";
RL Science 369:0-0(2020).
RN [53]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33439214; DOI=10.1083/jcb.202009194;
RA Orii M., Tsuji T., Ogasawara Y., Fujimoto T.;
RT "Transmembrane phospholipid translocation mediated by Atg9 is involved in
RT autophagosome formation.";
RL J. Cell Biol. 220:0-0(2021).
RN [54]
RP UBIQUITINATION AT LYS-113; LYS-121; LYS-138 AND LYS-701, PHOSPHORYLATION AT
RP SER-122, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-113; LYS-121;
RP SER-122; LYS-138 AND LYS-701.
RX PubMed=33443148; DOI=10.1073/pnas.2005539118;
RA Feng Y., Ariosa A.R., Yang Y., Hu Z., Dengjel J., Klionsky D.J.;
RT "Downregulation of autophagy by Met30-mediated Atg9 ubiquitination.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm
CC to vacuole transport (Cvt) vesicle formation (PubMed:7593182,
CC PubMed:8224160, PubMed:8663607, PubMed:10735854, PubMed:14504273,
CC PubMed:24440502, PubMed:27050455, PubMed:33106658, PubMed:33439214).
CC Cycles between the preautophagosomal structure/phagophore assembly site
CC (PAS) and the cytoplasmic vesicle pool and supplies membrane for the
CC growing autophagosome (PubMed:10662773, PubMed:11689437,
CC PubMed:17329962, PubMed:17426440, PubMed:18829864, PubMed:22826123,
CC PubMed:24905091, PubMed:33439214). Lipid scramblase activity plays a
CC key role in preautophagosomal structure/phagophore assembly by
CC distributing the phospholipids that arrive through ATG2 from the
CC cytoplasmic to the luminal leaflet of the bilayer, thereby driving
CC autophagosomal membrane expansion (PubMed:33106658, PubMed:32883836,
CC PubMed:33439214). Required for mitophagy (PubMed:18818209). Also
CC involved in endoplasmic reticulum-specific autophagic process and is
CC essential for the survival of cells subjected to severe ER stress
CC (PubMed:17132049). Recruits vesicle-tethering proteins TRS85 and YPT1
CC to the autophagosome formation site (PubMed:23129774). Recruits also
CC ATG23 and ATG8 to the PAS (PubMed:14504273).
CC {ECO:0000269|PubMed:10662773, ECO:0000269|PubMed:10735854,
CC ECO:0000269|PubMed:11689437, ECO:0000269|PubMed:14504273,
CC ECO:0000269|PubMed:17132049, ECO:0000269|PubMed:17329962,
CC ECO:0000269|PubMed:17426440, ECO:0000269|PubMed:18818209,
CC ECO:0000269|PubMed:18829864, ECO:0000269|PubMed:22826123,
CC ECO:0000269|PubMed:23129774, ECO:0000269|PubMed:24440502,
CC ECO:0000269|PubMed:24905091, ECO:0000269|PubMed:27050455,
CC ECO:0000269|PubMed:32883836, ECO:0000269|PubMed:33106658,
CC ECO:0000269|PubMed:33439214, ECO:0000269|PubMed:7593182,
CC ECO:0000269|PubMed:8224160, ECO:0000269|PubMed:8663607}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:33106658,
CC ECO:0000269|PubMed:33439214};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000269|PubMed:33106658,
CC ECO:0000269|PubMed:33439214};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:33106658};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-
CC 3-phosphate)(out); Xref=Rhea:RHEA:67920, ChEBI:CHEBI:58088;
CC Evidence={ECO:0000269|PubMed:33106658};
CC -!- SUBUNIT: Homotrimer; forms a homotrimer with a central pore that forms
CC a path between the two membrane leaflets (PubMed:33106658). Interacts
CC with ATG23 and ATG27 to form a cycling complex for trafficking to the
CC PAS (PubMed:14504273, PubMed:17178909, PubMed:27050455). Interacts (via
CC N-terminus) with ATG11, required for recruitment of ATG9 to the PAS for
CC the Cvt pathway during nutrient-rich conditions (PubMed:17178909,
CC PubMed:17192412, PubMed:19371383, PubMed:31356628). Interacts (via N-
CC terminus) with ATG17; required for recruitment to the PAS during
CC autophagy and starved conditions (PubMed:19371383). Interacts with ATG2
CC and ATG18; required for the retrieval of ATG9 from the PAS to the
CC cytoplasmic pool (PubMed:11382760, PubMed:14723849, PubMed:24905091,
CC PubMed:24440502). Interacts with ATG41 (PubMed:26565778). Interacts
CC with the conserved oligomeric Golgi (COG) complex subunits COG3 and
CC COG4 (PubMed:20065092). Interacts with TRS85 (PubMed:23129774).
CC {ECO:0000269|PubMed:11382760, ECO:0000269|PubMed:14504273,
CC ECO:0000269|PubMed:14723849, ECO:0000269|PubMed:17178909,
CC ECO:0000269|PubMed:17192412, ECO:0000269|PubMed:18829864,
CC ECO:0000269|PubMed:19371383, ECO:0000269|PubMed:20065092,
CC ECO:0000269|PubMed:23129774, ECO:0000269|PubMed:24440502,
CC ECO:0000269|PubMed:24905091, ECO:0000269|PubMed:26565778,
CC ECO:0000269|PubMed:27050455, ECO:0000269|PubMed:31356628,
CC ECO:0000269|PubMed:33106658}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:14723849, ECO:0000269|PubMed:15138258,
CC ECO:0000269|PubMed:16874040, ECO:0000269|PubMed:17135291,
CC ECO:0000269|PubMed:17295840, ECO:0000269|PubMed:17426440,
CC ECO:0000269|PubMed:18625846, ECO:0000269|PubMed:19371383,
CC ECO:0000269|PubMed:20065092, ECO:0000269|PubMed:22447937,
CC ECO:0000269|PubMed:23129774, ECO:0000269|PubMed:24440502,
CC ECO:0000269|PubMed:24905091, ECO:0000269|PubMed:33443148,
CC ECO:0000305|PubMed:10662773}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16847258}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:10735854, ECO:0000269|PubMed:14723849}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16847258}. Golgi apparatus
CC membrane {ECO:0000269|PubMed:17135291}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16847258}. Endoplasmic reticulum membrane; Multi-
CC pass membrane protein {ECO:0000269|PubMed:16847258}. Mitochondrion
CC membrane {ECO:0000269|PubMed:16787937, ECO:0000269|PubMed:16874040,
CC ECO:0000269|PubMed:17135291}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16847258}. Note=The vast majority of ATG9 exists on
CC cytoplasmic mobile vesicles (designated ATG9 vesicles) that were
CC derived from the Golgi apparatus in a process involving ATG23 and ATG27
CC (PubMed:22826123, PubMed:22509044). The peripheral pool of ATG9
CC partially colocalizes within tubulovesicular clusters adjacent to
CC mitochondria (PubMed:20855505, PubMed:26565778). It appears that
CC membrane that contains ATG9 is delivered to the autophagosome from the
CC Golgi-endosomal system rather than from the ER or mitochondria
CC (PubMed:20444982, PubMed:20861302). Within the PAS, localizes at the
CC edge of the isolation membrane (PubMed:22144692, PubMed:23549786). ATG9
CC cycling is regulated by at least the conserved oligomeric Golgi (COG)
CC complex, ARP2, HOG1, PIK1, SEC2, SEC9, SSO1 and SSO2 (PubMed:18287533,
CC PubMed:20444978, PubMed:21784249, PubMed:21576396, PubMed:22977244).
CC {ECO:0000269|PubMed:18287533, ECO:0000269|PubMed:20444978,
CC ECO:0000269|PubMed:20444982, ECO:0000269|PubMed:20855505,
CC ECO:0000269|PubMed:20861302, ECO:0000269|PubMed:21576396,
CC ECO:0000269|PubMed:21784249, ECO:0000269|PubMed:22144692,
CC ECO:0000269|PubMed:22509044, ECO:0000269|PubMed:22826123,
CC ECO:0000269|PubMed:22977244, ECO:0000269|PubMed:23549786,
CC ECO:0000269|PubMed:26565778}.
CC -!- DOMAIN: Forms a homotrimer with a solvated central pore, which is
CC connected laterally to the cytosol through the cavity within each
CC protomer (By similarity). Acts as a lipid scramblase that uses its
CC central pore to function: the central pore opens laterally to
CC accommodate lipid headgroups, thereby enabling lipid flipping and
CC redistribution of lipids added to the outer leaflet of ATG9-containing
CC vesicles, thereby enabling growth into autophagosomes (By similarity).
CC {ECO:0000250|UniProtKB:O74312}.
CC -!- PTM: Phosphorylated by ATG1; phosphorylation is required for autophagy
CC and cytoplasm to vacuole transport (Cvt) vesicle formation
CC (PubMed:24440502). Phosphorylation by ATG1 regulates ATG18 interaction
CC and preautophagosome elongation (PubMed:24905091). Phosphorylation at
CC Ser-122 is required for selective autophagy by regulating anterograde
CC trafficking and interaction with ATG23 and ATG27 (PubMed:27050455,
CC PubMed:33443148). Phosphorylation at Ser-122 prevents ubiquitination by
CC the SCF(MET30) complex (PubMed:33443148). {ECO:0000269|PubMed:24440502,
CC ECO:0000269|PubMed:24905091, ECO:0000269|PubMed:27050455,
CC ECO:0000269|PubMed:33443148}.
CC -!- PTM: Ubiquitinated by the SCF(MET30) complex in normal conditions,
CC leading to its degradation by the proteasome, thereby preventing
CC inappropriate induction of autophagy (PubMed:33443148). Ubiquitination
CC by the SCF(MET30) complex is prevented by phosphorylation at Ser-122
CC (PubMed:33443148). {ECO:0000269|PubMed:33443148}.
CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000305}.
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DR EMBL; X97751; CAA66342.1; -; Genomic_DNA.
DR EMBL; Z74197; CAA98723.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11709.1; -; Genomic_DNA.
DR PIR; S67697; S67697.
DR RefSeq; NP_010132.1; NM_001180209.1.
DR AlphaFoldDB; Q12142; -.
DR SMR; Q12142; -.
DR BioGRID; 31912; 269.
DR DIP; DIP-1938N; -.
DR IntAct; Q12142; 11.
DR MINT; Q12142; -.
DR STRING; 4932.YDL149W; -.
DR TCDB; 9.A.15.1.1; the autophagy-related phagophore-formation transporter (apt) family.
DR TCDB; 9.A.79.1.1; the autophagosomal phospholipid transmembrane translocase (atg9) family.
DR iPTMnet; Q12142; -.
DR MaxQB; Q12142; -.
DR PaxDb; Q12142; -.
DR PRIDE; Q12142; -.
DR EnsemblFungi; YDL149W_mRNA; YDL149W; YDL149W.
DR GeneID; 851406; -.
DR KEGG; sce:YDL149W; -.
DR SGD; S000002308; ATG9.
DR VEuPathDB; FungiDB:YDL149W; -.
DR eggNOG; KOG2173; Eukaryota.
DR GeneTree; ENSGT00390000014839; -.
DR HOGENOM; CLU_006200_1_0_1; -.
DR InParanoid; Q12142; -.
DR OMA; LGYVCKY; -.
DR BioCyc; YEAST:G3O-29546-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR PRO; PR:Q12142; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12142; protein.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0061908; C:phagophore; IDA:SGD.
DR GO; GO:0000407; C:phagophore assembly site; IDA:UniProtKB.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017128; F:phospholipid scramblase activity; IDA:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IDA:UniProtKB.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0044805; P:late 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:0061709; P:reticulophagy; IMP:SGD.
DR InterPro; IPR007241; Autophagy-rel_prot_9.
DR PANTHER; PTHR13038; PTHR13038; 1.
DR Pfam; PF04109; ATG9; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasmic vesicle; Endoplasmic reticulum; Golgi apparatus;
KW Isopeptide bond; Lipid transport; Membrane; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..997
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000119839"
FT TOPO_DOM 1..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..376
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 539..559
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 560..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..656
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 657..677
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 678..723
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 724..744
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 745..997
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT REGION 29..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine; by ATG1"
FT /evidence="ECO:0000269|PubMed:24440502"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27050455,
FT ECO:0000269|PubMed:33443148"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 657
FT /note="Phosphoserine; by ATG1"
FT /evidence="ECO:0000269|PubMed:24440502"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27050455"
FT MOD_RES 794
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27050455"
FT MOD_RES 802
FT /note="Phosphoserine; by ATG1"
FT /evidence="ECO:0000269|PubMed:24440502"
FT MOD_RES 804
FT /note="Phosphothreonine; by ATG1"
FT /evidence="ECO:0000269|PubMed:24440502"
FT MOD_RES 831
FT /note="Phosphoserine; by ATG1"
FT /evidence="ECO:0000269|PubMed:24440502"
FT MOD_RES 842
FT /note="Phosphoserine; by ATG1"
FT /evidence="ECO:0000269|PubMed:24440502"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:27050455"
FT MOD_RES 948
FT /note="Phosphoserine; by ATG1"
FT /evidence="ECO:0000269|PubMed:24440502"
FT MOD_RES 969
FT /note="Phosphoserine; by ATG1"
FT /evidence="ECO:0000269|PubMed:24440502"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:33443148"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:33443148"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:33443148"
FT CROSSLNK 701
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:33443148"
FT MUTAGEN 19
FT /note="S->A: Abolished autophagy and cytoplasm to vacuole
FT transport (Cvt) vesicle formation; when associated with A-
FT 657, A-802, A-804, A-831, A-842, A-948 and A-969."
FT /evidence="ECO:0000269|PubMed:24440502"
FT MUTAGEN 113
FT /note="K->R: Abolished ubiquitination by the SCF(MET30)
FT complex and subsequent degradation; when associated with R-
FT 121 and R-138."
FT /evidence="ECO:0000269|PubMed:33443148"
FT MUTAGEN 121
FT /note="K->R: Abolished ubiquitination by the SCF(MET30)
FT complex and subsequent degradation; when associated with R-
FT 113 and R-138."
FT /evidence="ECO:0000269|PubMed:33443148"
FT MUTAGEN 122
FT /note="S->A: Impaired selective autophagy. Does not affect
FT ubiquitination by the SCF(MET30) complex."
FT /evidence="ECO:0000269|PubMed:27050455,
FT ECO:0000269|PubMed:33443148"
FT MUTAGEN 122
FT /note="S->D: Phospho-mimetic mutant; increased selective
FT autophagy. Prevents ubiquitination by the SCF(MET30)
FT complex."
FT /evidence="ECO:0000269|PubMed:27050455,
FT ECO:0000269|PubMed:33443148"
FT MUTAGEN 138
FT /note="K->R: Abolished ubiquitination by the SCF(MET30)
FT complex and subsequent degradation; when associated with R-
FT 113 and R-121."
FT /evidence="ECO:0000269|PubMed:33443148"
FT MUTAGEN 192
FT /note="H->L: Abolishes interaction with ATG11 and disrupts
FT Cvt, but not bulk autophagy."
FT /evidence="ECO:0000269|PubMed:17178909"
FT MUTAGEN 325..329
FT /note="EKILN->AAILA: In Middle mutant; impaired autophagy."
FT /evidence="ECO:0000269|PubMed:33106658"
FT MUTAGEN 385
FT /note="F->A: In Entrance 1 mutant; does not affect
FT autophagy; when associated with S-545."
FT /evidence="ECO:0000269|PubMed:33106658"
FT MUTAGEN 389
FT /note="K->A: In Entrance 2 mutant; does not affect
FT autophagy."
FT /evidence="ECO:0000269|PubMed:33106658"
FT MUTAGEN 392
FT /note="Q->A: In Entrance 3 mutant; impaired autophagy
FT possibly caused by mislocalization; when associated with
FT 497-A--A-501."
FT /evidence="ECO:0000269|PubMed:33106658"
FT MUTAGEN 497..501
FT /note="WNINL->ANINA: In Entrance 3 mutant; impaired
FT autophagy possibly caused by mislocalization; when
FT associated with A-392."
FT /evidence="ECO:0000269|PubMed:33106658"
FT MUTAGEN 545
FT /note="L->S: In Entrance 1 mutant; does not affect
FT autophagy; when associated with A-385."
FT /evidence="ECO:0000269|PubMed:33106658"
FT MUTAGEN 560
FT /note="R->A: In Basic mutant; impaired autophagy; when
FT associated with A-576 and A-723."
FT /evidence="ECO:0000269|PubMed:33106658"
FT MUTAGEN 576
FT /note="Q->A: In Basic mutant; impaired autophagy; when
FT associated with A-560 and A-723."
FT /evidence="ECO:0000269|PubMed:33106658"
FT MUTAGEN 640..645
FT /note="TVFDPE->AVFAAA: In Acidic mutant; abolished
FT autophagy caused by defects in phospholipid scramblase
FT activity."
FT /evidence="ECO:0000269|PubMed:33106658"
FT MUTAGEN 657
FT /note="S->A: Abolished autophagy and cytoplasm to vacuole
FT transport (Cvt) vesicle formation; when associated with A-
FT 19, A-802, A-804, A-831, A-842, A-948 and A-969."
FT /evidence="ECO:0000269|PubMed:24440502"
FT MUTAGEN 661..670
FT /note="YITILGAIWS->AIAILAAIWA: In Wall mutant; abolished
FT autophagy caused by defects in phospholipid scramblase
FT activity."
FT /evidence="ECO:0000269|PubMed:33106658"
FT MUTAGEN 678..683
FT /note="QEYHVF->AAHVA: In Junction mutant; does not affect
FT autophagy."
FT /evidence="ECO:0000269|PubMed:33106658"
FT MUTAGEN 701
FT /note="K->R: Does not affect ubiquitination by the
FT SCF(MET30) complex and subsequent degradation."
FT /evidence="ECO:0000269|PubMed:33443148"
FT MUTAGEN 723
FT /note="R->A: In Basic mutant; impaired autophagy; when
FT associated with A-560 and A-576."
FT /evidence="ECO:0000269|PubMed:33106658"
FT MUTAGEN 761..775
FT /note="EYVDGLGYVCKYAMF->AAVDGLGYVCKYAAA: In Hexamer mutant;
FT does not affect autophagy."
FT /evidence="ECO:0000269|PubMed:33106658"
FT MUTAGEN 802
FT /note="S->A: Abolished autophagy and cytoplasm to vacuole
FT transport (Cvt) vesicle formation; when associated with A-
FT 19, A-657, A-804, A-831, A-842, A-948 and A-969."
FT /evidence="ECO:0000269|PubMed:24440502"
FT MUTAGEN 804
FT /note="T->A: Abolished autophagy and cytoplasm to vacuole
FT transport (Cvt) vesicle formation; when associated with A-
FT 19, A-657, A-802, A-831, A-842, A-948 and A-969."
FT /evidence="ECO:0000269|PubMed:24440502"
FT MUTAGEN 831
FT /note="S->A: Abolished autophagy and cytoplasm to vacuole
FT transport (Cvt) vesicle formation; when associated with A-
FT 19, A-657, A-802, A-804, A-842, A-948 and A-969."
FT /evidence="ECO:0000269|PubMed:24440502"
FT MUTAGEN 842
FT /note="S->A: Abolished autophagy and cytoplasm to vacuole
FT transport (Cvt) vesicle formation; when associated with A-
FT 19, A-657, A-802, A-804, A-831, A-948 and A-969."
FT /evidence="ECO:0000269|PubMed:24440502"
FT MUTAGEN 948
FT /note="S->A: Abolished autophagy and cytoplasm to vacuole
FT transport (Cvt) vesicle formation; when associated with A-
FT 19, A-657, A-802, A-804, A-831, A-842 and A-969."
FT /evidence="ECO:0000269|PubMed:24440502"
FT MUTAGEN 969
FT /note="S->A: Abolished autophagy and cytoplasm to vacuole
FT transport (Cvt) vesicle formation; when associated with A-
FT 19, A-657, A-802, A-804, A-831 and A-842."
FT /evidence="ECO:0000269|PubMed:24440502"
SQ SEQUENCE 997 AA; 115403 MW; E900AD5E3AC5D111 CRC64;
MERDEYQLPN SHGKNTFLSR IFGLQSDEVN PSLNSQEMSN FPLPDIERGS SLLHSTNDSR
EDVDENDLRV PESDQGTSTE EEDEVDEEQV QAYAPQISDG LDGDHQLNSV TSKENVLETE
KSNLERLVEG STDDSVPKVG QLSSEEEEDN EFINNDGFDD DTPLFQKSKI HEFSSKKSNT
IEDGKRPLFF RHILQNNRPQ RDTQKLFTSS NAIHHDKDKS ANNGPRNING NQKHGTKYFG
SATQPRFTGS PLNNTNRFTK LFPLRKPNLL SNISVLNNTP EDRINTLSVK ERALWKWANV
ENLDIFLQDV YNYYLGNGFY CIILEKILNI CTLLFVVFVS TYMGHCVDYS KLPTSHRVSD
IIIDKCYSNS ITGFTKFFLW MFYFFVILKI VQLYFDVQKL SELQNFYKYL LNISDDELQT
LPWQNVIQQL MYLKDQNAMT ANVVEVKAKN RIDAHDVANR IMRRENYLIA LYNSDILNLS
LPIPLFRTNV LTKTLEWNIN LCVMGFVFNE SGFIKQSILK PSQREFTREE LQKRFMLAGF
LNIILAPFLV TYFVLLYFFR YFNEYKTSPG SIGARQYTPI AEWKFREYNE LYHIFKKRIS
LSTTLANKYV DQFPKEKTNL FLKFVSFICG SFVAILAFLT VFDPENFLNF EITSDRSVIF
YITILGAIWS VSRNTITQEY HVFDPEETLK ELYEYTHYLP KEWEGRYHKE EIKLEFCKLY
NLRIVILLRE LTSLMITPFV LWFSLPSSAG RIVDFFRENS EYVDGLGYVC KYAMFNMKNI
DGEDTHSMDE DSLTKKIAVN GSHTLNSKRR SKFTAEDHSD KDLANNKMLQ SYVYFMDDYS
NSENLTGKYQ LPAKKGYPNN EGDSFLNNKY SWRKQFQPGQ KPELFRIGKH ALGPGHNISP
AIYSTRNPGK NWDNNNNGDD IKNGTNNATA KNDDNNGNND HEYVLTESFL DSGAFPNHDV
IDHNKMLNSN YNGNGILNKG GVLGLVKEYY KKSDVGR
