Detail Information for IndEnz0005001201
IED ID IndEnz0005001201
Enzyme Type ID lipase001201
Protein Name GPI inositol-deacylase
EC 3.1.-.-
Gene Name BST1 DEHA2D16632g
Organism Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Debaryomyces Debaryomyces hansenii (Yeast) (Torulaspora hansenii) Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Enzyme Sequence MDSKSRGKSRLNRSILTLVSFFGLVLFYLTWYLYTRGLTGADSPGCRIVYMGPSYARITAFDESHTKFASKYSLYLYREQGRDPLPDENEGFKHLGGIPILFIPGNAGSYRQVRSIAAETSDIYFDHYLDQPDGLNPNAKNYDFFTADFNEDFTAFHGRTLLDQAEYLNEAIKFILGLYANSEHPPRSVVVLGHSMGGVVSRVMVSLPNYIPDSINTIITLASPHAAAPLTFDGDILKIYSAVDRFWFQGYDNKETDNTIAKIAKERLSKISLISITGGLLDSILPADYTTLGYLVPPTNGFTVYTTGIPGVWTPIDHLAIVWCAQLRRRVSNALLEIANFDSPDKTYSLEKRMEIMRKNFLSGFEDYTSQDKVAYDKPADHILLKADSQQINFVQEGQKLKVTPGKMPSPLNVFRLPSPKVSKVQFSLLSSMDIGELKSDNNEGYTQPTLLLCNTMDAIKEDANIIDFTNKETTEIVMFKCIDVRDDSNMIPRSAVGTYSLSESSIGGDKSPFYAIQYNSTILKQYDTVIVTGSLGMESNDNENFLLAELSDYNSSQFNIHEDLFSLMTRGAKFSLPLDKPLSMNIKIPGAWSSILAYKLKVSWPEDRETTEYIPVFRTFIRQWSNEPYEVKWHVNIEANNQVLLNMHGIAPYTPFKVKSKEEYGLNIEIWTDSIPDKSLTTIRLRIDLLNSLRLLVLRYRLATISFCVSIILLALVFQVKHYKETNKFPTFLYGLSCICSPWVFGSILFTLSILTPIMSIKPLQKFLNVIDPVVLQDSNEINLSLTDEFKLNSFFLGLEEKSLWFIGPVFFVMGLGIVSLTFYSLLVAGNVIASISRVLLKRLKLSQTEKKQPNPGKLWANRRIIGVLFVLLVIPIYMPYQFAYVVSCIIQSIQVIKILVADKTNKSILNYHLSLLMLMLWVLPINVPILVVFVHNMTINWTTPFSSHHNFLAILPVILLMERYSNSRTLPKMSQTKYKVTQAFLAYYVFYCLVYGIRHTYWIHHLFNLLCCWLLVLHYDAQDDTSDHVQ
Enzyme Length 1032
Uniprot Accession Number Q6BRG1
Absorption
Active Site ACT_SITE 195; /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 (7); 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 117,343
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda