Detail Information for IndEnz0005001079
IED ID IndEnz0005001079
Enzyme Type ID lipase001079
Protein Name GPI inositol-deacylase
EC 3.1.-.-
Gene Name BST1 KLLA0F25124g
Organism Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Kluyveromyces Kluyveromyces lactis (Yeast) (Candida sphaerica) Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Enzyme Sequence MVQIDLPAESAVRIRYPTLTKKLRKRSTLVIIVGLLLLCIITSTHISHNFSGSDTPKCRSIYMYPSYARIDGFDSRHTKLAKKYHLYLYREQGKDKEPKHGDEIQLDGIPVLFIPGNAGSFKQARSIAAASANLYFDHKSTIQNSNAKNMDYFTADFNEDFTAFHGQTMLDQAVYLNDAVRYILSMYAQSAAYKESNRPLPKSVILLGHSMGGIVARLMLTLPNHIPESVNTILTLSSPHSTAPVTFDGDILKLYDRVNSYWTSAMNDMGSYFRNNVSVISITGGILDDILPADYTNLQGIVPESNGFTTFTTTIPELWTPIDHLAIVWCDQLRYLLAKYILEIVNDDAGGKTATLDIRMRKGRKFFLSGLERITDADKLIDKNLSAPAVDFSDTESVPENHLLVLNSSESMSTGYAFNISKSVDYSFEMLTSLVQFDIFFCKDIYGKDCINGFSSFSKVPHSTSLQKFPTDSSWGESVSPFRFISLNGSLLQGFQIIVFQGSMKKKEDFVLAKYSDDKSIETASDGLWKLSLFPFRMSLKNKHSFVHGLAFPNLWSSLISFNLKTTFSDEIDSMFRPMMRQYVNNPYETKWHLLAASSSHEINMHNISPFIPLDDTIDKSLNLMFFIPPGEEISLRLSINWKLTLKMLYIRFRLAFASIPISIIALVLCYQFYYYDSPDSKFISFDTGLMNVLNNHSLLIFLFLSVGPIAINHKAILTLLHYLDPISLSKPSSDSHMLNNNYMLGLRETFVWWIGPVFFIISVALLFIILRLINVIEFAVIKISSAITRYTRITFPDPLNDMTHHKLLFNNRQLLGVCFISLGVMVYVPYQFAFILVSLIQMWNCMKLAVFTNRNNAKYSNIHNYNVSFLMLTIFMIPINAPIVVVFLRNFAIRWETAFRSHHNFLAIAPTLLLTLRNSQCNIPIIKNRMNWLIVVSILGYLSFYSFMYGIRNLYWVYHISNILNGVLFFLTIL
Enzyme Length 975
Uniprot Accession Number Q6CIN9
Absorption
Active Site ACT_SITE 210; /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. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Glycosylation (8); Transmembrane (8)
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:0000250}; Multi-pass membrane protein {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 111,164
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda