Detail Information for IndEnz0010001714
IED ID IndEnz0010001714
Enzyme Type ID esterase001714
Protein Name Neuropathy target esterase sws
Swiss cheese
EC 3.1.1.5
Gene Name sws GK16217
Organism Drosophila willistoni (Fruit fly)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora willistoni group willistoni subgroup Drosophila willistoni (Fruit fly)
Enzyme Sequence MDVLELLRASANGCYNTIFSDAWSQYVSQQITSSLYLYIALGILTVLFVAWFIYFKRLARLRLRDEIARSLNAVTSASGGDLRGLRFRKRDKMLFYGRRMLRKMKNVSGQMYSSGKGYKRRAVMRFARRILQLRRENMPLEMRTVEPPAEYLEETIEGSDRVPPDALYMLQSIRIFGHFEKPVFLKLCKHTQVLELMAGDYLFKITDADDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVTSLLSFIDVLSGNPSYYKTVTAKAMEKSVVIRLPMQAFEEVFRENPDVMIRVIQVIMIRLQRVLFTALRNYLGLNAELVQNHMRNKSITISGHLNSQSQSSQSMRQQTTATATGGTSATALGGQQLPAAVPSLPLQRQPPPPTIAPPLRHSREEHTLSGPNPNPNSGNNVQLPEVHGDAPNIDIYHQQQHGGSTSTGNLSTRRGSLVQPSIGGGGGGSTAQEGGCAAAGAPTIDMRLIQSSAVESLRKELGLPNEDAHIIEPFVEVRELEPNVTLITEGNADDVCIWFVMTGTLAVYQGVADATRSSTATTKSDKSDLLIHFVHPGEIVGGLAMLTGEASAYTIRSRNNSRVAYIRRAAIYQIMRQRPRIVLDLGNGVVRRLSPLVRQCDYALDWIFLESGRAVYRQDESSDSTYIVLSGRMRSVITNPGGKKEIVGEYGKGDLVGIVEMITETSRTTTVMAVRDSELAKLPEGLFNAIKLRYPIVVTKLISFLSHRFLGSMQTRGSTGAPGAPVEANPVTHKYSTVALVPITDEVPLTPFTYELYHSLCAIGPVLRLTSEVVRKQLGQNIFEAANEYRLTSWLAQQEDRNIITLYQCDNSLSPWTHRCMRQADVILIVGLGDRSHLVGKFEREIDRLAMRTQKELVLLYPETTNAKPANTLSWLNARPWVTKHHHVLCVKRIFTRKSQYRINDLYSRVLLSEPNMHSDFSRLARWLTGNSIGLVLGGGGARGAAHIGMLKAIQEAGIPIDMVGGVSIGALMGALWCSERNITTVTQKARQWSKKMTKWFLQLLDLTYPITSMFSGREFNKTIHDTFGDVSIEDLWIPYFTLTTDITASCHRIHTNGSLWRYVRSSMSLSGYMPPLCDPKDGHLLLDGGYVNNLPGHLWRYCRASMSIAGVFPPFCDYRDGHLLLDGCYTNNVPADVMHNLGAAHIIAIDVGSQDDTDLTNYGDDLSGWWLLYKKWNPFTSPVKVPDLPDIQSRLAYVSCVRQLEEVKNSDYCEYIRPPIDKYKTLAFGSFDEIRDVGYVFGKNYFESMAKAGRLGRFNQWFNKEPPKRGNHASLNEYTFIDLAQIVCKLPETYAVNTAEIFSEDEDCDGYISEPSTLNTDRRIQVPRAGNSLSLSEAEMDSDVEIDFRSDSKKDKATQSTPPAPGKDNEDKTDAVDRIPLLTLERPLTDQQQQHSDETDEQETPRAMKDGTNTMTTQTTSPTTDAGSEWAGSESELEKENKNVNTKN
Enzyme Length 1481
Uniprot Accession Number B4N1W9
Absorption
Active Site ACT_SITE 1000; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1120; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9U969};
DNA Binding
EC Number 3.1.1.5
Enzyme Function FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Plays a role in the signaling mechanism between neurons and glia that regulates glia wrapping during development of the adult brain. Essential for membrane lipid homeostasis and cell survival in both neurons and glia of the adult brain (By similarity). {ECO:0000250|UniProtKB:Q9U969}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 175..302; /note=cNMP 1; /evidence=ECO:0000255; NP_BIND 492..624; /note=cNMP 2; /evidence=ECO:0000255; NP_BIND 613..740; /note=cNMP 3; /evidence=ECO:0000255
Features Active site (2); Chain (1); Compositional bias (7); Domain (1); Modified residue (2); Motif (3); Nucleotide binding (3); Region (2); Topological domain (2); Transmembrane (1)
Keywords Developmental protein;Endoplasmic reticulum;Hydrolase;Lipid degradation;Lipid metabolism;Membrane;Neurogenesis;Phosphoprotein;Reference proteome;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the membrane. {ECO:0000250|UniProtKB:Q9U969}.
Modified Residue MOD_RES 448; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9U969; MOD_RES 1214; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9U969
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 971..976; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 998..1002; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1120..1122; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161
Gene Encoded By
Mass 165,348
Kinetics
Metal Binding
Rhea ID RHEA:15177
Cross Reference Brenda