| 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 |