Detail Information for IndEnz0005001199
IED ID IndEnz0005001199
Enzyme Type ID lipase001199
Protein Name GPI inositol-deacylase
EC 3.1.-.-
Gene Name BST1 CHGG_04544
Organism Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) (Soil fungus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Chaetomiaceae Chaetomium Chaetomium globosum (Soil fungus) Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) (Soil fungus)
Enzyme Sequence MRRHSSGSSEDDDASPVEAPHANSSRFSAKDSRSSAHPTTKLDHNRNADRPPSFSISRRSSSINWRLPESRNGNGTVEKRPSPERTSPSSPLGLIMTANGELRTKEVEKTPETVIPARRPPWRSPWAITFSALVAAIVGIGFLVAVLHSSVTRQLDPKGCRMSYMRPSYAKLNEFDTEHTRLASKYSLYLYREQDIDRDTKVRGVPVLFIPGNAGSYKQVRPIAAEAANYFHNVLQHDESAMNAGTRNLDFFTVDFNEDITAFHGQTLLDQAEYLNEAVRYILSLYLDPRVADRDPDLPDPTSVIVLGHSMGGIVARTMLIMPNFQSHSINTIITMSAPHARPPVSFDSQSVQTYKDINDYWRRAYSQQWANDNPLWHVTLVSIAGGGLDTVVPSDYASVESLVPDTHGFTVFTSTIPNVWTSMDHQAILWCDQFRKVVAQAIYDVVDVHRATQTKPRAERMRVFKKWFLTGMETIAEKAAPRSEPTTLLTVDDNSDSIIAEGERLVLRNLGTAGTVRAHLMPIPPSGSPGMKRFTLLTDTKLDKPGEHGKLEVLFCSVIPSQPSQSWAGFPSQMDLSKGSTGSTRLACRSAAPDVVSLPASTSSTQFPFYLNGEKEITPFSYLEYGVDDIAEHQFVAVVEKTTAPTPGFVVAEFSDYTQSHRTRHISLRSLLTFGMKFHLPAERPMVSEVKVPSLQSSLLAYNLRISHQDCNGDSELFAPLVRQYLAEPYESKYFVNAREATVSLHGVAPYVPPPLTGKLDENGLSFQFWTDPTCSSSIHIELTADFMGSLGKLYMRYRTVFAAFPLFIVALVLRKQFRVYDTTGMFIPFLEGLDLCLRQSIPLMLASLTLLTLSTGIMAPASNASFWHWRNGTSSIMDFQHNDLLIGTEDPLFLFLIPLIAIVCVGVCTVFNYMALTLTHLLGVLASLVTFHPGWIGNEDRKKTTPAAFFSPSPRRRMITTAVLLLLVTTMVPYQFAYLVACLVQLMTTVRAQRIASELRSTANSNFYNYTHSIFILMLWILPINLPTFVVWVHNLAVHWLTPFSSHHNVLSVMPFIVLVETLTTGKMIPRMGSRLKHVTSLLLFGMAVYAAVYGVTYAYTLHYVANFLAFWLAIVHSTSDSWSLAGLTHLYSGDAGIRKRGKEP
Enzyme Length 1147
Uniprot Accession Number Q2H102
Absorption
Active Site ACT_SITE 310; /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); Compositional bias (3); Erroneous initiation (1); Glycosylation (5); Region (1); 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: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 127,892
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda