Detail Information for IndEnz0005001075
IED ID IndEnz0005001075
Enzyme Type ID lipase001075
Protein Name GPI inositol-deacylase A
EC 3.1.-.-
Gene Name BST1A YALI0F03927g
Organism Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Dipodascaceae Yarrowia Yarrowia lipolytica (Candida lipolytica) Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Enzyme Sequence MHIATFPALAITALALVLWATVATHSSNTNSCHMSYMKPDMIAMTGFNTTQTPLAHKYSLHLYRELDVDLSREVGGRPVLFVPGNGGSMRQIRSIAGEAAVQYWHDPRRAGADADTWANGSTARPKSALQKLNTFAFGDTESDTEGVRGLGDAVTARDMSGDDRRDAVERPLSNGKLPSQWPDDLPLDFFTVNFQEDLTAFDGTTVIDQAEYLNQAIAYILSLYSSHPNPPTSVIVIGHSMGGIVARTMVTLDSYIHGSINTILTLATPHVLPPVSFDKGIVGLYHNVNEFWKTETVPGGKLEDTLLVSVTGGIRDQMIPAEYSSVDTFLPPTNGFAVATTSIPDVWMSIDHQAMVWCHQLRRVVAETLLVVAGETTEKVSTRLDTFQEYFLSGMERVEKKAQNASESSKLTLDTLVSINTPLTTTSNIIINDHSPNQLVKTKSYFKFPVLKASEINEMSRSFAMPVDKGKSLLVKTNMPLEDLHILVCRTNTGDVDTNGFSFLRYGSKSKGVRVGTDTLVCANVAGEAVAMPSSIKYATGAKIPEEEETGEDNDIPVDSAISSTSLSEYIQLDASSLSGFQYVVVIDNTMSETISSDSYLLAEMALPSDMAVVAAPTWWEVLKVGRFTIELPEKRALLTKISLPHFWSSLVAFSIRLSTSDSFSMEYQCEAKKSMGSEHDVLFAPLLMQYSAQLHEAKFSTNLCGGYEQGTRVAVHGGAPYMPLAEGRDVSGTELYLWTDSSSRSSESLSLTLEIDLWGSLGRFLGFYRVMFAIFPMFVFLCLLMIQLRVWTTTELFVSLSDALDVFVDFQLPWILAGSCAIPFVPHVLVSLLYPQMSQPGQFFLGLNGTHLWFLGPVSLVIATGIVVVLHWLLQILTLWVCQCYYMLGLAPIAPESPFSVRRIVTISFLLLLVFKIVPHQFAFMVAVLVMAMGAGKARVGRLMQSEDKDNKSEPCVVIDRNLINYTHSLLLLLVLLLPINAPTLVVWLHNMANKWHTPLESHHEVSAILPILLLVLTASRGIMIRLPQSKRAIYATFAFLAYFALFVLFHGVVHSYRLHLLTNGLCLCLLYLSL
Enzyme Length 1076
Uniprot Accession Number Q6C2Z2
Absorption
Active Site ACT_SITE 240; /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 (6); 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 118,703
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda