ATG18_YEAST
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 03-AUG-2022, entry version 190.
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},
GN CVT18 {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.
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).
CC -!- FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis
CC and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC May negatively regulate FAB1 activity by sequestering or masking VAC7
CC from FAB1. Necessary for proper vacuole morphology. Plays an important
CC role in osmotically-induced vacuole fragmentation. Required for
CC cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and
CC starvation-induced autophagy. Involved in correct ATG9 trafficking to
CC the pre-autophagosomal structure. Might also be involved in premeiotic
CC DNA replication. With ATG2, protects ATG8 from ATG4-mediated cleavage.
CC {ECO:0000269|PubMed:11470404, ECO:0000269|PubMed:11536337,
CC ECO:0000269|PubMed:11707261, ECO:0000269|PubMed:11739783,
CC ECO:0000269|PubMed:14723849, ECO:0000269|PubMed:15155809,
CC ECO:0000269|PubMed:15194695, ECO:0000269|PubMed:16876790,
CC ECO:0000269|PubMed:17699591, ECO:0000269|PubMed:18586673,
CC ECO:0000269|PubMed:18769150, 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. Interacts with ATG2, ATG9 and VAC17.
CC The ATG2-ATG18 complex is essential for autophagosome formation.
CC {ECO:0000269|PubMed:14723849, ECO:0000269|PubMed:15103325,
CC ECO:0000269|PubMed:15155809, ECO:0000269|PubMed:17699591,
CC ECO:0000269|PubMed:18586673, ECO:0000269|PubMed:18829864,
CC ECO:0000269|PubMed:19037259, ECO:0000269|PubMed:24440502,
CC ECO:0000269|PubMed:24905091}.
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 -!- 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}.
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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 PDBsum; 6KYB; -.
DR AlphaFoldDB; P43601; -.
DR SMR; P43601; -.
DR BioGRID; 31174; 200.
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; P43601; -.
DR PRIDE; P43601; -.
DR EnsemblFungi; YFR021W_mRNA; YFR021W; YFR021W.
DR GeneID; 850577; -.
DR KEGG; sce:YFR021W; -.
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; TLGQIFP; -.
DR BioCyc; YEAST:G3O-30472-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
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; IC:ComplexPortal.
DR GO; GO:0000045; P:autophagosome assembly; IC:ComplexPortal.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0030242; P:autophagy of peroxisome; IMP:SGD.
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:0044805; P:late nucleophagy; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IDA: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:0006497; P:protein lipidation; IBA:GO_Central.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR GO; GO:0010511; P:regulation of phosphatidylinositol biosynthetic process; IC:ComplexPortal.
DR GO; GO:0006624; P:vacuolar protein processing; IDA:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 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 REPEAT 288..327
FT /note="WD 2"
FT REGION 174..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..287
FT /note="Necessary for proper localization to vacuole
FT membrane"
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: Slight reduction of PIP2 binding."
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: 40-fold decrease of affinity to PIP2."
FT /evidence="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
