Detail Information for IndEnz0005001083
IED ID IndEnz0005001083
Enzyme Type ID lipase001083
Protein Name GPI inositol-deacylase
EC 3.1.-.-
Bypass of SEC30 protein 1
Gene Name BST1 YFL025C
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 MGIRRLVSVITRPIINKVNSSGQYSRVLATREDQDKASPKYMNNDKIAKKPYTYRLFSILGILSICSLLLISLLKPFNGADAPQCESIYMFPSYARIDGFDERYTPLAHKYHLYLYREQSVDREPLNGDELQLDGIPVLFIPGNAGSFRQCRSIASACSNIYFDSNTRATLRNENVRNLDFFTADFNEDFTAFHGETMLDQAEYLNDAIKYILSLYERTPDYPHPKPQSVIIVGHSMGGIVSRVMLTLKNHVPGSISTILTLSSPHAASPVTFDGDILKLYKNTNEYWRKQLSQNDSFFSKNISLVSITGGILDTTLPADYASVEDLVSLENGFTSFTTTIPDVWTPIDHLAIVWCKQLREVLARLLLESIDASKPEKVKPLNQRLQIARKLLLSGFEDYSWMNSKLNYPQENLQEFSDNFFSDYATLEMNDVLDFEMFNLEKWHNNYTKINIPSNISSTEHLHFTLLTSLDMPMIYFCTESRVNLSCITAVDSILTVPRSSKDTQFAADSSFGEAKNPFKAVSVGKNILQKYDYLMISKPTYGEFSEQEGMEDNQGFLLALLRNVSNVQIVNTTPSQILLFGEQLHLDGKDIEQVISFSNLWDSLLSYKLETKIEASNEGIASEETLFQPFIRQWVYEPFESKWHLNIINKSLDINMHNVAPFIPLNESEPRSLQLSFFIPPGMSLEAKMTINWSLTLKMLFIRYRLALASFPVAFIALVLSYQFYWYNKTSEFPSFDSTLGYILRKHGILMFFTLFLASPVVNNKLVQRILYLLDPVGLNYPFLLSERNMHANFYYLGIRDWFMSTIGILFGVMTVGLLALVSKIFGSLEILVIFLQRKLSKKNTEDKEAFDTIEHKAYGKGRLMASVLLLLLVFFHIPYQMAFVISLVIQIATCIRVALLKLSNNEQKLNLLNYNMTLLLLLLFVSAINIPIIIVFLHNVAIKWETSFRSHHNILAVAPIIFLVGNNSIFKMPNSVPLDTWDGKVTIILFVYLTVFSFIYGIRNLYWIHHLVNIICAWLLFFETIH
Enzyme Length 1029
Uniprot Accession Number P43571
Absorption
Active Site ACT_SITE 236; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.1.-.-
Enzyme Function FUNCTION: Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins. Required for the transport of misfolded protein to the Golgi, although dipensable for the transport of many normal proteins. {ECO:0000269|PubMed:11673477, ECO:0000269|PubMed:14734546, ECO:0000269|PubMed:16319176, ECO:0000269|PubMed:8862519}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Glycosylation (11); Transmembrane (9)
Keywords Endoplasmic reticulum;Glycoprotein;Hydrolase;Membrane;Protein transport;Reference proteome;Transmembrane;Transmembrane helix;Transport
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Modified Residue
Post Translational Modification PTM: Glycosylated. {ECO:0000269|PubMed:8862519}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12096123; 12878605; 14690591; 16093310; 16859984; 17233591; 17361015; 17913366; 17989219; 18323404; 19054390; 19433630; 19536198; 19883648; 21266254; 21490136; 21603271; 22177309; 22194828; 22265715; 23135325; 23202731; 23209158; 24391512; 24784135; 24906797; 25936552; 26450970; 26456335; 26563290; 26646153; 27325793; 27462707; 27693354;
Motif
Gene Encoded By
Mass 117,755
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda