ATG11_YEAST
ID ATG11_YEAST Reviewed; 1178 AA.
AC Q12527; D6W457;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Autophagy-related protein 11;
DE AltName: Full=Cytoplasm to vacuole targeting protein 9;
GN Name=ATG11; Synonyms=CVT9; OrderedLocusNames=YPR049C; ORFNames=YP9499.07c;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND INTERACTION WITH ATG1.
RX PubMed=10995454; DOI=10.1083/jcb.150.6.1507;
RA Kamada Y., Funakoshi T., Shintani T., Nagano K., Ohsumi M., Ohsumi Y.;
RT "Tor-mediated induction of autophagy via an Apg1 protein kinase complex.";
RL J. Cell Biol. 150:1507-1513(2000).
RN [5]
RP FUNCTION.
RX PubMed=11264288; DOI=10.1074/jbc.m101150200;
RA Hutchins M.U., Klionsky D.J.;
RT "Vacuolar localization of oligomeric alpha-mannosidase requires the
RT cytoplasm to vacuole targeting and autophagy pathway components in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 276:20491-20498(2001).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11309418; DOI=10.1083/jcb.153.2.381;
RA Kim J., Kamada Y., Stromhaug P.E., Guan J., Hefner-Gravink A., Baba M.,
RA Scott S.V., Ohsumi Y., Dunn W.A. Jr., Klionsky D.J.;
RT "Cvt9/Gsa9 functions in sequestering selective cytosolic cargo destined for
RT the vacuole.";
RL J. Cell Biol. 153:381-396(2001).
RN [7]
RP FUNCTION, AND 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 [8]
RP SUBCELLULAR LOCATION.
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 [9]
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 [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
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 [12]
RP FUNCTION.
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 [13]
RP SUBCELLULAR LOCATION, INTERACTION WITH ATG17; ATG19 AND ATG20, AND
RP FUNCTION.
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 [14]
RP FUNCTION.
RX PubMed=16901900; DOI=10.1074/jbc.m607007200;
RA Yorimitsu T., Nair U., Yang Z., Klionsky D.J.;
RT "Endoplasmic reticulum stress triggers autophagy.";
RL J. Biol. Chem. 281:30299-30304(2006).
RN [15]
RP FUNCTION, AND INTERACTION WITH ATG9.
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 [16]
RP FUNCTION.
RX PubMed=17012830; DOI=10.4161/auto.3371;
RA Cao Y., Klionsky D.J.;
RT "Atg26 is not involved in autophagy-related pathways in Saccharomyces
RT cerevisiae.";
RL Autophagy 3:17-20(2007).
RN [17]
RP FUNCTION.
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 [18]
RP FUNCTION, AND INTERACTION WITH ATG9.
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 [19]
RP FUNCTION.
RX PubMed=18497569; DOI=10.4161/auto.6308;
RA Ma J., Bharucha N., Dobry C.J., Frisch R.L., Lawson S., Kumar A.;
RT "Localization of autophagy-related proteins in yeast using a versatile
RT plasmid-based resource of fluorescent protein fusions.";
RL Autophagy 4:792-800(2008).
RN [20]
RP SUBCELLULAR LOCATION, AND FUNCTION.
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 [21]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [22]
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 [23]
RP FUNCTION.
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 [24]
RP FUNCTION.
RX PubMed=18287526; DOI=10.1091/mbc.e07-10-1048;
RA Kawamata T., Kamada Y., Kabeya Y., Sekito T., Ohsumi Y.;
RT "Organization of the pre-autophagosomal structure responsible for
RT autophagosome formation.";
RL Mol. Biol. Cell 19:2039-2050(2008).
RN [25]
RP FUNCTION.
RX PubMed=18701704; DOI=10.1091/mbc.e08-04-0363;
RA Krick R., Muehe Y., Prick T., Bremer S., Schlotterhose P., Eskelinen E.L.,
RA Millen J., Goldfarb D.S., Thumm M.;
RT "Piecemeal microautophagy of the nucleus requires the core macroautophagy
RT genes.";
RL Mol. Biol. Cell 19:4492-4505(2008).
RN [26]
RP IDENTIFICATION BY 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 [27]
RP FUNCTION.
RX PubMed=19061865; DOI=10.1016/j.bbrc.2008.11.084;
RA Kageyama T., Suzuki K., Ohsumi Y.;
RT "Lap3 is a selective target of autophagy in yeast, Saccharomyces
RT cerevisiae.";
RL Biochem. Biophys. Res. Commun. 378:551-557(2009).
RN [28]
RP ACETYLATION BY NUA4.
RX PubMed=19303850; DOI=10.1016/j.cell.2009.01.033;
RA Lin Y.Y., Lu J.Y., Zhang J., Walter W., Dang W., Wan J., Tao S.C., Qian J.,
RA Zhao Y., Boeke J.D., Berger S.L., Zhu H.;
RT "Protein acetylation microarray reveals that NuA4 controls key metabolic
RT target regulating gluconeogenesis.";
RL Cell 136:1073-1084(2009).
RN [29]
RP FUNCTION, AND 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 [30]
RP FUNCTION, AND INTERACTION WITH ATG32.
RX PubMed=19619495; DOI=10.1016/j.devcel.2009.06.014;
RA Kanki T., Wang K., Cao Y., Baba M., Klionsky D.J.;
RT "Atg32 is a mitochondrial protein that confers selectivity during
RT mitophagy.";
RL Dev. Cell 17:98-109(2009).
RN [31]
RP FUNCTION, AND INTERACTION WITH ATG9.
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 [32]
RP FUNCTION.
RX PubMed=20647741; DOI=10.4161/auto.6.7.12753;
RA Ecker N., Mor A., Journo D., Abeliovich H.;
RT "Induction of autophagic flux by amino acid deprivation is distinct from
RT nitrogen starvation-induced macroautophagy.";
RL Autophagy 6:879-890(2010).
RN [33]
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 [34]
RP FUNCTION.
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 [35]
RP FUNCTION.
RX PubMed=21343297; DOI=10.1074/jbc.m110.173906;
RA Yuga M., Gomi K., Klionsky D.J., Shintani T.;
RT "Aspartyl aminopeptidase is imported from the cytoplasm to the vacuole by
RT selective autophagy in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 286:13704-13713(2011).
RN [36]
RP FUNCTION.
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 [37]
RP INTERACTION WITH ATG32, AND FUNCTION.
RX PubMed=21757540; DOI=10.1091/mbc.e11-02-0145;
RA Aoki Y., Kanki T., Hirota Y., Kurihara Y., Saigusa T., Uchiumi T., Kang D.;
RT "Phosphorylation of Serine 114 on Atg32 mediates mitophagy.";
RL Mol. Biol. Cell 22:3206-3217(2011).
RN [38]
RP FUNCTION.
RX PubMed=22157017; DOI=10.1074/jbc.m111.280156;
RA Kurihara Y., Kanki T., Aoki Y., Hirota Y., Saigusa T., Uchiumi T., Kang D.;
RT "Mitophagy plays an essential role in reducing mitochondrial production of
RT reactive oxygen species and mutation of mitochondrial DNA by maintaining
RT mitochondrial quantity and quality in yeast.";
RL J. Biol. Chem. 287:3265-3272(2012).
RN [39]
RP FUNCTION, AND INTERACTION WITH ATG32.
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).
RN [40]
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 [41]
RP INTERACTION WITH YPT1, SUBCELLULAR LOCATION, AND FUNCTION.
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 [42]
RP INTERACTION WITH ATG30 AND ATG36, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=23559066; DOI=10.1038/embor.2013.40;
RA Farre J.C., Burkenroad A., Burnett S.F., Subramani S.;
RT "Phosphorylation of mitophagy and pexophagy receptors coordinates their
RT interaction with Atg8 and Atg11.";
RL EMBO Rep. 14:441-449(2013).
RN [43]
RP FUNCTION.
RX PubMed=23337777; DOI=10.1016/j.exger.2013.01.006;
RA Aris J.P., Alvers A.L., Ferraiuolo R.A., Fishwick L.K., Hanvivatpong A.,
RA Hu D., Kirlew C., Leonard M.T., Losin K.J., Marraffini M., Seo A.Y.,
RA Swanberg V., Westcott J.L., Wood M.S., Leeuwenburgh C., Dunn W.A. Jr.;
RT "Autophagy and leucine promote chronological longevity and respiration
RT proficiency during calorie restriction in yeast.";
RL Exp. Gerontol. 48:1107-1119(2013).
RN [44]
RP FUNCTION, AND INTERACTION WITH ATG9.
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).
CC -!- FUNCTION: Involved in cytoplasm to vacuole transport (Cvt), pexophagy,
CC mitophagy and nucleophagy. Recruits mitochondria for their selective
CC degradation via autophagy (mitophagy) during starvation, through its
CC interaction with ATG32. Works as scaffold proteins that recruit ATG
CC proteins to the pre-autophagosome (PAS), the site of
CC vesicle/autophagosome formation. Required for ATG9 anterograde
CC transport from the mitochondria to the PAS. Recruits also the ATG19-
CC prAPE1 complex to the PAS. Required for the Cvt vesicles completion.
CC Plays a significant role in life span extension.
CC {ECO:0000269|PubMed:10995454, ECO:0000269|PubMed:11264288,
CC ECO:0000269|PubMed:11309418, ECO:0000269|PubMed:12479808,
CC ECO:0000269|PubMed:15138258, ECO:0000269|PubMed:15659643,
CC ECO:0000269|PubMed:16901900, ECO:0000269|PubMed:17012830,
CC ECO:0000269|PubMed:17178909, ECO:0000269|PubMed:17192412,
CC ECO:0000269|PubMed:17295840, ECO:0000269|PubMed:18077553,
CC ECO:0000269|PubMed:18287526, ECO:0000269|PubMed:18497569,
CC ECO:0000269|PubMed:18625846, ECO:0000269|PubMed:18701704,
CC ECO:0000269|PubMed:18725539, ECO:0000269|PubMed:18818209,
CC ECO:0000269|PubMed:19061865, ECO:0000269|PubMed:19371383,
CC ECO:0000269|PubMed:19619494, ECO:0000269|PubMed:19619495,
CC ECO:0000269|PubMed:20647741, ECO:0000269|PubMed:20855505,
CC ECO:0000269|PubMed:21343297, ECO:0000269|PubMed:21429936,
CC ECO:0000269|PubMed:21757540, ECO:0000269|PubMed:22157017,
CC ECO:0000269|PubMed:22308029, ECO:0000269|PubMed:22509044,
CC ECO:0000269|PubMed:22768199, ECO:0000269|PubMed:23337777,
CC ECO:0000269|PubMed:23559066, ECO:0000269|PubMed:31356628,
CC ECO:0000269|PubMed:8663607}.
CC -!- SUBUNIT: Homodimer and potential homooligomers. Interacts with ATG1
CC kinase and the ATG19 and ATG34 cargo protein transporters. Interacts
CC with ATG9, ATG17, ATG20, ATG30, ATG32, ATG36 and YPT1.
CC {ECO:0000269|PubMed:10995454, ECO:0000269|PubMed:12479808,
CC ECO:0000269|PubMed:15659643, ECO:0000269|PubMed:17178909,
CC ECO:0000269|PubMed:17192412, ECO:0000269|PubMed:19371383,
CC ECO:0000269|PubMed:19619494, ECO:0000269|PubMed:19619495,
CC ECO:0000269|PubMed:20639194, ECO:0000269|PubMed:21757540,
CC ECO:0000269|PubMed:22308029, ECO:0000269|PubMed:22509044,
CC ECO:0000269|PubMed:23559066, ECO:0000269|PubMed:31356628}.
CC -!- INTERACTION:
CC Q12527; P53104: ATG1; NbExp=3; IntAct=EBI-31977, EBI-2657;
CC Q12527; P35193: ATG19; NbExp=5; IntAct=EBI-31977, EBI-29291;
CC Q12527; P40458: ATG32; NbExp=2; IntAct=EBI-31977, EBI-25256;
CC Q12527; Q12292: ATG34; NbExp=2; IntAct=EBI-31977, EBI-36362;
CC Q12527; Q06159: ATG39; NbExp=2; IntAct=EBI-31977, EBI-33888;
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Peripheral
CC membrane protein. Vacuole membrane; Peripheral membrane protein.
CC Note=During pexophagy, accumulates in the vacuolar membrane region,
CC where the peroxisomes contact the vacuole. ATG11 localization is
CC dependent on ATG11-ATG30 interaction.
CC -!- PTM: Acetylated by the NuA4 histone acetyltransferase (HAT) complex.
CC {ECO:0000269|PubMed:19303850}.
CC -!- MISCELLANEOUS: Present with 86 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATG11 family. {ECO:0000305}.
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DR EMBL; Z71255; CAA94996.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89169.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11473.1; -; Genomic_DNA.
DR PIR; S54073; S54073.
DR RefSeq; NP_015374.1; NM_001184146.1.
DR PDB; 6VZF; X-ray; 2.03 A; A=699-800.
DR PDBsum; 6VZF; -.
DR AlphaFoldDB; Q12527; -.
DR SMR; Q12527; -.
DR BioGRID; 36225; 165.
DR DIP; DIP-1492N; -.
DR IntAct; Q12527; 26.
DR MINT; Q12527; -.
DR STRING; 4932.YPR049C; -.
DR TCDB; 9.A.15.1.1; the autophagy-related phagophore-formation transporter (apt) family.
DR iPTMnet; Q12527; -.
DR MaxQB; Q12527; -.
DR PaxDb; Q12527; -.
DR PRIDE; Q12527; -.
DR EnsemblFungi; YPR049C_mRNA; YPR049C; YPR049C.
DR GeneID; 856162; -.
DR KEGG; sce:YPR049C; -.
DR SGD; S000006253; ATG11.
DR VEuPathDB; FungiDB:YPR049C; -.
DR eggNOG; ENOG502QVZE; Eukaryota.
DR HOGENOM; CLU_272501_0_0_1; -.
DR InParanoid; Q12527; -.
DR OMA; EIDVHYF; -.
DR BioCyc; YEAST:G3O-34204-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR PRO; PR:Q12527; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12527; protein.
DR GO; GO:1990316; C:Atg1/ULK1 kinase complex; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0060090; F:molecular adaptor activity; IGI:SGD.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IDA:SGD.
DR GO; GO:0000045; P:autophagosome assembly; IDA:SGD.
DR GO; GO:0006914; P:autophagy; IDA:SGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0030242; P:autophagy of peroxisome; IMP:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IGI:SGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IDA:SGD.
DR GO; GO:0031503; P:protein-containing complex localization; IMP:SGD.
DR GO; GO:0140255; P:regulation of cellular response to phosphate starvation; IDA:SGD.
DR GO; GO:0061709; P:reticulophagy; IMP:SGD.
DR InterPro; IPR040040; ATG11.
DR InterPro; IPR019460; Atg11_C.
DR InterPro; IPR045326; ATG17-like_dom.
DR PANTHER; PTHR13222; PTHR13222; 1.
DR Pfam; PF10377; ATG11; 1.
DR Pfam; PF04108; ATG17_like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Autophagy; Coiled coil; Membrane;
KW Protein transport; Reference proteome; Transport; Vacuole.
FT CHAIN 1..1178
FT /note="Autophagy-related protein 11"
FT /id="PRO_0000124554"
FT COILED 538..572
FT /evidence="ECO:0000255"
FT COILED 696..850
FT /evidence="ECO:0000255"
FT HELIX 702..783
FT /evidence="ECO:0007829|PDB:6VZF"
SQ SEQUENCE 1178 AA; 135025 MW; A904B92E9AE79449 CRC64;
MADADEYSTA PTQQEITPLQ TTATIINAIS GECITTNVDF FVSLDKFKQF IARKWKIPPD
QLLILLPYGN KLKPSMFKEL LINRSFTLND FYVYDRRLFS LVSKPTPTNL LTSKDSNPMN
SPNSNDLTET LEYLIKNSHI SQYQGSDTIM IKPMPSPLED ADVDLSRLNY HSVTSLLTTN
LGWLSALEID VHYFKSLIPD IIAHIKRIFD GLTVCSQYLK LYCFDVESLY NSNVQFLNQL
VDNGMTSKWE KCFNDTLSKL TALEGDSLQK FINIESLLEN EKSVKILNHS INGKLNKIKR
EIDENASFRD IITVNIDRLR QMFTPNESKF ELEDQMAESF EVLVSEMRTR SRNVLDKEEE
EFNSQEFLKS MNVMLEKDKK ESVKTLFTIS QALYSQIGEL IDLKKSLQKH AVAILGNIAF
TQMEILGIKR LLLNECNKDL ELYKKYEVEF AQVEDLPLIY GLYLIEKYRR LSWFQQILSF
ISNFNQDLEL FKQNELRTRN KWVKNFGSIA TVFCEDLLSS SDFKRLNEYH SHTSPPNEDE
EDENENSIAN YRQDLVKVSQ AIDNYMTQIK ETDVSEPIID LLSKTLFETK RFHIIYSNFK
NNNNNSSNGN SISPEGSIAL KSDDVVKGYK TRIKKLESLL HEFQYSDIGH WPQGVLNTHL
KPFRGSATSI NKKKFLGASV LLEPANISEV NIDSVSQANN HQIQELESNV DDLLHQLQLL
KEENNRKSMQ ISEMGKKISD LEVEKTAYRE TLTNLNQELA RLTNEEQSHR TEIFTLNASF
KKQLNDIISQ DNEKIEKLTG DYDDVSKSRE RLQMDLDESN KKHEQEVNLL KADIERLGKQ
IVTSEKSYAE TNSSSMEKGE KFETIPLAED PGRENQISAY TQTLQDRIFD IISTNIFILE
NIGLLLTFDN NNNIQIRRVK GLKKGTAQSN ILDESTQMLD AHDNSLIKSP VFQKLKDEYE
LIKSVANGSE KDTQQSIFLG NITQLYDNKL YEVAVIRRFK DIETLAKKLT KENKIKRTLL
ERFQREKVTL RNFQIGDLAL FLPTRENVNS VGSMSSSTSS LSSSFSSVDL STPPPLDAMS
IQSSPSVIHS NVINQASISG RDKNKLMRPW AAFTAFEEST RYFLKDEKGL TKGKEWFVGR
IVTLEHFVAD SPSNNPFRLP KGSVWFQVTA VVVSYQGV
