| IED ID | IndEnz0010001471 |
| Enzyme Type ID | esterase001471 |
| Protein Name |
Patatin-like phospholipase domain-containing protein 6 Neuropathy target esterase EC 3.1.1.5 |
| Gene Name | Pnpla6 Nte |
| Organism | Mus musculus (Mouse) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MGTPSHELNTTSSGAEVIQKTLEEGLGRRICVAQPVPFVPQVLGVMIGAGVAVLVTAVLILLVVRRLRVQKTPAPEGPRYRFRKRDKVLFYGRKIMRKVSQSTSSLVDTSVSTTSRPRMKKKLKMLNIAKKILRIQKETPTLQRKEPPPSVLEADLTEGDLANSHLPSEVLYMLKNVRVLGHFEKPLFLELCRHMVFQRLGQGDYVFRPGQPDASIYVVQDGLLELCLPGPDGKECVVKEVVPGDSVNSLLSILDVITGHQHPQRTVSARAARDSTVLRLPVEAFSAVFTKYPESLVRVVQIIMVRLQRVTFLALHNYLGLTNELFSHEIQPLRLFPSPGLPTRTSPVRGSKRVVSTSGTEDTSKETSGRPLDSIGAPLPGPAGDPVKPTSLEAPPAPLLSRCISMPVDISGLQGGPRSDFDMAYERGRISVSLQEEASGGPQTASPRELREQPAGACEYSYCEDESATGGCPFGPYQGRQTSSIFEAAKRELAKLMRIEDPSLLNSRVLLHHAKAGTIIARQGDQDVSLHFVLWGCLHVYQRMIDKAEEVCLFVAQPGELVGQLAVLTGEPLIFTLRAQRDCTFLRISKSHFYEIMRAQPSVVLSAAHTVAARMSPFVRQMDFAIDWTAVEAGRALYRQGDRSDCTYIVLNGRLRSVIQRGSGKKELVGEYGRGDLIGVVEALTRQPRATTVHAVRDTELAKLPEGTLGHIKRRYPQVVTRLIHLLSQKILGNLQQLQGPFPGSGLSVPQHSELTNPASNLSTVAILPVCAEVPMMAFTLELQHALQAIGPTLLLNSDVIRALLGASALDSIQEFRLSGWLAQQEDAHRIVLYQTDTSLTPWTVRCLRQADCILIVGLGDQEPTVGQLEQMLENTAVRALKQLVLLHREEGPGPTRTVEWLNMRSWCSGHLHLRCPRRLFSRRSPAKLHELYEKVFSRRADRHSDFSRLARVLTGNTIALVLGGGGARGCSHIGVLKALEEAGVPVDLVGGTSIGSFIGALYAEERSASRTKQRAREWAKSMTSVLEPVLDLTYPVTSMFTGSAFNRSIHRVFQDKQIEDLWLPYFNVTTDITASAMRVHKDGSLWRYVRASMTLSGYLPPLCDPKDGHLLMDGGYINNLPADIARSMGAKTVIAIDVGSQDETDLSTYGDSLSGWWLLWKRLNPWADKVKVPDMAEIQSRLAYVSCVRQLEVVKSSSYCEYLRPSIDCFKTMDFGKFDQIYDVGYQYGKAVFGGWTRGEVIEKMLTDRRSTDLNESRRADILAFPSSGFTDLAEIVSRIEPPTSYVSDGCADGEESDCLTEYEEDAGPDCSRDEGGSPEGASPSTASEVEEEKSTLRQRRFLPQETPSSVADA |
| Enzyme Length | 1355 |
| Uniprot Accession Number | Q3TRM4 |
| Absorption | |
| Active Site | ACT_SITE 994; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1114; /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:0000269|PubMed:16963094}. |
| 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:0000269|PubMed:18086666, ECO:0000305|PubMed:16963094};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000269|PubMed:18086666}; 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:0000269|PubMed:18086666};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000269|PubMed:18086666}; 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:0000269|PubMed:18086666};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093; Evidence={ECO:0000269|PubMed:18086666}; 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}; |
| DNA Binding | |
| EC Number | 3.1.1.5 |
| Enzyme Function | FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho) (PubMed:18086666) (Probable). 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 (By similarity). {ECO:0000250|UniProtKB:Q8IY17, ECO:0000269|PubMed:18086666, ECO:0000305|PubMed:16963094}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:18086666}; |
| Pathway | |
| nucleotide Binding | NP_BIND 179..306; /note=cNMP 1; NP_BIND 492..614; /note=cNMP 2; NP_BIND 610..730; /note=cNMP 3 |
| Features | Active site (2); Alternative sequence (4); Chain (1); Compositional bias (1); Domain (1); Glycosylation (1); Modified residue (5); Motif (3); Nucleotide binding (3); Region (2); Sequence conflict (1); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;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:0000269|PubMed:16963094}; Single-pass type III membrane protein {ECO:0000305|PubMed:16963094}. |
| Modified Residue | MOD_RES 338; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8IY17; MOD_RES 345; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q8IY17; MOD_RES 346; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8IY17; MOD_RES 356; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8IY17; MOD_RES 405; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q8IY17 |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11897010; 12466851; 12520002; 12805562; 14681479; 14749382; 15051870; 15094302; 16186328; 17015841; 18799693; 19524041; 19759306; 20112100; 28206686; |
| Motif | MOTIF 965..970; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 992..996; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1114..1116; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 149,537 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15177; RHEA:15178; RHEA:40435; RHEA:40436; RHEA:49092; RHEA:49093; RHEA:40807; RHEA:40808; RHEA:39959; RHEA:39960; RHEA:39963; RHEA:39964; RHEA:38487; RHEA:38488; RHEA:38491; RHEA:38492; RHEA:26132; RHEA:26133 |
| Cross Reference Brenda |