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 |