| IED ID | IndEnz0010001513 |
| Enzyme Type ID | esterase001513 |
| Protein Name |
Patatin-like phospholipase domain-containing protein 6 Neuropathy target esterase EC 3.1.1.5 |
| Gene Name | PNPLA6 NTE |
| Organism | Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Ponginae Pongo Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
| Enzyme Sequence | MGTSSHGLATNSSGAKVAERDGFQDVPAPGEGAAGRICGAQPVPFVPQVLGVMIGAGVAVVVTAVLILLVVRRLRVPKTPAPDGPRYRFRKRDKVLFYGRKIMRKVSQSTSSLVDTSVSATSRPRMKKKLKMLNIAKKILRIQKETPTLQRKEPPPAVLEADLTEGDLANSHLPSEVLYMFKNVRVLGHFEKPLFLELCRHMVFQRLGQGDYVFRPGQPDASIYVVQDGLLELCLPGPDGKECVVKEVVPGDSVNSLLSILDVITGHQHPQRTVSARAARDSTVLRLPVEAFSAVFAKYPESLVRVVQIIMVRLQRVTFLALHNYLGLTNELFSHEIQPLRLFPSPGLPTRTSPVRGSKRMVSTSATDEPRETPGRPPDPTGAPLPGPTGDPVKPTSLETPSAPLLSRCVSMPGDISGLQGGPRSDFDMAYERGRISVSLQEGASGGSLAAPARTPTQEPREQPAGACEYSYCEDESATGGCPFGPYQGRQTSSIFEAAKRELAKLMRIEDPSLLNSRVLLHHAKAGTIIARQGDQDVSLHFVLWGCLHVYQHMIDKAEDVCLFVAQPGELVGQLAVLTGEPLIFTLRAQRDCTFLRISKSDFYEIMRAQPSVVLSAAHTVAARMSPFVRQMDFAIDWTAVEAGRALYRQGDRSDCTYIVLNGRLRSVIQRGSGKKELVGEYGRGDLIGVVEALTRQPRATTVHAVRDTELAKLPEGTLGHIKRRHPQVVTRLIHLLSQKILGNLQQLQGPFPGSGLGVPPHSELTNPASNLATVAVLPVCAEVPMVAFTLELQHALQAIGPTLLLNSDIIRARLGASALDSIQEFRLSGWLAQQEDAHRIVLYQTDASLTPWTVRCLRQADCILIVGLGDQEPTLGQLEQMLENTAVRALKQLVLLHREEGAGPTRTVEWLNMRSWCSGHPHLRCPRRLFSRRSPAKLHELYEKVFSRRADRHSDFSRLARVLTGNTIALVLGGGGARGCSHIGVLKALEEAGVPVDLVGGTSIGSFIGALYAEERSASRTKQRAREWAKSMTSVLEPVLDLTYPVTSMFTGSAFNRSIHRVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSLWRYVRASMTLSGYLPPLCDPKDGHLLMDGGYINNLPADIARSMGAKTVIAIDVGSQDETDLSTYGDSLSGWWLLWKRLNPWADKVKVPDMAEIQSRLAYVSCVRQLEVVKSSSYCEYLRPPIDCFKTMDFGKFDQVYDVGYQYGKAVFGGWSRGNVIEKMLTDRRSTDLNESRRADVLAYPSSGFTDLAEIVSRIEPPTSYVSDGCADGEESDCLTEYEEDAGPDCSRDEGGSPEGASPSTASEMEEEKSILRQRRCLPQEPPGSATDA |
| Enzyme Length | 1365 |
| Uniprot Accession Number | Q5RDS0 |
| Absorption | |
| Active Site | ACT_SITE 1004; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1124; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by a series a OPs such as mipafox (MPX), phenyl saligenin phosphate (PSP), phenyl dipentyl phosphinate (PDPP), diisopropyl fluorophosphate and paraoxon. {ECO:0000250|UniProtKB:Q8IY17}. |
| 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:Q3TRM4};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000250|UniProtKB:Q3TRM4}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:Q3TRM4, ECO:0000250|UniProtKB:Q8IY17};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000250|UniProtKB:Q3TRM4, ECO:0000250|UniProtKB:Q8IY17}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40807, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823; Evidence={ECO:0000250|UniProtKB:Q8IY17};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808; Evidence={ECO:0000250|UniProtKB:Q8IY17}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:39959, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:69081; Evidence={ECO:0000250|UniProtKB:Q8IY17};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39960; Evidence={ECO:0000250|UniProtKB:Q8IY17}; CATALYTIC ACTIVITY: Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:75455; Evidence={ECO:0000250|UniProtKB:Q8IY17};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39964; Evidence={ECO:0000250|UniProtKB:Q8IY17}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q8IY17};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000250|UniProtKB:Q8IY17}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q8IY17};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; Evidence={ECO:0000250|UniProtKB:Q8IY17}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; Evidence={ECO:0000250|UniProtKB:Q8IY17};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000250|UniProtKB:Q8IY17}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:49092, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:57597; Evidence={ECO:0000250|UniProtKB:Q3TRM4};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093; Evidence={ECO:0000250|UniProtKB:Q3TRM4}; |
| 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. Catalyzes the hydrolysis of several naturally occurring membrane-associated lipids. Hydrolyzes lysophospholipids and monoacylglycerols, preferring the 1-acyl to the 2-acyl isomer. Does not catalyze hydrolysis of di- or triacylglycerols or fatty acid amides. {ECO:0000250|UniProtKB:Q8IY17}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 186..313; /note=cNMP 1; NP_BIND 502..624; /note=cNMP 2; NP_BIND 620..740; /note=cNMP 3 |
| Features | Active site (2); Chain (1); Compositional bias (2); Domain (1); Glycosylation (1); Modified residue (6); Motif (3); Nucleotide binding (3); Region (3); Topological domain (2); Transmembrane (1) |
| Keywords | Endoplasmic reticulum;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Membrane;Phosphoprotein;Reference proteome;Repeat;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IY17}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:Q8IY17}. |
| Modified Residue | MOD_RES 345; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8IY17; MOD_RES 352; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q8IY17; MOD_RES 353; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8IY17; MOD_RES 363; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8IY17; MOD_RES 411; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8IY17; MOD_RES 455; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q8IY17 |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000250|UniProtKB:Q8IY17}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 975..980; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1002..1006; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1124..1126; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 149,750 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15177; RHEA:15178; RHEA:40435; RHEA:40436; RHEA:40807; RHEA:40808; RHEA:39959; RHEA:39960; RHEA:39963; RHEA:39964; RHEA:38487; RHEA:38488; RHEA:38491; RHEA:38492; RHEA:26132; RHEA:26133; RHEA:49092; RHEA:49093 |
| Cross Reference Brenda |