ID ATG18_YEAST Reviewed; 500 AA. AC P43601; D6VTQ1; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 197. DE RecName: Full=Autophagy-related protein 18 {ECO:0000303|PubMed:14536056}; DE AltName: Full=Cytoplasm to vacuole targeting protein 18 {ECO:0000303|PubMed:11739783}; DE AltName: Full=Needed for premeiotic replication protein 1 {ECO:0000303|PubMed:11470404}; DE AltName: Full=Swollen vacuole phenotype protein 1 {ECO:0000303|PubMed:15103325}; GN Name=ATG18 {ECO:0000303|PubMed:14536056}; GN Synonyms=AUT10 {ECO:0000303|PubMed:11707261}, CVT18 GN {ECO:0000303|PubMed:11739783}, NMR1 {ECO:0000303|PubMed:11470404}, GN SVP1 {ECO:0000303|PubMed:15103325}; GN OrderedLocusNames=YFR021W {ECO:0000312|SGD:S000001917}; 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=7670463; DOI=10.1038/ng0795-261; RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., RA Eki T.; RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces RT cerevisiae."; RL Nat. Genet. 10:261-268(1995). 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=11470404; DOI=10.1016/s0960-9822(01)00274-3; RA Rabitsch K.P., Toth A., Galova M., Schleiffer A., Schaffner G., Aigner E., RA Rupp C., Penkner A.M., Moreno-Borchart A.C., Primig M., Esposito R.E., RA Klein F., Knop M., Nasmyth K.; RT "A screen for genes required for meiosis and spore formation based on RT whole-genome expression."; RL Curr. Biol. 11:1001-1009(2001). RN [4] RP FUNCTION. RX PubMed=11707261; DOI=10.1016/s0014-5793(01)03016-2; RA Barth H., Meiling-Wesse K., Epple U.D., Thumm M.; RT "Autophagy and the cytoplasm to vacuole targeting pathway both require RT Aut10p."; RL FEBS Lett. 508:23-28(2001). RN [5] RP FUNCTION. RX PubMed=11739783; DOI=10.1091/mbc.12.12.3821; RA Guan J., Stromhaug P.E., George M.D., Habibzadegah-Tari P., Bevan A., RA Dunn W.A. Jr., Klionsky D.J.; RT "Cvt18/Gsa12 is required for cytoplasm-to-vacuole transport, pexophagy, and RT autophagy in Saccharomyces cerevisiae and Pichia pastoris."; RL Mol. Biol. Cell 12:3821-3838(2001). RN [6] RP FUNCTION. RX PubMed=11536337; DOI=10.1002/yea.764; RA Georgakopoulos T., Koutroubas G., Vakonakis I., Tzermia M., Prokova V., RA Voutsina A., Alexandraki D.; RT "Functional analysis of the Saccharomyces cerevisiae RT YFR021w/YGR223c/YPL100w ORF family suggests relations to RT mitochondrial/peroxisomal functions and amino acid signalling pathways."; RL Yeast 18:1155-1171(2001). RN [7] 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 [8] 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 [9] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATG9. 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 [10] RP INTERACTION WITH PIP2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP 73-ARG--ARG-76 AND 285-ARG-ARG-286. RX PubMed=15103325; DOI=10.1038/sj.emboj.7600203; RA Dove S.K., Piper R.C., McEwen R.K., Yu J.W., King M.C., Hughes D.C., RA Thuring J., Holmes A.B., Cooke F.T., Michell R.H., Parker P.J., RA Lemmon M.A.; RT "Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate RT effectors."; RL EMBO J. 23:1922-1933(2004). RN [11] RP FUNCTION. 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 [12] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PIP2. 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 [13] RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=16876790; DOI=10.1016/j.febslet.2006.07.041; RA Krick R., Tolstrup J., Appelles A., Henke S., Thumm M.; RT "The relevance of the phosphatidylinositolphosphat-binding motif FRRGT of RT Atg18 and Atg21 for the Cvt pathway and autophagy."; RL FEBS Lett. 580:4632-4638(2006). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VAC17, AND MUTAGENESIS OF RP 285-ARG--ARG-286. RX PubMed=17699591; DOI=10.1091/mbc.e07-04-0301; RA Efe J.A., Botelho R.J., Emr S.D.; RT "Atg18 regulates organelle morphology and Fab1 kinase activity independent RT of its membrane recruitment by phosphatidylinositol 3,5-bisphosphate."; RL Mol. Biol. Cell 18:4232-4244(2007). RN [15] RP SUBCELLULAR LOCATION. 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 [16] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=18769150; DOI=10.4161/auto.6801; RA Krick R., Henke S., Tolstrup J., Thumm M.; RT "Dissecting the localization and function of Atg18, Atg21 and Ygr223c."; RL Autophagy 4:896-910(2008). RN [17] RP IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX, FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=19037259; DOI=10.1038/emboj.2008.248; RA Jin N., Chow C.Y., Liu L., Zolov S.N., Bronson R., Davisson M., RA Petersen J.L., Zhang Y., Park S., Duex J.E., Goldowitz D., Meisler M.H., RA Weisman L.S.; RT "VAC14 nucleates a protein complex essential for the acute interconversion RT of PI3P and PI(3,5)P(2) in yeast and mouse."; RL EMBO J. 27:3221-3234(2008). RN [18] RP FUNCTION, INTERACTION WITH ATG2, PI3P-BINDING, AND SUBCELLULAR LOCATION. RX PubMed=18586673; DOI=10.1074/jbc.m803180200; RA Obara K., Sekito T., Niimi K., Ohsumi Y.; RT "The Atg18-Atg2 complex is recruited to autophagic membranes via RT phosphatidylinositol 3-phosphate and exerts an essential function."; RL J. Biol. Chem. 283:23972-23980(2008). RN [19] RP INTERACTION WITH ATG9, AND SUBCELLULAR LOCATION. 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, 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 [21] RP FUNCTION, AND DOMAIN. 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 [22] RP FUNCTION. RX PubMed=22108003; DOI=10.4161/auto.7.12.18424; RA Nair U., Thumm M., Klionsky D.J., Krick R.; RT "GFP-Atg8 protease protection as a tool to monitor autophagosome RT biogenesis."; RL Autophagy 7:1546-1550(2011). RN [23] RP PIP2-BINDING. RX PubMed=21536737; DOI=10.1101/gad.1998611; RA Han B.K., Emr S.D.; RT "Phosphoinositide [PI(3,5)P2] lipid-dependent regulation of the general RT transcriptional regulator Tup1."; RL Genes Dev. 25:984-995(2011). RN [24] RP SUBCELLULAR LOCATION. RX PubMed=22889849; DOI=10.4161/auto.20681; RA Taylor R. Jr., Chen P.H., Chou C.C., Patel J., Jin S.V.; RT "KCS1 deletion in Saccharomyces cerevisiae leads to a defect in RT translocation of autophagic proteins and reduces autophagosome formation."; RL Autophagy 8:1300-1311(2012). RN [25] RP FUNCTION OF THE ATG2-ATG8 COMPLEX, AND SUBUNIT. RX PubMed=22728243; DOI=10.1016/j.febslet.2012.06.008; RA Kobayashi T., Suzuki K., Ohsumi Y.; RT "Autophagosome formation can be achieved in the absence of Atg18 by RT expressing engineered PAS-targeted Atg2."; RL FEBS Lett. 586:2473-2478(2012). RN [26] RP SUBCELLULAR LOCATION. RX PubMed=22704557; DOI=10.1016/j.molcel.2012.05.027; RA Baskaran S., Ragusa M.J., Boura E., Hurley J.H.; RT "Two-site recognition of phosphatidylinositol 3-phosphate by PROPPINs in RT autophagy."; RL Mol. Cell 47:339-348(2012). RN [27] RP FUNCTION. RX PubMed=22787281; DOI=10.1091/mbc.e12-05-0347; RA Zieger M., Mayer A.; RT "Yeast vacuoles fragment in an asymmetrical two-phase process with distinct RT protein requirements."; RL Mol. Biol. Cell 23:3438-3449(2012). RN [28] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-264; THR-268; ARG-271; RP ARG-285; ARG-286; SER-311; THR-313 AND HIS-315. RX PubMed=22753491; DOI=10.1073/pnas.1205128109; RA Krick R., Busse R.A., Scacioc A., Stephan M., Janshoff A., Thumm M., RA Kuhnel K.; RT "Structural and functional characterization of the two phosphoinositide RT binding sites of PROPPINs, a beta-propeller protein family."; RL Proc. Natl. Acad. Sci. U.S.A. 109:E2042-E2049(2012). RN [29] RP FUNCTION, AND INTERACTION WITH ATG9. 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 [30] RP INTERACTION WITH ATG9. 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 [31] {ECO:0007744|PDB:6KYB} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), DOMAIN, AND INTERACTION WITH ATG2. RX PubMed=32809042; DOI=10.1007/s00018-020-03621-9; RA Lei Y., Tang D., Liao G., Xu L., Liu S., Chen Q., Li C., Duan J., Wang K., RA Wang J., Sun B., Li Z., Dai L., Cheng W., Qi S., Lu K.; RT "The crystal structure of Atg18 reveals a new binding site for Atg2 in RT Saccharomyces cerevisiae."; RL Cell. Mol. Life Sci. 78:2131-2143(2021). CC -!- FUNCTION: Phosphoinositide binding protein that plays a key role in CC cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and CC starvation-induced autophagy (PubMed:11470404, PubMed:11707261, CC PubMed:11739783, PubMed:11536337, PubMed:15155809, PubMed:15194695, CC PubMed:16876790, PubMed:20154084, PubMed:18769150). Component of the CC PI(3,5)P2 regulatory complex that regulates both the synthesis and CC turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) CC (PubMed:19037259, PubMed:18586673). Involved in correct ATG9 CC trafficking to the pre-autophagosomal structure (PubMed:14723849, CC PubMed:18829864, PubMed:24905091). With ATG2, protects ATG8 from ATG4- CC mediated cleavage (PubMed:22108003, PubMed:22728243). May negatively CC regulate FAB1 activity by sequestering or masking VAC7 from FAB1 CC (PubMed:17699591). Plays an important role in osmotically-induced CC vacuole fragmentation (PubMed:22787281). {ECO:0000269|PubMed:11470404, CC ECO:0000269|PubMed:11536337, ECO:0000269|PubMed:11707261, CC ECO:0000269|PubMed:11739783, ECO:0000269|PubMed:14723849, CC ECO:0000269|PubMed:15155809, ECO:0000269|PubMed:15194695, CC ECO:0000269|PubMed:16876790, ECO:0000269|PubMed:17699591, CC ECO:0000269|PubMed:18586673, ECO:0000269|PubMed:18769150, CC ECO:0000269|PubMed:18829864, ECO:0000269|PubMed:19037259, CC ECO:0000269|PubMed:20154084, ECO:0000269|PubMed:22108003, CC ECO:0000269|PubMed:22728243, ECO:0000269|PubMed:22787281, CC ECO:0000269|PubMed:24905091}. CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex, composed of CC ATG18, FIG4, FAB1, VAC14 and VAC7. VAC14 nucleates the assembly of the CC complex and serves as a scaffold (PubMed:19037259, PubMed:18586673). CC Interacts with ATG2, the ATG2-ATG18 complex being essential for CC autophagosome formation (PubMed:22728243, PubMed:32809042). Interacts CC with ATG9 (PubMed:14723849, PubMed:15103325, PubMed:15155809, CC PubMed:18829864, PubMed:24905091, PubMed:24440502). Interacts also with CC VAC17 (PubMed:17699591). {ECO:0000269|PubMed:14723849, CC ECO:0000269|PubMed:15103325, ECO:0000269|PubMed:15155809, CC ECO:0000269|PubMed:17699591, ECO:0000269|PubMed:18586673, CC ECO:0000269|PubMed:18829864, ECO:0000269|PubMed:19037259, CC ECO:0000269|PubMed:22728243, ECO:0000269|PubMed:24440502, CC ECO:0000269|PubMed:24905091, ECO:0000269|PubMed:32809042}. CC -!- INTERACTION: CC P43601; P53855: ATG2; NbExp=5; IntAct=EBI-22968, EBI-29212; CC P43601; Q06708: VAC14; NbExp=5; IntAct=EBI-22968, EBI-27189; CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane CC {ECO:0000269|PubMed:14723849, ECO:0000269|PubMed:16876790, CC ECO:0000269|PubMed:18497569, ECO:0000269|PubMed:18586673, CC ECO:0000269|PubMed:18829864}; Peripheral membrane protein CC {ECO:0000269|PubMed:14723849, ECO:0000269|PubMed:16876790, CC ECO:0000269|PubMed:18497569, ECO:0000269|PubMed:18586673, CC ECO:0000269|PubMed:18829864}. Vacuole membrane CC {ECO:0000269|PubMed:15103325, ECO:0000269|PubMed:15155809, CC ECO:0000269|PubMed:16876790, ECO:0000269|PubMed:17699591, CC ECO:0000269|PubMed:18497569, ECO:0000269|PubMed:19037259}; Peripheral CC membrane protein {ECO:0000269|PubMed:15103325, CC ECO:0000269|PubMed:15155809, ECO:0000269|PubMed:16876790, CC ECO:0000269|PubMed:17699591, ECO:0000269|PubMed:18497569, CC ECO:0000269|PubMed:19037259}. Endosome membrane CC {ECO:0000269|PubMed:18769150}; Peripheral membrane protein CC {ECO:0000269|PubMed:18769150}. Note=Requires VAC7 for vacuole membrane CC localization. Under mid-log phase growth, localizes to the vacuolar CC membrane; but when cells are starved, is almost completely released CC from the vacuole membrane. {ECO:0000269|PubMed:17699591}. CC -!- DOMAIN: The 377 first amino acids might form a beta-propeller domain CC involved in specific binding to phosphatidylinositol 3,5-bisphosphate CC (PIP2), leading to the association of the protein to the membrane. CC Association to the membrane can also occur through binding to CC phosphatidylinositol 3-monophosphate (PI3P). CC {ECO:0000269|PubMed:22753491}. CC -!- DOMAIN: The L/FRRG motif is essential for the cytoplasm to vacuole CC transport (Cvt) pathway, for the recruitment of ATG8 and ATG16 to the CC PAS in nutrient-rich medium, and for its recruitment to and CC dissociation from the PAS under starvation conditions. CC {ECO:0000269|PubMed:16876790}. CC -!- DOMAIN: The 7AB loop (residues 433-460) is important for interaction CC with Atg2 and required for autophagy. {ECO:0000269|PubMed:32809042}. CC -!- MISCELLANEOUS: Present with 1560 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN 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; D50617; BAA09260.1; -; Genomic_DNA. DR EMBL; BK006940; DAA12461.1; -; Genomic_DNA. DR PIR; S56276; S56276. DR RefSeq; NP_444297.1; NM_001179986.1. DR PDB; 6KYB; X-ray; 2.80 A; A/B/C/D=1-500. DR PDB; 8AFQ; EM; 3.30 A; A/C/D/E=1-500. DR PDB; 8AFW; EM; 3.80 A; A/B/C/D=1-500. DR PDB; 8AFY; EM; 26.00 A; A/B/C/D/E/F/G/H=1-500. DR PDBsum; 6KYB; -. DR PDBsum; 8AFQ; -. DR PDBsum; 8AFW; -. DR PDBsum; 8AFY; -. DR AlphaFoldDB; P43601; -. DR EMDB; EMD-15408; -. DR EMDB; EMD-15410; -. DR EMDB; EMD-15412; -. DR SMR; P43601; -. DR BioGRID; 31174; 204. DR ComplexPortal; CPX-3088; PAS complex. DR ComplexPortal; CPX-361; ATG2-ATG18 complex. DR DIP; DIP-5185N; -. DR IntAct; P43601; 28. DR MINT; P43601; -. DR STRING; 4932.YFR021W; -. DR TCDB; 9.A.15.1.1; the autophagy-related phagophore-formation transporter (apt) family. DR iPTMnet; P43601; -. DR MaxQB; P43601; -. DR PaxDb; 4932-YFR021W; -. DR PeptideAtlas; P43601; -. DR EnsemblFungi; YFR021W_mRNA; YFR021W; YFR021W. DR GeneID; 850577; -. DR KEGG; sce:YFR021W; -. DR AGR; SGD:S000001917; -. DR SGD; S000001917; ATG18. DR VEuPathDB; FungiDB:YFR021W; -. DR eggNOG; KOG2110; Eukaryota. DR GeneTree; ENSGT00940000167852; -. DR HOGENOM; CLU_025895_5_2_1; -. DR InParanoid; P43601; -. DR OMA; KTMGRMI; -. DR OrthoDB; 391429at2759; -. DR BioCyc; YEAST:G3O-30472-MONOMER; -. DR Reactome; R-SCE-1632852; Macroautophagy. DR BioGRID-ORCS; 850577; 0 hits in 10 CRISPR screens. DR PRO; PR:P43601; -. DR Proteomes; UP000002311; Chromosome VI. DR RNAct; P43601; Protein. DR GO; GO:0071944; C:cell periphery; HDA:SGD. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005768; C:endosome; IDA:SGD. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central. DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD. DR GO; GO:0070772; C:PAS complex; IDA:SGD. DR GO; GO:0061908; C:phagophore; IDA:SGD. DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD. DR GO; GO:0034045; C:phagophore assembly site membrane; IDA:ComplexPortal. DR GO; GO:0032991; C:protein-containing complex; IDA:ComplexPortal. DR GO; GO:0005774; C:vacuolar membrane; IDA:UniProtKB. DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:SGD. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD. DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD. DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD. DR GO; GO:1903100; P:1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate metabolic process; NAS:ComplexPortal. DR GO; GO:0000045; P:autophagosome assembly; NAS:ComplexPortal. DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IDA:SGD. DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD. DR GO; GO:0016236; P:macroautophagy; IDA:SGD. DR GO; GO:0044804; P:nucleophagy; IMP:SGD. DR GO; GO:0000425; P:pexophagy; IMP:SGD. DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD. DR GO; GO:0044090; P:positive regulation of vacuole organization; IMP:SGD. DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0010511; P:regulation of phosphatidylinositol biosynthetic process; NAS:ComplexPortal. DR GO; GO:0006624; P:vacuolar protein processing; IDA:SGD. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR048720; PROPPIN. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR11227:SF17; WD REPEAT DOMAIN PHOSPHOINOSITIDE-INTERACTING PROTEIN 2; 1. DR PANTHER; PTHR11227; WD-REPEAT PROTEIN INTERACTING WITH PHOSPHOINOSIDES WIPI -RELATED; 1. DR Pfam; PF21032; PROPPIN; 2. DR SMART; SM00320; WD40; 2. DR SUPFAM; SSF50978; WD40 repeat-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Autophagy; Endosome; Membrane; Phosphoprotein; KW Protein transport; Reference proteome; Repeat; Transport; Vacuole; KW WD repeat. FT CHAIN 1..500 FT /note="Autophagy-related protein 18" FT /id="PRO_0000050874" FT REPEAT 243..283 FT /note="WD 1" FT /evidence="ECO:0000255" FT REPEAT 288..327 FT /note="WD 2" FT /evidence="ECO:0000255" FT REGION 174..197 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 328..358 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 284..288 FT /note="L/FRRG motif" FT /evidence="ECO:0000303|PubMed:16876790" FT COMPBIAS 340..355 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 354 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MUTAGEN 73..76 FT /note="RRLR->SSLS: Leads to a slight reduction of PIP2 FT binding." FT /evidence="ECO:0000269|PubMed:15103325" FT MUTAGEN 264 FT /note="S->A: Impairs membrane-association." FT /evidence="ECO:0000269|PubMed:22753491" FT MUTAGEN 268 FT /note="T->A: Impairs membrane-association." FT /evidence="ECO:0000269|PubMed:22753491" FT MUTAGEN 271 FT /note="R->A: Impairs membrane-association." FT /evidence="ECO:0000269|PubMed:22753491" FT MUTAGEN 285..286 FT /note="RR->GG: Loss of recruitment to vacuole membrane." FT /evidence="ECO:0000269|PubMed:22753491" FT MUTAGEN 285..286 FT /note="RR->TT: Leads to a 40-fold decrease of affinity to FT PIP2." FT /evidence="ECO:0000269|PubMed:15103325, FT ECO:0000269|PubMed:22753491" FT MUTAGEN 285 FT /note="R->A: Impairs membrane-association." FT /evidence="ECO:0000269|PubMed:22753491" FT MUTAGEN 286 FT /note="R->A: Impairs membrane-association." FT /evidence="ECO:0000269|PubMed:22753491" FT MUTAGEN 311 FT /note="S->A: Impairs membrane-association." FT /evidence="ECO:0000269|PubMed:22753491" FT MUTAGEN 313 FT /note="T->A: Impairs membrane-association." FT /evidence="ECO:0000269|PubMed:22753491" FT MUTAGEN 315 FT /note="H->A: Impairs membrane-association." FT /evidence="ECO:0000269|PubMed:22753491" FT STRAND 8..13 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 17..26 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 28..32 FT /evidence="ECO:0007829|PDB:6KYB" FT TURN 33..36 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 37..42 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 47..52 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 54..63 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:6KYB" FT TURN 80..83 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 84..90 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 102..109 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 112..117 FT /evidence="ECO:0007829|PDB:6KYB" FT TURN 118..120 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 123..128 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 147..151 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 225..231 FT /evidence="ECO:0007829|PDB:6KYB" FT TURN 232..235 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 236..246 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 248..253 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 259..264 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 268..274 FT /evidence="ECO:0007829|PDB:6KYB" FT TURN 275..277 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 280..285 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 293..298 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 302..309 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 312..318 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 412..416 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 427..431 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 437..439 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 465..471 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 474..481 FT /evidence="ECO:0007829|PDB:6KYB" FT TURN 483..485 FT /evidence="ECO:0007829|PDB:6KYB" FT STRAND 490..497 FT /evidence="ECO:0007829|PDB:6KYB" SQ SEQUENCE 500 AA; 55102 MW; 06B2DFAF842AE933 CRC64; MSDSSPTINF INFNQTGTCI SLGTSKGFKI FNCEPFGKFY SEDSGGYAIV EMLFSTSLLA LVGIGDQPAL SPRRLRIINT KKHSIICEVT FPTSILSVKM NKSRLVVLLQ EQIYIYDINT MRLLHTIETN PNPRGLMAMS PSVANSYLVY PSPPKVINSE IKAHATTNNI TLSVGGNTET SFKRDQQDAG HSDISDLDQY SSFTKRDDAD PTSSNGGNSS IIKNGDVIVF NLETLQPTMV IEAHKGEIAA MAISFDGTLM ATASDKGTII RVFDIETGDK IYQFRRGTYA TRIYSISFSE DSQYLAVTGS SKTVHIFKLG HSMSNNKLDS DDSNMEEAAA DDSSLDTTSI DALSDEENPT RLAREPYVDA SRKTMGRMIR YSSQKLSRRA ARTLGQIFPI KVTSLLESSR HFASLKLPVE TNSHVMTISS IGSPIDIDTS EYPELFETGN SASTESYHEP VMKMVPIRVV SSDGYLYNFV MDPERGGDCL ILSQYSILMD //