Detail Information for IndEnz0002014400
IED ID IndEnz0002014400
Enzyme Type ID protease014400
Protein Name Autophagy-related protein 18
Cytoplasm to vacuole targeting protein 18
Needed for premeiotic replication protein 1
Swollen vacuole phenotype protein 1
Gene Name ATG18 AUT10 CVT18 NMR1 SVP1 YFR021W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Enzyme Sequence MSDSSPTINFINFNQTGTCISLGTSKGFKIFNCEPFGKFYSEDSGGYAIVEMLFSTSLLALVGIGDQPALSPRRLRIINTKKHSIICEVTFPTSILSVKMNKSRLVVLLQEQIYIYDINTMRLLHTIETNPNPRGLMAMSPSVANSYLVYPSPPKVINSEIKAHATTNNITLSVGGNTETSFKRDQQDAGHSDISDLDQYSSFTKRDDADPTSSNGGNSSIIKNGDVIVFNLETLQPTMVIEAHKGEIAAMAISFDGTLMATASDKGTIIRVFDIETGDKIYQFRRGTYATRIYSISFSEDSQYLAVTGSSKTVHIFKLGHSMSNNKLDSDDSNMEEAAADDSSLDTTSIDALSDEENPTRLAREPYVDASRKTMGRMIRYSSQKLSRRAARTLGQIFPIKVTSLLESSRHFASLKLPVETNSHVMTISSIGSPIDIDTSEYPELFETGNSASTESYHEPVMKMVPIRVVSSDGYLYNFVMDPERGGDCLILSQYSILMD
Enzyme Length 500
Uniprot Accession Number P43601
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). May negatively regulate FAB1 activity by sequestering or masking VAC7 from FAB1. Necessary for proper vacuole morphology. Plays an important role in osmotically-induced vacuole fragmentation. Required for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and starvation-induced autophagy. Involved in correct ATG9 trafficking to the pre-autophagosomal structure. Might also be involved in premeiotic DNA replication. With ATG2, protects ATG8 from ATG4-mediated cleavage. {ECO:0000269|PubMed:11470404, ECO:0000269|PubMed:11536337, ECO:0000269|PubMed:11707261, ECO:0000269|PubMed:11739783, ECO:0000269|PubMed:14723849, ECO:0000269|PubMed:15155809, ECO:0000269|PubMed:15194695, ECO:0000269|PubMed:16876790, ECO:0000269|PubMed:17699591, ECO:0000269|PubMed:18586673, ECO:0000269|PubMed:18769150, ECO:0000269|PubMed:19037259, ECO:0000269|PubMed:20154084, ECO:0000269|PubMed:22108003, ECO:0000269|PubMed:22728243, ECO:0000269|PubMed:22787281, ECO:0000269|PubMed:24905091}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (29); Chain (1); Compositional bias (1); Modified residue (1); Motif (1); Mutagenesis (11); Region (3); Repeat (2); Turn (6)
Keywords 3D-structure;Autophagy;Endosome;Membrane;Phosphoprotein;Protein transport;Reference proteome;Repeat;Transport;Vacuole;WD repeat
Interact With P53855; Q06708
Induction
Subcellular Location SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000269|PubMed:14723849, ECO:0000269|PubMed:16876790, ECO:0000269|PubMed:18497569, ECO:0000269|PubMed:18586673, ECO:0000269|PubMed:18829864}; Peripheral membrane protein {ECO:0000269|PubMed:14723849, ECO:0000269|PubMed:16876790, ECO:0000269|PubMed:18497569, ECO:0000269|PubMed:18586673, ECO:0000269|PubMed:18829864}. Vacuole membrane {ECO:0000269|PubMed:15103325, ECO:0000269|PubMed:15155809, ECO:0000269|PubMed:16876790, ECO:0000269|PubMed:17699591, ECO:0000269|PubMed:18497569, ECO:0000269|PubMed:19037259}; Peripheral membrane protein {ECO:0000269|PubMed:15103325, ECO:0000269|PubMed:15155809, ECO:0000269|PubMed:16876790, ECO:0000269|PubMed:17699591, ECO:0000269|PubMed:18497569, ECO:0000269|PubMed:19037259}. Endosome membrane {ECO:0000269|PubMed:18769150}; Peripheral membrane protein {ECO:0000269|PubMed:18769150}. Note=Requires VAC7 for vacuole membrane localization. Under mid-log phase growth, localizes to the vacuolar membrane; but when cells are starved, is almost completely released from the vacuole membrane. {ECO:0000269|PubMed:17699591}.
Modified Residue MOD_RES 354; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18407956
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 6KYB;
Mapped Pubmed ID 11169858; 11283351; 11805826; 11805837; 14690591; 15001715; 15350980; 15590821; 15615779; 15975782; 16230342; 16247502; 16429126; 16554755; 16607287; 16860663; 17043098; 17224625; 17382324; 17909521; 18006683; 18467557; 18701704; 18725539; 18769109; 18786576; 19079287; 19158662; 19272020; 19416362; 19491929; 19536198; 19619494; 19653858; 19659885; 19802558; 19841731; 19941614; 20083110; 20124347; 20138172; 20146925; 20184884; 20223289; 20487284; 20712412; 20811355; 21070969; 21119626; 21121900; 21194379; 21315770; 21317551; 21490802; 21548784; 21736686; 21801009; 22150273; 22240478; 22333915; 22374087; 22399380; 22536249; 22550491; 22722653; 22743996; 22768199; 22842922; 22851171; 22905177; 22992453; 23069643; 23230146; 23383298; 23416930; 23435086; 23549786; 23669359; 23725457; 23733851; 23750326; 23774579; 23904270; 24258026; 24366339; 24366340; 24710476; 24789822; 24806931; 24879146; 24928445; 25426852; 25568150; 25568152; 25713145; 25747593; 25759175; 25803831; 26081468; 26108642; 26563567; 26703187; 26780479; 26908221; 26940206; 27189367; 27381245; 27498190; 27693354; 27723509; 27957648; 30254161; 32809042;
Motif MOTIF 284..288; /note=L/FRRG motif; /evidence=ECO:0000303|PubMed:16876790
Gene Encoded By
Mass 55,102
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda